HEADER OXIDOREDUCTASE (CHOH(D)-NAD+(A)) 05-JUN-95 1HYH COMPND Mol_id: 1; COMPND 1 Molecule: L-2-hydroxyisocaproate Dehydrogenase; COMPND 2 Chain: A, B, C, D; COMPND 3 Synonym: L-hicdh; COMPND 4 Ec: 1.1.1.27; COMPND 5 Engineered: Yes; COMPND 6 Heterogen: Nad+; COMPND 7 Heterogen: Sulfate SOURCE Mol_id: 1; SOURCE 1 Organism_scientific: Lactobacillus Confusus; SOURCE 2 Expression_system: Escherichia Coli; SOURCE 3 Expression_system_strain: Jm103; SOURCE 4 Expression_system_plasmid: Phl6; SOURCE 5 Other_details: German Collection Of Microorganisms (Dsm) SOURCE 6 Number Dsm 20196, Cell Plasm KEYWDS L-2-HYDROXYCARBOXYLATE DEHYDROGENASE, L-LACTATE KEYWDS 1 DEHYDROGENASE EXPDTA single-crystal x-ray diffraction AUTHOR K.Niefind,H.-J.Hecht,D.Schomburg JRNL AUTH K.Niefind,H.-J.Hecht,D.Schomburg JRNL TITL Crystal Structure Of L-2-hydroxyisocaproate JRNL TITL 2 Dehydrogenase From Lactobacillus Confusus At 2.2 JRNL TITL 3 Angstroms Resolution - An Example Of Strong JRNL TITL 4 Asymmetry Between Subunits JRNL REF J.MOL.BIOL. V. 251 256 1995 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 REMARK 1 REFERENCE 1 REMARK 1 AUTH I.K.Feil,H.-P.Lerch,D.Schomburg REMARK 1 TITL Deletion Variants Of L-hydroxyisocaproate REMARK 1 TITL 2 Dehydrogenase - Probing Substrate Specificity REMARK 1 REF EUR.J.BIOCHEM. V. 223 857 1994 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.Niefind REMARK 1 TITL Roentgenkristallographische Untersuchungen An Drei REMARK 1 TITL 2 Mikrobiellen Enzymen: REMARK 1 TITL 3 D-2-hydroxyisocaproat-dehydrogenase Aus REMARK 1 TITL 4 Lactobacillus Casei, REMARK 1 TITL 5 L-2-hydroxyisocaproat-dehydrogenase Aus REMARK 1 TITL 6 Lactobacillus Confusus, Alkalische Protease Aus REMARK 1 TITL 7 Bacillus Alcalophilus(Slash)variante Q59r (German, REMARK 1 TITL 8 With English Summary) REMARK 1 REF THESIS, TECHNISCHE 1993 REMARK 1 REF 2 UNIVERSITAT REMARK 1 REF 3 CAROLO-WILHELMINA ZU REMARK 1 REF 4 BRAUNSCHWEIG REMARK 1 PUBL ? REMARK 1 REFN GW 2069 REMARK 1 REFERENCE 3 REMARK 1 AUTH H.-P.Lerch,R.Frank,J.Collins REMARK 1 TITL Cloning, Sequencing And Expression Of The REMARK 1 TITL 2 L-2-hydroxyisocaproate Dehydrogenase-encoding Gene REMARK 1 TITL 3 Of Lactobacillus Confusus In Escherichia Coli REMARK 1 REF GENE V. 83 263 1989 REMARK 1 REFN ASTM GENED6 NE ISSN 0378-1119 0861 REMARK 1 REFERENCE 4 REMARK 1 AUTH H.Schuette,W.Hummel,M.-R.Kula REMARK 1 TITL L-2-hydroxyisocaproate Dehydrogenase - A New Enzyme REMARK 1 TITL 2 From Lactobacillus Confusus For The Stereospecific REMARK 1 TITL 3 Reduction Of 2-ketocarboxylic Acids REMARK 1 REF APPL.MICROBIOL.BIOTECHNOL. V. 19 167 1984 REMARK 1 REFN ASTM AMBIDG GW ISSN 0175-7598 0786 REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ 5.10 IN THE CCP4-SUITE REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.210 REMARK 3 FREE R VALUE 0.250 REMARK 3 FREE R VALUE TEST SET 10.00 % REMARK 3 MEAN B VALUE 27.6 ANGSTROMS**2 REMARK 3 ESD FROM LUZZATI PLOT 0.27 ANGSTROMS REMARK 3 FINAL RMS COORD. SHIFT 0.011 ANGSTROMS REMARK 3 NUMBER OF REFLECTIONS 102618 REMARK 3 RESOLUTION RANGE 8. - 2.2 ANGSTROMS REMARK 3 DATA CUTOFF 2. SIGMA(F) REMARK 3 COMPLETENESS FOR RANGE 93.2 % REMARK 3 DATA COLLECTION. REMARK 3 NUMBER OF UNIQUE REFLECTIONS 105688 REMARK 3 RESOLUTION RANGE 15.1 - 2.22 ANGSTROMS REMARK 3 COMPLETENESS OF DATA 94.9 % REMARK 3 REJECTION CRITERIA 3. SIGMA(I) REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. REMARK 3 NUMBER OF PROTEIN ATOMS 8812 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 REMARK 3 NUMBER OF HETEROGEN ATOMS 196 REMARK 3 NUMBER OF SOLVENT ATOMS 309 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS). REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS). REMARK 3 BOND DISTANCE 0.015(0.015) REMARK 3 ANGLE DISTANCE 0.030(0.020) REMARK 3 PLANAR 1-4 DISTANCE 0.034(0.030) REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.011(0.015) REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.065(0.050) REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS). REMARK 3 SINGLE TORSION CONTACT 0.180(0.200) REMARK 3 MULTIPLE TORSION CONTACT 0.194(0.200) REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES). REMARK 3 PLANAR 2.0 REMARK 3 STAGGERED 15.0 REMARK 3 ORTHONORMAL 33.8 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2). REMARK 3 MAIN-CHAIN BOND 1.260(1.000) REMARK 3 MAIN-CHAIN ANGLE 1.964(1.500) REMARK 3 SIDE-CHAIN BOND 1.383(1.000) REMARK 3 SIDE-CHAIN ANGLE 1.953(1.500) REMARK 3 REMARK: THE DEPOSITORS USED THE FILE "PROTIN_VL.DIC" FROM REMARK 3 THE CCP4-DICTIONARY (VERSION 5.10) TO NUMBER 4 (1994). REMARK 3 ACTA CRYST. D50, 760-763] REMARK 4 REMARK 4 L-HICDH IS A TETRAMER WITH THREE ORTHOGONAL TWO-FOLD AXES. REMARK 4 THE AXIAL SYSTEM OF THIS COORDINATE ENTRY HAS X,Y,Z REMARK 4 COINCIDENT WITH THE P,Q,R SET CUSTOMARILY USED FOR MEMBERS REMARK 4 OF THE L-LACTATE DEHYDROGENASE FAMILY AND DEFINED BY REMARK 4 M.G.ROSSMANN ET AL. IN J.MOL.BIOL,V.76 533 1973. REMARK 5 REMARK 5 NO NON-CRYSTALLOGRAPHIC SYMMETRY RESTRAINTS WERE APPLIED REMARK 5 IN THE FINAL REFINEMENT. REMARK 6 REMARK 6 FOUR L-HICDH SUBUNITS ARE INCLUDED. EACH SUBUNIT HAS NAD+ REMARK 6 AND A SULFATE ION IN THE ACTIVE SITE. REMARK 7 REMARK 7 RESIDUES ARE NUMBERED SEQUENTIALLY STARTING WITH ALA 21 AND REMARK 7 ENDING WITH LEU 329. THE REASON FOR BEGINNING WITH 21 REMARK 7 IS THAT L-HICDH MISSES AN N-TERMINAL ARM OF ABOUT 20 REMARK 7 RESIDUES, WHICH IS PRESENT IN HOMOLOGOUS EUKARYOTIC REMARK 7 L-LACTATE DEHYDROGENASES. REMARK 8 REMARK 8 THE *SCALE* TRANSFORMATION BELOW GENERATES FRACTIONAL. REMARK 8 COORDINATES WITH RESPECT TO SPACE GROUP P 32 2 1. REMARK 9 REMARK 9 NON-CRYSTALLOGRAPHIC SYMMETRY IS WELL PRESERVED AROUND REMARK 9 THE MOLECULAR P-AXIS, WHILE IT IS STRONGLY DISTURBED AROUND REMARK 9 Q AND R. STRUCTURAL DIFFERENCES BETWEEN THE CHAINS *A* AND REMARK 9 *B* ON THE ONE SIDE AND *C* AND *D* ON THE OTHER ARE REMARK 9 ESPECIALLY PRONOUNCED IN THE REGION OF THE ACTIVE SITE. REMARK 10 REMARK 10 MTRIX REMARK 10 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW REMARK 10 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE REMARK 10 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE REMARK 10 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL REMARK 10 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED REMARK 10 SECOND. REMARK 10 APPLIED TO TRANSFORMED TO REMARK 10 MTRIX RESIDUES RESIDUES RMSD REMARK 10 M1 A 21 .. A 331 B 21 .. B 331 0.244 REMARK 10 M2 A 21 .. A 331 C 21 .. C 331 5.043 REMARK 10 M3 A 21 .. A 331 D 21 .. D 331 5.041 REMARK 10 THE FIRST MTRIX-OPERATION DESCRIBES THE TWO-FOLD REMARK 10 ROTATION AROUND THE MOLECULAR P-AXIS AND MAPS CHAIN *A* REMARK 10 ON CHAIN *B* (INCLUDING THE BOUND NAD+ AND SULFATE, REMARK 10 RESPECTIVELY). REMARK 10 THE SECOND MTRIX-OPERATION DESCRIBES THE TWO-FOLD REMARK 10 ROTATION AROUND THE MOLECULAR Q-AXIS AND MAPS CHAIN *A* REMARK 10 ON CHAIN *C* (INCLUDING THE BOUND NAD+ AND SULFATE, REMARK 10 RESPECTIVELY). REMARK 10 THE THIRD MTRIX-OPERATION DESCRIBES THE TWO-FOLD REMARK 10 ROTATION AROUND THE MOLECULAR R-AXIS AND MAPS CHAIN *A* REMARK 10 ON CHAIN *D* (INCLUDING THE BOUND NAD+ AND SULFATE, REMARK 10 RESPECTIVELY). REMARK 11 REMARK 11 ATOMS OG SER A 255 AND OG SER B 255 ARE PRESENTED WITH REMARK 11 ALTERNATE SIDE CHAIN CONFORMATIONS. REMARK 12 REMARK 12 SOURCE: REMARK 12 DSM NUMBER: DSM 20196 (DSM = DEUTSCHE SAMMLUNG VON REMARK 12 MIKROORGANISMEN/GERMAN COLLECTION OF MICROORGANISMS) REMARK 13 REMARK 13 THE FOLLOWING PARTS OF THE MOLECULE ARE NOT INCLUDED IN REMARK 13 THIS ENTRY, BECAUSE THEY ARE NOT DEFINED BY ELECTRON REMARK 13 DENSITY: REMARK 13 SUBUNIT A: REMARK 13 COMPLETELY MISSING: ASP 105 - ARG 111, ALA 220 - ASP 224 REMARK 13 PARTLY MISSING: LYS 101, ILE 225, ASP 226, ARG 235, REMARK 13 GLU 309, GLN 313, ASP 327 REMARK 13 SUBUNIT B: REMARK 13 COMPLETELY MISSING: ASP 105 - ARG 111, ALA 220 - ASP 224, REMARK 13 ASP 327 - LEU 329 REMARK 13 PARTLY MISSING: LYS 101, LYS 116, ILE 225, ASP 226, REMARK 13 ARG 235, GLU 309, GLN 320, ARG 321, REMARK 13 VAL 326 REMARK 13 SUBUNIT C: REMARK 13 COMPLETELY MISSING: ASN 99 - THR 108, GLY 223 - ASP 224 REMARK 13 PARTLY MISSING: ASP 110, GLU 114, GLU 232, ARG 235, REMARK 13 LYS 236, ARG 321 REMARK 13 SUBUNIT D: REMARK 13 COMPLETELY MISSING: ASN 99 - THR 108, GLY 223 - ASP 224 REMARK 13 PARTLY MISSING: ASN 200, GLU 232, ARG 235, LYS 236, REMARK 13 GLU 309, GLN 320, ARG 321 REMARK 14 REMARK 14 THE RESIDUES BEHIND THE STRUCTURAL GAPS SPECIFIED IN REMARK REMARK 14 13 CONTAIN SOME BOND ANGLES WITH LARGE DISTORTIONS FROM REMARK 14 STANDARD GEOMETRY AND SHOULD BE LEFT OUT IN STRUCTURAL REMARK 14 STUDIES. THESE RESIDUES ARE: REMARK 14 SUBUNIT A: PHE 112, ILE 225 REMARK 14 SUBUNIT B: PHE 112, ILE 225 REMARK 14 SUBUNIT C: GLY 109, ILE 225 REMARK 14 SUBUNIT D: GLY 109, ILE 225 REMARK 15 REMARK 15 STRUCTURE FACTORS CORRESPONDING TO THIS ENTRY HAVE BEEN REMARK 15 DEPOSITED WITH THE PROTEIN DATA BANK. REMARK 18 REMARK 18 EXPERIMENTAL DETAILS. REMARK 18 DATE OF DATA COLLECTION : 30-NOV-93 REMARK 18 SOURCE : DESY REMARK 18 BEAMLINE : BW6 REMARK 18 MONOCHROMATIC (Y/N) : Y REMARK 18 LAUE (Y/N) : N REMARK 18 WAVELENGTH OR RANGE (A) : 1.0 REMARK 18 DETECTOR TYPE : IMAGE PLATE (300MM) REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH REMARK 18 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 18 DATA REDUNDANCY : 3.5 REMARK 18 MERGING R VALUE (INTENSITY) : 0.076 REMARK 19 REMARK 19 SOLVENT CONTENT (VS) : 70.4 % REMARK 19 MATTHEWS COEFFICIENT (VM) : 4.15 ANGSTROMS**3/DA REMARK 999 REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME REMARK 999 DHL2_LACCO A REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME REMARK 999 DHL2_LACCO B REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME REMARK 999 DHL2_LACCO C REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME REMARK 999 DHL2_LACCO D REMARK 999 SEQUENCE REMARK 999 REFERENCE REMARK 999 DATABASE: SWISS-PROT, RELEASE 31.0 (3/95) REMARK 999 ENTRY_NAME: DHL2_LACCO; P14295 REMARK 999 REFERENCE: H.-P. LERCH, R. FRANK, J. COLLINS (1989). REMARK 999 CLONING, SEQUENCING, EXPRESSION OF THE REMARK 999 L-2-HYDROXYISOCAPROATE DEHYDROGENASE-ENCODING GENE OF REMARK 999 LACTOBACILLUS CONFUSUS IN ESCHERICHIA COLI. GENE, 83, REMARK 999 263-270. REMARK 960 REMARK 960 EMBEDDED CIF REMARK 960 REMARK 960 ################################################### REMARK 960 # # REMARK 960 # Converted from PDB format to CIF format by # REMARK 960 # pdb2cif version 2.3.6 15 Jun 98 # REMARK 960 # by # REMARK 960 # P.E. Bourne, H.J. Bernstein and F.C. Bernstein # REMARK 960 # # REMARK 960 # *** See the remarks at the end of this *** # REMARK 960 # *** file for information on conversion *** # REMARK 960 # *** of this entry and on the program *** # REMARK 960 # *** pdb2cif *** # REMARK 960 ################################################### REMARK 960 REMARK 960 REMARK 960 data_1HYH REMARK 960 REMARK 960 _entry.id 1HYH REMARK 960 REMARK 960 REMARK 960 REMARK 960 ################## REMARK 960 # # REMARK 960 # STRUCT # REMARK 960 # # REMARK 960 ################## REMARK 960 REMARK 960 loop_ REMARK 960 _struct.entry_id REMARK 960 1HYH REMARK 960 _struct.title ' Compound::' REMARK 960 _exptl.method REMARK 960 'single-crystal x-ray diffraction' REMARK 960 REMARK 960 REMARK 960 REMARK 960 #################### REMARK 960 # # REMARK 960 # AUDIT_AUTHOR # REMARK 960 # # REMARK 960 #################### REMARK 960 REMARK 960 REMARK 960 _audit_author.name .0 REMARK 960 #< not correct type REMARK 960 _citation.id primary REMARK 960 _citation.page_first .0 REMARK 960 #< not correct type REMARK 960 _citation.year ? REMARK 960 _symmetry.entry_id 1HYH REMARK 960 _audit.revision_id 1HYH REMARK 960 _audit.creation_date 1995-06-05 REMARK 960 ; REMARK 960 1998-06-15 Converted to mmCIF format by pdb2cif.pl 2.3.6 REMARK 960 ; REMARK 960 REMARK 960 REMARK 960 ############################# REMARK 960 # # REMARK 960 # STRUCT_KEYWORDS # REMARK 960 # # REMARK 960 ############################# REMARK 960 REMARK 960 loop_ REMARK 960 _struct_keywords.entry_id REMARK 960 _entity_poly_seq.entity_id REMARK 960 1 REMARK 960 ; REMARK 960 Protein chain: A, B, C, D REMARK 960 ; REMARK 960 5 'het group NAD' REMARK 960 6 'het group SO4' REMARK 960 7 HOH REMARK 960 REMARK 960 loop_ REMARK 960 _struct_asym.entity_id REMARK 960 _chem_comp.id REMARK 960 _chem_comp.mon_nstd_flag REMARK 960 NAD REMARK 960 ; REMARK 960 4(C21 H27 N7 O14 P2) REMARK 960 ; REMARK 960 ; REMARK 960 NICOTINAMIDE-ADENINE-DINUCLEOTIDE REMARK 960 ; REMARK 960 SO4 REMARK 960 ; REMARK 960 4(O4 S1 2-) REMARK 960 ; REMARK 960 ; REMARK 960 SULFATE ION REMARK 960 ; REMARK 960 HOH REMARK 960 ; REMARK 960 309(H2 O1) REMARK 960 ; REMARK 960 ; REMARK 960 ; REMARK 960 ALA 'C3 H7 N1 O2' Alanine REMARK 960 ARG 'C6 H14 N4 O2' Arginine REMARK 960 ASN 'C4 H8 N2 O3' Asparagine REMARK 960 ASP 'C4 H7 N1 O4' 'Aspartic acid' REMARK 960 GLN 'C5 H10 N2 O3' Glutamine REMARK 960 GLU 'C5 H9 N1 O4' 'Glutamic acid' REMARK 960 GLY 'C2 H5 N1 O2' Glycine REMARK 960 HIS 'C6 H9 N3 O2' Histidine REMARK 960 ILE 'C6 H13 N1 O2' Isoleucine REMARK 960 LEU 'C6 H13 N1 O2' Leucine REMARK 960 LYS 'C6 H14 N2 O2' Lysine REMARK 960 MET 'C5 H11 N1 O2 S1' REMARK 960 Methionine REMARK 960 PHE 'C9 H11 N1 O2' Phenylalanine REMARK 960 PRO 'C5 H9 N1 O2' Proline REMARK 960 SER 'C3 H7 N1 O3' Serine REMARK 960 THR 'C4 H9 N1 O3' Threonine REMARK 960 TRP 'C11 H12 N2 O2' Tryptophan REMARK 960 TYR 'C9 H11 N1 O3' Tyrosine REMARK 960 VAL 'C5 H11 N1 O2' V aline REMARK 960 REMARK 960 REMARK 960 REMARK 960 ###################### REMARK 960 # # REMARK 960 # ATOM_SITES # REMARK 960 # # REMARK 960 ###################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _database_PDB_matrix.entry_id REMARK 960 1HYH REMARK 960 REMARK 960 loop_ REMARK 960 _database_PDB_matrix.origx[1][1] REMARK 960 _database_PDB_matrix.origx[1][2] REMARK 960 1HYH REMARK 960 'See _atom_sites.fract_transf_matrix[i][j]' REMARK 960 REMARK 960 loop_ REMARK 960 _atom_sites.fract_transf_matrix[1][1] REMARK 960 _atom_sites.fract_transf_matrix[1][2] REMARK 960 _atom_sites.fract_transf_matrix[1][3] REMARK 960 _atom_sites.fract_transf_vector[1] REMARK 960 _atom_sites.fract_transf_matrix[2][1] REMARK 960 _atom_sites.fract_transf_matrix[2][2] REMARK 960 _atom_sites.fract_transf_matrix[2][3] REMARK 960 _atom_sites.fract_transf_vector[2] REMARK 960 _atom_sites.fract_transf_matrix[3][1] REMARK 960 _atom_sites.fract_transf_matrix[3][2] REMARK 960 _atom_sites.fract_transf_matrix[3][3] REMARK 960 _atom_sites.fract_transf_vector[3] REMARK 960 _struct_ncs_oper.id REMARK 960 _struct_ncs_oper.code REMARK 960 1 given REMARK 960 0.999990 -0.003090 0.002180 0.00903 REMARK 960 -0.003090 -0.999990 -0.001610 0.01442 REMARK 960 0.002190 0.001600 -1.000000 -0.05906 REMARK 960 2 given REMARK 960 -0.999980 0.002870 -0.005370 0.00929 REMARK 960 0.002910 0.999970 -0.006560 0.21671 REMARK 960 0.005350 -0.006570 -0.999960 -0.06222 REMARK 960 3 given REMARK 960 -1.000000 -0.000110 -0.002370 0.00131 REMARK 960 0.000100 -0.999980 0.006730 -0.22078 REMARK 960 -0.002370 0.006730 0.999970 0.03004 REMARK 960 REMARK 960 REMARK 960 REMARK 960 #################### REMARK 960 # # REMARK 960 # ATOM_SITES_ALT # REMARK 960 # # REMARK 960 #################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _atom_sites_alt.id REMARK 960 _atom_sites_alt.details REMARK 960 A ? REMARK 960 B ? REMARK 960 REMARK 960 REMARK 960 REMARK 960 ###################### REMARK 960 # # REMARK 960 # ATOM_SITES_FOOTNOTE# REMARK 960 # # REMARK 960 ###################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _atom_sites_footnote.id REMARK 960 _atom_sites_footnote.text REMARK 960 1 REMARK 960 ; REMARK 960 CIS PROLINE - PRO A 144 REMARK 960 ; REMARK 960 2 REMARK 960 ; REMARK 960 CIS PROLINE - PRO B 144 REMARK 960 ; REMARK 960 3 REMARK 960 ; REMARK 960 CIS PROLINE - PRO C 144 REMARK 960 ; REMARK 960 4 REMARK 960 ; REMARK 960 CIS PROLINE - PRO D 144 REMARK 960 ; REMARK 960 REMARK 960 REMARK 960 REMARK 960 #################### REMARK 960 # # REMARK 960 # ATOM_SITE # REMARK 960 # # REMARK 960 #################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 _atom_site.label_seq_id '1 ' REMARK 960 loop_ REMARK 960 _atom_site.label_atom_id REMARK 960 _atom_site.label_comp_id REMARK 960 _atom_site.label_asym_id REMARK 960 _atom_site.auth_seq_id REMARK 960 _atom_site.label_alt_id REMARK 960 _atom_site.Cartn_x REMARK 960 1 1995-10-15 REMARK 960 0 . . . REMARK 960 REMARK 960 REMARK 960 REMARK 960 #################### REMARK 960 # # REMARK 960 # STRUCT_BIOL # REMARK 960 # # REMARK 960 #################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_biol.id REMARK 960 1HYH REMARK 960 A REMARK 960 B REMARK 960 C REMARK 960 D REMARK 960 loop_ REMARK 960 _struct_biol.details REMARK 960 _struct_biol_gen.biol_id REMARK 960 _struct_biol_gen.asym_id REMARK 960 _struct_biol_gen.symmetry REMARK 960 1HYH A 1_555 . REMARK 960 1HYH B 1_555 . REMARK 960 1HYH C 1_555 . REMARK 960 1HYH D 1_555 . REMARK 960 1HYH NAD 1_555 . REMARK 960 1HYH SO4 1_555 . REMARK 960 1HYH HOH 1_555 . REMARK 960 A A 1_555 . REMARK 960 B B 1_555 . REMARK 960 C C 1_555 . REMARK 960 D D 1_555 . REMARK 960 REMARK 960 REMARK 960 REMARK 960 ############################## REMARK 960 # # REMARK 960 # STRUCT_CONN_TYPE # REMARK 960 # # REMARK 960 ############################## REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_conn_type.id REMARK 960 _struct_conn_type.criteria REMARK 960 _struct_conn_type.reference REMARK 960 . 'unknown bond type from PDB entry' ? REMARK 960 saltbr 'salt bridge from PDB entry' ? REMARK 960 hydrog 'hydrogen bond from PDB entry' ? REMARK 960 REMARK 960 REMARK 960 REMARK 960 ############################## REMARK 960 # # REMARK 960 # STRUCT_CONN # REMARK 960 # # REMARK 960 ############################## REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_conn.id REMARK 960 _struct_conn.conn_type_id REMARK 960 _struct_conn.ptnr1_label_comp_id REMARK 960 _struct_conn.ptnr1_label_asym_id REMARK 960 _struct_conn.ptnr1_auth_seq_id REMARK 960 _struct_conn.ptnr1_label_atom_id REMARK 960 _struct_conn.ptnr1_label_alt_id REMARK 960 _struct_conn.ptnr1_role REMARK 960 _struct_conn.ptnr1_symmetry REMARK 960 _struct_conn.ptnr2_label_comp_id REMARK 960 _struct_conn.ptnr2_label_asym_id REMARK 960 _struct_conn.ptnr2_auth_seq_id REMARK 960 _struct_conn.ptnr2_label_atom_id REMARK 960 _struct_conn.ptnr2_label_alt_id REMARK 960 _struct_conn.ptnr2_role REMARK 960 _struct_conn.ptnr2_symmetry REMARK 960 _struct_conn.ptnr1_atom_site_id REMARK 960 #< not in dictionary REMARK 960 _struct_conn.ptnr1_label_seq_id REMARK 960 _struct_conn.ptnr2_atom_site_id REMARK 960 #< not in dictionary REMARK 960 _struct_conn.ptnr2_label_seq_id REMARK 960 1 . NAD A 330 AO1 . . . NAD A 330 AP REMARK 960 . . . REMARK 960 2220 . 2219 . REMARK 960 2 . NAD A 330 AO2 . . . NAD A 330 AP REMARK 960 . . . REMARK 960 2221 . 2219 . REMARK 960 3 . NAD A 330 AO5* . . . NAD A 330 AP REMARK 960 . . . REMARK 960 2222 . 2219 . REMARK 960 4 . NAD A 330 O3 . . . NAD A 330 AP REMARK 960 . . . REMARK 960 2241 . 2219 . REMARK 960 5 . NAD A 330 AC5* . . . NAD A 330 AO5* REMARK 960 . . . REMARK 960 2223 . 2222 . REMARK 960 6 . NAD A 330 AC4* . . . NAD A 330 AC5* REMARK 960 . . . REMARK 960 2224 . 2223 . REMARK 960 7 . NAD A 330 AC4* . . . NAD A 330 AO4* REMARK 960 . . . REMARK 960 2224 . 2225 . REMARK 960 8 . NAD A 330 AC3* . . . NAD A 330 AC4* REMARK 960 . . . REMARK 960 2226 . 2224 . REMARK 960 9 . NAD A 330 AC1* . . . NAD A 330 AO4* REMARK 960 . . . REMARK 960 2230 . 2225 . REMARK 960 10 . NAD A 330 AC3* . . . NAD A 330 AO3* REMARK 960 . . . REMARK 960 2226 . 2227 . REMARK 960 11 . NAD A 330 AC2* . . . NAD A 330 AC3* REMARK 960 . . . REMARK 960 2228 . 2226 . REMARK 960 12 . NAD A 330 AC2* . . . NAD A 330 AO2* REMARK 960 . . . REMARK 960 2228 . 2229 . REMARK 960 13 . NAD A 330 AC1* . . . NAD A 330 AC2* REMARK 960 . . . REMARK 960 2230 . 2228 . REMARK 960 14 . NAD A 330 AC1* . . . NAD A 330 AN9 REMARK 960 . . . REMARK 960 2230 . 2231 . REMARK 960 15 . NAD A 330 AC8 . . . NAD A 330 AN9 REMARK 960 . . . REMARK 960 2232 . 2231 . REMARK 960 16 . NAD A 330 AC4 . . . NAD A 330 AN9 REMARK 960 . . . REMARK 960 2240 . 2231 . REMARK 960 17 . NAD A 330 AC8 . . . NAD A 330 AN7 REMARK 960 . . . REMARK 960 2232 . 2233 . REMARK 960 18 . NAD A 330 AC5 . . . NAD A 330 AN7 REMARK 960 . . . REMARK 960 2234 . 2233 . REMARK 960 19 . NAD A 330 AC5 . . . NAD A 330 AC6 REMARK 960 . . . REMARK 960 2234 . 2235 . REMARK 960 20 . NAD A 330 AC4 . . . NAD A 330 AC5 REMARK 960 . . . REMARK 960 2240 . 2234 . REMARK 960 21 . NAD A 330 AC6 . . . NAD A 330 AN6 REMARK 960 . . . REMARK 960 2235 . 2236 . REMARK 960 22 . NAD A 330 AC6 . . . NAD A 330 AN1 REMARK 960 . . . REMARK 960 2235 . 2237 . REMARK 960 23 . NAD A 330 AC2 . . . NAD A 330 AN1 REMARK 960 . . . REMARK 960 2238 . 2237 . REMARK 960 24 . NAD A 330 AC2 . . . NAD A 330 AN3 REMARK 960 . . . REMARK 960 2238 . 2239 . REMARK 960 25 . NAD A 330 AC4 . . . NAD A 330 AN3 REMARK 960 . . . REMARK 960 2240 . 2239 . REMARK 960 26 . NAD A 330 O3 . . . NAD A 330 NP REMARK 960 . . . REMARK 960 2241 . 2242 . REMARK 960 27 . NAD A 330 NO1 . . . NAD A 330 NP REMARK 960 . . . REMARK 960 2243 . 2242 . REMARK 960 28 . NAD A 330 NO2 . . . NAD A 330 NP REMARK 960 . . . REMARK 960 2244 . 2242 . REMARK 960 29 . NAD A 330 NO5* . . . NAD A 330 NP REMARK 960 . . . REMARK 960 2245 . 2242 . REMARK 960 30 . NAD A 330 NC5* . . . NAD A 330 NO5* REMARK 960 . . . REMARK 960 2246 . 2245 . REMARK 960 31 . NAD A 330 NC4* . . . NAD A 330 NC5* REMARK 960 . . . REMARK 960 2247 . 2246 . REMARK 960 32 . NAD A 330 NC4* . . . NAD A 330 NO4* REMARK 960 . . . REMARK 960 2247 . 2248 . REMARK 960 33 . NAD A 330 NC3* . . . NAD A 330 NC4* REMARK 960 . . . REMARK 960 2249 . 2247 . REMARK 960 34 . NAD A 330 NC1* . . . NAD A 330 NO4* REMARK 960 . . . REMARK 960 2253 . 2248 . REMARK 960 35 . NAD A 330 NC3* . . . NAD A 330 NO3* REMARK 960 . . . REMARK 960 2249 . 2250 . REMARK 960 36 . NAD A 330 NC2* . . . NAD A 330 NC3* REMARK 960 . . . REMARK 960 2251 . 2249 . REMARK 960 37 . NAD A 330 NC2* . . . NAD A 330 NO2* REMARK 960 . . . REMARK 960 2251 . 2252 . REMARK 960 38 . NAD A 330 NC1* . . . NAD A 330 NC2* REMARK 960 . . . REMARK 960 2253 . 2251 . REMARK 960 39 . NAD A 330 NC1* . . . NAD A 330 NN1 REMARK 960 . . . REMARK 960 2253 . 2254 . REMARK 960 40 . NAD A 330 NC2 . . . NAD A 330 NN1 REMARK 960 . . . REMARK 960 2255 . 2254 . REMARK 960 41 . NAD A 330 NC6 . . . NAD A 330 NN1 REMARK 960 . . . REMARK 960 2262 . 2254 . REMARK 960 42 . NAD A 330 NC2 . . . NAD A 330 NC3 REMARK 960 . . . REMARK 960 2255 . 2256 . REMARK 960 43 . NAD A 330 NC3 . . . NAD A 330 NC7 REMARK 960 . . . REMARK 960 2256 . 2257 . REMARK 960 44 . NAD A 330 NC3 . . . NAD A 330 NC4 REMARK 960 . . . REMARK 960 2256 . 2260 . REMARK 960 45 . NAD A 330 NC7 . . . NAD A 330 NO7 REMARK 960 . . . REMARK 960 2257 . 2258 . REMARK 960 46 . NAD A 330 NC7 . . . NAD A 330 NN7 REMARK 960 . . . REMARK 960 2257 . 2259 . REMARK 960 47 . NAD A 330 NC4 . . . NAD A 330 NC5 REMARK 960 . . . REMARK 960 2260 . 2261 . REMARK 960 48 . NAD A 330 NC5 . . . NAD A 330 NC6 REMARK 960 . . . REMARK 960 2261 . 2262 . REMARK 960 49 . SO4 A 331 O1 . . . SO4 A 331 S REMARK 960 . . . REMARK 960 2264 . 2263 . REMARK 960 50 . SO4 A 331 O2 . . . SO4 A 331 S REMARK 960 . . . REMARK 960 2265 . 2263 . REMARK 960 51 . SO4 A 331 O3 . . . SO4 A 331 S REMARK 960 . . . REMARK 960 2266 . 2263 . REMARK 960 52 . SO4 A 331 O4 . . . SO4 A 331 S REMARK 960 . . . REMARK 960 2267 . 2263 . REMARK 960 53 . NAD B 330 AO1 . . . NAD B 330 AP REMARK 960 . . . REMARK 960 4540 . 4539 . REMARK 960 54 . NAD B 330 AO2 . . . NAD B 330 AP REMARK 960 . . . REMARK 960 4541 . 4539 . REMARK 960 55 . NAD B 330 AO5* . . . NAD B 330 AP REMARK 960 . . . REMARK 960 4542 . 4539 . REMARK 960 56 . NAD B 330 O3 . . . NAD B 330 AP REMARK 960 . . . REMARK 960 4561 . 4539 . REMARK 960 57 . NAD B 330 AC5* . . . NAD B 330 AO5* REMARK 960 . . . REMARK 960 4543 . 4542 . REMARK 960 58 . NAD B 330 AC4* . . . NAD B 330 AC5* REMARK 960 . . . REMARK 960 4544 . 4543 . REMARK 960 59 . NAD B 330 AC4* . . . NAD B 330 AO4* REMARK 960 . . . REMARK 960 4544 . 4545 . REMARK 960 60 . NAD B 330 AC3* . . . NAD B 330 AC4* REMARK 960 . . . REMARK 960 4546 . 4544 . REMARK 960 61 . NAD B 330 AC1* . . . NAD B 330 AO4* REMARK 960 . . . REMARK 960 4550 . 4545 . REMARK 960 62 . NAD B 330 AC3* . . . NAD B 330 AO3* REMARK 960 . . . REMARK 960 4546 . 4547 . REMARK 960 63 . NAD B 330 AC2* . . . NAD B 330 AC3* REMARK 960 . . . REMARK 960 4548 . 4546 . REMARK 960 64 . NAD B 330 AC2* . . . NAD B 330 AO2* REMARK 960 . . . REMARK 960 4548 . 4549 . REMARK 960 65 . NAD B 330 AC1* . . . NAD B 330 AC2* REMARK 960 . . . REMARK 960 4550 . 4548 . REMARK 960 66 . NAD B 330 AC1* . . . NAD B 330 AN9 REMARK 960 . . . REMARK 960 4550 . 4551 . REMARK 960 67 . NAD B 330 AC8 . . . NAD B 330 AN9 REMARK 960 . . . REMARK 960 4552 . 4551 . REMARK 960 68 . NAD B 330 AC4 . . . NAD B 330 AN9 REMARK 960 . . . REMARK 960 4560 . 4551 . REMARK 960 69 . NAD B 330 AC8 . . . NAD B 330 AN7 REMARK 960 . . . REMARK 960 4552 . 4553 . REMARK 960 70 . NAD B 330 AC5 . . . NAD B 330 AN7 REMARK 960 . . . REMARK 960 4554 . 4553 . REMARK 960 71 . NAD B 330 AC5 . . . NAD B 330 AC6 REMARK 960 . . . REMARK 960 4554 . 4555 . REMARK 960 72 . NAD B 330 AC4 . . . NAD B 330 AC5 REMARK 960 . . . REMARK 960 4560 . 4554 . REMARK 960 73 . NAD B 330 AC6 . . . NAD B 330 AN6 REMARK 960 . . . REMARK 960 4555 . 4556 . REMARK 960 74 . NAD B 330 AC6 . . . NAD B 330 AN1 REMARK 960 . . . REMARK 960 4555 . 4557 . REMARK 960 75 . NAD B 330 AC2 . . . NAD B 330 AN1 REMARK 960 . . . REMARK 960 4558 . 4557 . REMARK 960 76 . NAD B 330 AC2 . . . NAD B 330 AN3 REMARK 960 . . . REMARK 960 4558 . 4559 . REMARK 960 77 . NAD B 330 AC4 . . . NAD B 330 AN3 REMARK 960 . . . REMARK 960 4560 . 4559 . REMARK 960 78 . NAD B 330 O3 . . . NAD B 330 NP REMARK 960 . . . REMARK 960 4561 . 4562 . REMARK 960 79 . NAD B 330 NO1 . . . NAD B 330 NP REMARK 960 . . . REMARK 960 4563 . 4562 . REMARK 960 80 . NAD B 330 NO2 . . . NAD B 330 NP REMARK 960 . . . REMARK 960 4564 . 4562 . REMARK 960 81 . NAD B 330 NO5* . . . NAD B 330 NP REMARK 960 . . . REMARK 960 4565 . 4562 . REMARK 960 82 . NAD B 330 NC5* . . . NAD B 330 NO5* REMARK 960 . . . REMARK 960 4566 . 4565 . REMARK 960 83 . NAD B 330 NC4* . . . NAD B 330 NC5* REMARK 960 . . . REMARK 960 4567 . 4566 . REMARK 960 84 . NAD B 330 NC4* . . . NAD B 330 NO4* REMARK 960 . . . REMARK 960 4567 . 4568 . REMARK 960 85 . NAD B 330 NC3* . . . NAD B 330 NC4* REMARK 960 . . . REMARK 960 4569 . 4567 . REMARK 960 86 . NAD B 330 NC1* . . . NAD B 330 NO4* REMARK 960 . . . REMARK 960 4573 . 4568 . REMARK 960 87 . NAD B 330 NC3* . . . NAD B 330 NO3* REMARK 960 . . . REMARK 960 4569 . 4570 . REMARK 960 88 . NAD B 330 NC2* . . . NAD B 330 NC3* REMARK 960 . . . REMARK 960 4571 . 4569 . REMARK 960 89 . NAD B 330 NC2* . . . NAD B 330 NO2* REMARK 960 . . . REMARK 960 4571 . 4572 . REMARK 960 90 . NAD B 330 NC1* . . . NAD B 330 NC2* REMARK 960 . . . REMARK 960 4573 . 4571 . REMARK 960 91 . NAD B 330 NC1* . . . NAD B 330 NN1 REMARK 960 . . . REMARK 960 4573 . 4574 . REMARK 960 92 . NAD B 330 NC2 . . . NAD B 330 NN1 REMARK 960 . . . REMARK 960 4575 . 4574 . REMARK 960 93 . NAD B 330 NC6 . . . NAD B 330 NN1 REMARK 960 . . . REMARK 960 4582 . 4574 . REMARK 960 94 . NAD B 330 NC2 . . . NAD B 330 NC3 REMARK 960 . . . REMARK 960 4575 . 4576 . REMARK 960 95 . NAD B 330 NC3 . . . NAD B 330 NC7 REMARK 960 . . . REMARK 960 4576 . 4577 . REMARK 960 96 . NAD B 330 NC3 . . . NAD B 330 NC4 REMARK 960 . . . REMARK 960 4576 . 4580 . REMARK 960 97 . NAD B 330 NC7 . . . NAD B 330 NO7 REMARK 960 . . . REMARK 960 4577 . 4578 . REMARK 960 98 . NAD B 330 NC7 . . . NAD B 330 NN7 REMARK 960 . . . REMARK 960 4577 . 4579 . REMARK 960 99 . NAD B 330 NC4 . . . NAD B 330 NC5 REMARK 960 . . . REMARK 960 4580 . 4581 . REMARK 960 100 . NAD B 330 NC5 . . . NAD B 330 NC6 REMARK 960 . . . REMARK 960 4581 . 4582 . REMARK 960 101 . SO4 B 331 O1 . . . SO4 B 331 S REMARK 960 . . . REMARK 960 4584 . 4583 . REMARK 960 102 . SO4 B 331 O2 . . . SO4 B 331 S REMARK 960 . . . REMARK 960 4585 . 4583 . REMARK 960 103 . SO4 B 331 O3 . . . SO4 B 331 S REMARK 960 . . . REMARK 960 4586 . 4583 . REMARK 960 104 . SO4 B 331 O4 . . . SO4 B 331 S REMARK 960 . . . REMARK 960 4587 . 4583 . REMARK 960 105 . NAD C 330 AO1 . . . NAD C 330 AP REMARK 960 . . . REMARK 960 6863 . 6862 . REMARK 960 106 . NAD C 330 AO2 . . . NAD C 330 AP REMARK 960 . . . REMARK 960 6864 . 6862 . REMARK 960 107 . NAD C 330 AO5* . . . NAD C 330 AP REMARK 960 . . . REMARK 960 6865 . 6862 . REMARK 960 108 . NAD C 330 O3 . . . NAD C 330 AP REMARK 960 . . . REMARK 960 6884 . 6862 . REMARK 960 109 . NAD C 330 AC5* . . . NAD C 330 AO5* REMARK 960 . . . REMARK 960 6866 . 6865 . REMARK 960 110 . NAD C 330 AC4* . . . NAD C 330 AC5* REMARK 960 . . . REMARK 960 6867 . 6866 . REMARK 960 111 . NAD C 330 AC4* . . . NAD C 330 AO4* REMARK 960 . . . REMARK 960 6867 . 6868 . REMARK 960 112 . NAD C 330 AC3* . . . NAD C 330 AC4* REMARK 960 . . . REMARK 960 6869 . 6867 . REMARK 960 113 . NAD C 330 AC1* . . . NAD C 330 AO4* REMARK 960 . . . REMARK 960 6873 . 6868 . REMARK 960 114 . NAD C 330 AC3* . . . NAD C 330 AO3* REMARK 960 . . . REMARK 960 6869 . 6870 . REMARK 960 115 . NAD C 330 AC2* . . . NAD C 330 AC3* REMARK 960 . . . REMARK 960 6871 . 6869 . REMARK 960 116 . NAD C 330 AC2* . . . NAD C 330 AO2* REMARK 960 . . . REMARK 960 6871 . 6872 . REMARK 960 117 . NAD C 330 AC1* . . . NAD C 330 AC2* REMARK 960 . . . REMARK 960 6873 . 6871 . REMARK 960 118 . NAD C 330 AC1* . . . NAD C 330 AN9 REMARK 960 . . . REMARK 960 6873 . 6874 . REMARK 960 119 . NAD C 330 AC8 . . . NAD C 330 AN9 REMARK 960 . . . REMARK 960 6875 . 6874 . REMARK 960 120 . NAD C 330 AC4 . . . NAD C 330 AN9 REMARK 960 . . . REMARK 960 6883 . 6874 . REMARK 960 121 . NAD C 330 AC8 . . . NAD C 330 AN7 REMARK 960 . . . REMARK 960 6875 . 6876 . REMARK 960 122 . NAD C 330 AC5 . . . NAD C 330 AN7 REMARK 960 . . . REMARK 960 6877 . 6876 . REMARK 960 123 . NAD C 330 AC5 . . . NAD C 330 AC6 REMARK 960 . . . REMARK 960 6877 . 6878 . REMARK 960 124 . NAD C 330 AC4 . . . NAD C 330 AC5 REMARK 960 . . . REMARK 960 6883 . 6877 . REMARK 960 125 . NAD C 330 AC6 . . . NAD C 330 AN6 REMARK 960 . . . REMARK 960 6878 . 6879 . REMARK 960 126 . NAD C 330 AC6 . . . NAD C 330 AN1 REMARK 960 . . . REMARK 960 6878 . 6880 . REMARK 960 127 . NAD C 330 AC2 . . . NAD C 330 AN1 REMARK 960 . . . REMARK 960 6881 . 6880 . REMARK 960 128 . NAD C 330 AC2 . . . NAD C 330 AN3 REMARK 960 . . . REMARK 960 6881 . 6882 . REMARK 960 129 . NAD C 330 AC4 . . . NAD C 330 AN3 REMARK 960 . . . REMARK 960 6883 . 6882 . REMARK 960 130 . NAD C 330 O3 . . . NAD C 330 NP REMARK 960 . . . REMARK 960 6884 . 6885 . REMARK 960 131 . NAD C 330 NO1 . . . NAD C 330 NP REMARK 960 . . . REMARK 960 6886 . 6885 . REMARK 960 132 . NAD C 330 NO2 . . . NAD C 330 NP REMARK 960 . . . REMARK 960 6887 . 6885 . REMARK 960 133 . NAD C 330 NO5* . . . NAD C 330 NP REMARK 960 . . . REMARK 960 6888 . 6885 . REMARK 960 134 . NAD C 330 NC5* . . . NAD C 330 NO5* REMARK 960 . . . REMARK 960 6889 . 6888 . REMARK 960 135 . NAD C 330 NC4* . . . NAD C 330 NC5* REMARK 960 . . . REMARK 960 6890 . 6889 . REMARK 960 136 . NAD C 330 NC4* . . . NAD C 330 NO4* REMARK 960 . . . REMARK 960 6890 . 6891 . REMARK 960 137 . NAD C 330 NC3* . . . NAD C 330 NC4* REMARK 960 . . . REMARK 960 6892 . 6890 . REMARK 960 138 . NAD C 330 NC1* . . . NAD C 330 NO4* REMARK 960 . . . REMARK 960 6896 . 6891 . REMARK 960 139 . NAD C 330 NC3* . . . NAD C 330 NO3* REMARK 960 . . . REMARK 960 6892 . 6893 . REMARK 960 140 . NAD C 330 NC2* . . . NAD C 330 NC3* REMARK 960 . . . REMARK 960 6894 . 6892 . REMARK 960 141 . NAD C 330 NC2* . . . NAD C 330 NO2* REMARK 960 . . . REMARK 960 6894 . 6895 . REMARK 960 142 . NAD C 330 NC1* . . . NAD C 330 NC2* REMARK 960 . . . REMARK 960 6896 . 6894 . REMARK 960 143 . NAD C 330 NC1* . . . NAD C 330 NN1 REMARK 960 . . . REMARK 960 6896 . 6897 . REMARK 960 144 . NAD C 330 NC2 . . . NAD C 330 NN1 REMARK 960 . . . REMARK 960 6898 . 6897 . REMARK 960 145 . NAD C 330 NC6 . . . NAD C 330 NN1 REMARK 960 . . . REMARK 960 6905 . 6897 . REMARK 960 146 . NAD C 330 NC2 . . . NAD C 330 NC3 REMARK 960 . . . REMARK 960 6898 . 6899 . REMARK 960 147 . NAD C 330 NC3 . . . NAD C 330 NC7 REMARK 960 . . . REMARK 960 6899 . 6900 . REMARK 960 148 . NAD C 330 NC3 . . . NAD C 330 NC4 REMARK 960 . . . REMARK 960 6899 . 6903 . REMARK 960 149 . NAD C 330 NC7 . . . NAD C 330 NO7 REMARK 960 . . . REMARK 960 6900 . 6901 . REMARK 960 150 . NAD C 330 NC7 . . . NAD C 330 NN7 REMARK 960 . . . REMARK 960 6900 . 6902 . REMARK 960 151 . NAD C 330 NC4 . . . NAD C 330 NC5 REMARK 960 . . . REMARK 960 6903 . 6904 . REMARK 960 152 . NAD C 330 NC5 . . . NAD C 330 NC6 REMARK 960 . . . REMARK 960 6904 . 6905 . REMARK 960 153 . SO4 C 331 O1 . . . SO4 C 331 S REMARK 960 . . . REMARK 960 6907 . 6906 . REMARK 960 154 . SO4 C 331 O2 . . . SO4 C 331 S REMARK 960 . . . REMARK 960 6908 . 6906 . REMARK 960 155 . SO4 C 331 O3 . . . SO4 C 331 S REMARK 960 . . . REMARK 960 6909 . 6906 . REMARK 960 156 . SO4 C 331 O4 . . . SO4 C 331 S REMARK 960 . . . REMARK 960 6910 . 6906 . REMARK 960 157 . NAD D 330 AO1 . . . NAD D 330 AP REMARK 960 . . . REMARK 960 9203 . 9202 . REMARK 960 158 . NAD D 330 AO2 . . . NAD D 330 AP REMARK 960 . . . REMARK 960 9204 . 9202 . REMARK 960 159 . NAD D 330 AO5* . . . NAD D 330 AP REMARK 960 . . . REMARK 960 9205 . 9202 . REMARK 960 160 . NAD D 330 O3 . . . NAD D 330 AP REMARK 960 . . . REMARK 960 9224 . 9202 . REMARK 960 161 . NAD D 330 AC5* . . . NAD D 330 AO5* REMARK 960 . . . REMARK 960 9206 . 9205 . REMARK 960 162 . NAD D 330 AC4* . . . NAD D 330 AC5* REMARK 960 . . . REMARK 960 9207 . 9206 . REMARK 960 163 . NAD D 330 AC4* . . . NAD D 330 AO4* REMARK 960 . . . REMARK 960 9207 . 9208 . REMARK 960 164 . NAD D 330 AC3* . . . NAD D 330 AC4* REMARK 960 . . . REMARK 960 9209 . 9207 . REMARK 960 165 . NAD D 330 AC1* . . . NAD D 330 AO4* REMARK 960 . . . REMARK 960 9213 . 9208 . REMARK 960 166 . NAD D 330 AC3* . . . NAD D 330 AO3* REMARK 960 . . . REMARK 960 9209 . 9210 . REMARK 960 167 . NAD D 330 AC2* . . . NAD D 330 AC3* REMARK 960 . . . REMARK 960 9211 . 9209 . REMARK 960 168 . NAD D 330 AC2* . . . NAD D 330 AO2* REMARK 960 . . . REMARK 960 9211 . 9212 . REMARK 960 169 . NAD D 330 AC1* . . . NAD D 330 AC2* REMARK 960 . . . REMARK 960 9213 . 9211 . REMARK 960 170 . NAD D 330 AC1* . . . NAD D 330 AN9 REMARK 960 . . . REMARK 960 9213 . 9214 . REMARK 960 171 . NAD D 330 AC8 . . . NAD D 330 AN9 REMARK 960 . . . REMARK 960 9215 . 9214 . REMARK 960 172 . NAD D 330 AC4 . . . NAD D 330 AN9 REMARK 960 . . . REMARK 960 9223 . 9214 . REMARK 960 173 . NAD D 330 AC8 . . . NAD D 330 AN7 REMARK 960 . . . REMARK 960 9215 . 9216 . REMARK 960 174 . NAD D 330 AC5 . . . NAD D 330 AN7 REMARK 960 . . . REMARK 960 9217 . 9216 . REMARK 960 175 . NAD D 330 AC5 . . . NAD D 330 AC6 REMARK 960 . . . REMARK 960 9217 . 9218 . REMARK 960 176 . NAD D 330 AC4 . . . NAD D 330 AC5 REMARK 960 . . . REMARK 960 9223 . 9217 . REMARK 960 177 . NAD D 330 AC6 . . . NAD D 330 AN6 REMARK 960 . . . REMARK 960 9218 . 9219 . REMARK 960 178 . NAD D 330 AC6 . . . NAD D 330 AN1 REMARK 960 . . . REMARK 960 9218 . 9220 . REMARK 960 179 . NAD D 330 AC2 . . . NAD D 330 AN1 REMARK 960 . . . REMARK 960 9221 . 9220 . REMARK 960 180 . NAD D 330 AC2 . . . NAD D 330 AN3 REMARK 960 . . . REMARK 960 9221 . 9222 . REMARK 960 181 . NAD D 330 AC4 . . . NAD D 330 AN3 REMARK 960 . . . REMARK 960 9223 . 9222 . REMARK 960 182 . NAD D 330 O3 . . . NAD D 330 NP REMARK 960 . . . REMARK 960 9224 . 9225 . REMARK 960 183 . NAD D 330 NO1 . . . NAD D 330 NP REMARK 960 . . . REMARK 960 9226 . 9225 . REMARK 960 184 . NAD D 330 NO2 . . . NAD D 330 NP REMARK 960 . . . REMARK 960 9227 . 9225 . REMARK 960 185 . NAD D 330 NO5* . . . NAD D 330 NP REMARK 960 . . . REMARK 960 9228 . 9225 . REMARK 960 186 . NAD D 330 NC5* . . . NAD D 330 NO5* REMARK 960 . . . REMARK 960 9229 . 9228 . REMARK 960 187 . NAD D 330 NC4* . . . NAD D 330 NC5* REMARK 960 . . . REMARK 960 9230 . 9229 . REMARK 960 188 . NAD D 330 NC4* . . . NAD D 330 NO4* REMARK 960 . . . REMARK 960 9230 . 9231 . REMARK 960 189 . NAD D 330 NC3* . . . NAD D 330 NC4* REMARK 960 . . . REMARK 960 9232 . 9230 . REMARK 960 190 . NAD D 330 NC1* . . . NAD D 330 NO4* REMARK 960 . . . REMARK 960 9236 . 9231 . REMARK 960 191 . NAD D 330 NC3* . . . NAD D 330 NO3* REMARK 960 . . . REMARK 960 9232 . 9233 . REMARK 960 192 . NAD D 330 NC2* . . . NAD D 330 NC3* REMARK 960 . . . REMARK 960 9234 . 9232 . REMARK 960 193 . NAD D 330 NC2* . . . NAD D 330 NO2* REMARK 960 . . . REMARK 960 9234 . 9235 . REMARK 960 194 . NAD D 330 NC1* . . . NAD D 330 NC2* REMARK 960 . . . REMARK 960 9236 . 9234 . REMARK 960 195 . NAD D 330 NC1* . . . NAD D 330 NN1 REMARK 960 . . . REMARK 960 9236 . 9237 . REMARK 960 196 . NAD D 330 NC2 . . . NAD D 330 NN1 REMARK 960 . . . REMARK 960 9238 . 9237 . REMARK 960 197 . NAD D 330 NC6 . . . NAD D 330 NN1 REMARK 960 . . . REMARK 960 9245 . 9237 . REMARK 960 198 . NAD D 330 NC2 . . . NAD D 330 NC3 REMARK 960 . . . REMARK 960 9238 . 9239 . REMARK 960 199 . NAD D 330 NC3 . . . NAD D 330 NC7 REMARK 960 . . . REMARK 960 9239 . 9240 . REMARK 960 200 . NAD D 330 NC3 . . . NAD D 330 NC4 REMARK 960 . . . REMARK 960 9239 . 9243 . REMARK 960 201 . NAD D 330 NC7 . . . NAD D 330 NO7 REMARK 960 . . . REMARK 960 9240 . 9241 . REMARK 960 202 . NAD D 330 NC7 . . . NAD D 330 NN7 REMARK 960 . . . REMARK 960 9240 . 9242 . REMARK 960 203 . NAD D 330 NC4 . . . NAD D 330 NC5 REMARK 960 . . . REMARK 960 9243 . 9244 . REMARK 960 204 . NAD D 330 NC5 . . . NAD D 330 NC6 REMARK 960 . . . REMARK 960 9244 . 9245 . REMARK 960 205 . SO4 D 331 O1 . . . SO4 D 331 S REMARK 960 . . . REMARK 960 9247 . 9246 . REMARK 960 206 . SO4 D 331 O2 . . . SO4 D 331 S REMARK 960 . . . REMARK 960 9248 . 9246 . REMARK 960 207 . SO4 D 331 O3 . . . SO4 D 331 S REMARK 960 . . . REMARK 960 9249 . 9246 . REMARK 960 208 . SO4 D 331 O4 . . . SO4 D 331 S REMARK 960 . . . REMARK 960 9250 . 9246 . REMARK 960 REMARK 960 REMARK 960 REMARK 960 #################### REMARK 960 # # REMARK 960 # STRUCT_CONF # REMARK 960 # # REMARK 960 #################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_conf_type.id REMARK 960 _struct_conf_type.criteria REMARK 960 _struct_conf_type.reference REMARK 960 HELX_RH_AL_P 'From PDB' . REMARK 960 HELX_RH_3T_P 'From PDB' . REMARK 960 REMARK 960 loop_ REMARK 960 _struct_conf.id REMARK 960 _struct_conf.conf_type_id REMARK 960 _struct_conf.beg_label_comp_id REMARK 960 _struct_conf.beg_label_asym_id REMARK 960 _struct_conf.beg_auth_seq_id REMARK 960 _struct_conf.end_label_comp_id REMARK 960 _struct_conf.end_label_asym_id REMARK 960 _struct_conf.end_auth_seq_id REMARK 960 _struct_conf.details REMARK 960 _struct_conf.beg_label_seq_id REMARK 960 _struct_conf.end_label_seq_id REMARK 960 helix_1 HELX_RH_AL_P ASN A 31 GLN A 43 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 11 23 REMARK 960 helix_2 HELX_RH_AL_P GLU A 56 ASN A 72 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 36 52 REMARK 960 helix_3 HELX_RH_3T_P TRP A 84 LEU A 87 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 64 67 REMARK 960 helix_4 HELX_RH_3T_P ILE A 100 GLN A 103 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 80 83 REMARK 960 helix_5 HELX_RH_3T_P ALA A 113 GLU A 131 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 93 111 REMARK 960 helix_6 HELX_RH_AL_P VAL A 145 THR A 156 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 125 136 REMARK 960 helix_7 HELX_RH_AL_P GLY A 167 PHE A 183 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 147 163 REMARK 960 helix_8 HELX_RH_AL_P LEU A 227 LYS A 245 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 207 225 REMARK 960 helix_9 HELX_RH_AL_P TYR A 250 MET A 264 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 230 244 REMARK 960 helix_10 HELX_RH_AL_P THR A 305 VAL A 326 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 285 306 REMARK 960 helix_11 HELX_RH_AL_P ASN B 31 GLN B 43 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 11 23 REMARK 960 helix_12 HELX_RH_AL_P GLU B 56 ASN B 72 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 36 52 REMARK 960 helix_13 HELX_RH_3T_P TRP B 84 LEU B 87 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 64 67 REMARK 960 helix_14 HELX_RH_3T_P ILE B 100 GLN B 103 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 80 83 REMARK 960 helix_15 HELX_RH_3T_P ALA B 113 SER B 132 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 93 112 REMARK 960 helix_16 HELX_RH_AL_P VAL B 145 THR B 156 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 125 136 REMARK 960 helix_17 HELX_RH_AL_P GLY B 167 PHE B 183 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 147 163 REMARK 960 helix_18 HELX_RH_AL_P LEU B 227 LYS B 245 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 207 225 REMARK 960 helix_19 HELX_RH_AL_P TYR B 250 MET B 264 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 230 244 REMARK 960 helix_20 HELX_RH_AL_P THR B 305 ILE B 325 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 285 305 REMARK 960 helix_21 HELX_RH_AL_P ASN C 31 GLN C 43 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 11 23 REMARK 960 helix_22 HELX_RH_AL_P GLU C 56 ASN C 72 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 36 52 REMARK 960 helix_23 HELX_RH_3T_P TRP C 84 ASP C 89 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 64 69 REMARK 960 helix_24 HELX_RH_AL_P ASP C 110 SER C 132 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 90 112 REMARK 960 helix_25 HELX_RH_AL_P VAL C 145 THR C 156 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 125 136 REMARK 960 helix_26 HELX_RH_AL_P LEU C 169 ALA C 182 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 149 162 REMARK 960 helix_27 HELX_RH_AL_P ILE C 216 ASP C 221 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 196 201 REMARK 960 helix_28 HELX_RH_AL_P LEU C 227 LYS C 245 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 207 225 REMARK 960 helix_29 HELX_RH_AL_P TYR C 250 MET C 264 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 230 244 REMARK 960 helix_30 HELX_RH_AL_P THR C 305 THR C 328 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 285 308 REMARK 960 helix_31 HELX_RH_AL_P ASN D 31 ALA D 42 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 11 22 REMARK 960 helix_32 HELX_RH_AL_P GLU D 56 ASN D 72 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 36 52 REMARK 960 helix_33 HELX_RH_3T_P TRP D 84 LEU D 87 REMARK 960 'RIGHT-HANDED 3/10 HELIX' REMARK 960 64 67 REMARK 960 helix_34 HELX_RH_AL_P ASP D 110 SER D 132 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 90 112 REMARK 960 helix_35 HELX_RH_AL_P VAL D 145 THR D 156 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 125 136 REMARK 960 helix_36 HELX_RH_AL_P GLY D 167 PHE D 183 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 147 163 REMARK 960 helix_37 HELX_RH_AL_P ILE D 216 ASP D 221 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 196 201 REMARK 960 helix_38 HELX_RH_AL_P LEU D 227 LYS D 245 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 207 225 REMARK 960 helix_39 HELX_RH_AL_P TYR D 250 ALA D 265 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 230 245 REMARK 960 helix_40 HELX_RH_AL_P THR D 305 ASP D 327 REMARK 960 'RIGHT-HANDED ALPHA HELIX' REMARK 960 285 307 REMARK 960 REMARK 960 REMARK 960 REMARK 960 ################ REMARK 960 # # REMARK 960 # STRUCT_SHEET # REMARK 960 # # REMARK 960 ################ REMARK 960 REMARK 960 loop_ REMARK 960 _struct_sheet.id REMARK 960 _struct_sheet.number_strands REMARK 960 A 6 REMARK 960 B 3 REMARK 960 C 3 REMARK 960 D 6 REMARK 960 E 3 REMARK 960 F 3 REMARK 960 G 6 REMARK 960 H 3 REMARK 960 I 3 REMARK 960 J 6 REMARK 960 K 3 REMARK 960 L 3 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_sheet_hbond.sheet_id REMARK 960 _struct_sheet_hbond.range_id_1 REMARK 960 _struct_sheet_hbond.range_id_2 REMARK 960 _struct_sheet_hbond.range_1_beg_auth_seq_id REMARK 960 _struct_sheet_hbond.range_1_beg_label_atom_id REMARK 960 _struct_sheet_hbond.range_2_beg_auth_seq_id REMARK 960 _struct_sheet_hbond.range_2_beg_label_atom_id REMARK 960 _struct_sheet_hbond.range_1_end_auth_seq_id REMARK 960 _struct_sheet_hbond.range_1_end_label_atom_id REMARK 960 _struct_sheet_hbond.range_2_end_auth_seq_id REMARK 960 _struct_sheet_hbond.range_2_end_label_atom_id REMARK 960 _struct_sheet_hbond.range_1_beg_label_seq_id REMARK 960 _struct_sheet_hbond.range_2_beg_label_seq_id REMARK 960 _struct_sheet_hbond.range_1_end_label_seq_id REMARK 960 _struct_sheet_hbond.range_2_end_label_seq_id REMARK 960 A 1_A 2_A 164 O 138 N 164 O 138 REMARK 960 N REMARK 960 144 118 144 118 REMARK 960 A 2_A 3_A 137 O 93 N 137 O 93 REMARK 960 N REMARK 960 117 73 117 73 REMARK 960 A 3_A 4_A 92 O 25 N 92 O 25 REMARK 960 N REMARK 960 72 5 72 5 REMARK 960 A 4_A 5_A 24 O 48 N 24 O 48 REMARK 960 N REMARK 960 4 28 4 28 REMARK 960 A 5_A 6_A 49 O 78 N 49 O 78 REMARK 960 N REMARK 960 29 58 29 58 REMARK 960 B 1_B 2_B 193 O 205 N 193 O 205 REMARK 960 N REMARK 960 173 185 173 185 REMARK 960 B 2_B 3_B 210 O 214 N 210 O 214 REMARK 960 N REMARK 960 190 194 190 194 REMARK 960 C 1_C 2_C 269 O 290 N 269 O 290 REMARK 960 N REMARK 960 249 270 249 270 REMARK 960 C 2_C 3_C 289 O 297 N 289 O 297 REMARK 960 N REMARK 960 269 277 269 277 REMARK 960 D 1_D 2_D 164 O 138 N 164 O 138 REMARK 960 N REMARK 960 144 118 144 118 REMARK 960 D 2_D 3_D 137 O 93 N 137 O 93 REMARK 960 N REMARK 960 117 73 117 73 REMARK 960 D 3_D 4_D 92 O 25 N 92 O 25 REMARK 960 N REMARK 960 72 5 72 5 REMARK 960 D 4_D 5_D 24 O 48 N 24 O 48 REMARK 960 N REMARK 960 4 28 4 28 REMARK 960 D 5_D 6_D 49 O 78 N 49 O 78 REMARK 960 N REMARK 960 29 58 29 58 REMARK 960 E 1_E 2_E 193 O 205 N 193 O 205 REMARK 960 N REMARK 960 173 185 173 185 REMARK 960 E 2_E 3_E 210 O 214 N 210 O 214 REMARK 960 N REMARK 960 190 194 190 194 REMARK 960 F 1_F 2_F 269 O 290 N 269 O 290 REMARK 960 N REMARK 960 249 270 249 270 REMARK 960 F 2_F 3_F 289 O 297 N 289 O 297 REMARK 960 N REMARK 960 269 277 269 277 REMARK 960 G 1_G 2_G 164 O 138 N 164 O 138 REMARK 960 N REMARK 960 144 118 144 118 REMARK 960 G 2_G 3_G 137 O 93 N 137 O 93 REMARK 960 N REMARK 960 117 73 117 73 REMARK 960 G 3_G 4_G 92 O 25 N 92 O 25 REMARK 960 N REMARK 960 72 5 72 5 REMARK 960 G 4_G 5_G 24 O 48 N 24 O 48 REMARK 960 N REMARK 960 4 28 4 28 REMARK 960 G 5_G 6_G 49 O 78 N 49 O 78 REMARK 960 N REMARK 960 29 58 29 58 REMARK 960 H 1_H 2_H 193 O 205 N 193 O 205 REMARK 960 N REMARK 960 173 185 173 185 REMARK 960 H 2_H 3_H 210 O 214 N 210 O 214 REMARK 960 N REMARK 960 190 194 190 194 REMARK 960 I 1_I 2_I 269 O 290 N 269 O 290 REMARK 960 N REMARK 960 249 270 249 270 REMARK 960 I 2_I 3_I 289 O 297 N 289 O 297 REMARK 960 N REMARK 960 269 277 269 277 REMARK 960 J 1_J 2_J 164 O 138 N 164 O 138 REMARK 960 N REMARK 960 144 118 144 118 REMARK 960 J 2_J 3_J 137 O 93 N 137 O 93 REMARK 960 N REMARK 960 117 73 117 73 REMARK 960 J 3_J 4_J 92 O 25 N 92 O 25 REMARK 960 N REMARK 960 72 5 72 5 REMARK 960 J 4_J 5_J 24 O 48 N 24 O 48 REMARK 960 N REMARK 960 4 28 4 28 REMARK 960 J 5_J 6_J 49 O 78 N 49 O 78 REMARK 960 N REMARK 960 29 58 29 58 REMARK 960 K 1_K 2_K 193 O 205 N 193 O 205 REMARK 960 N REMARK 960 173 185 173 185 REMARK 960 K 2_K 3_K 210 O 214 N 210 O 214 REMARK 960 N REMARK 960 190 194 190 194 REMARK 960 L 1_L 2_L 269 O 290 N 269 O 290 REMARK 960 N REMARK 960 249 270 249 270 REMARK 960 L 2_L 3_L 289 O 297 N 289 O 297 REMARK 960 N REMARK 960 269 277 269 277 REMARK 960 REMARK 960 loop_ REMARK 960 _struct_sheet_order.sheet_id REMARK 960 _struct_sheet_order.range_id_1 REMARK 960 _struct_sheet_order.range_id_2 REMARK 960 _struct_sheet_order.offset REMARK 960 _struct_sheet_order.sense REMARK 960 A 1_A 2_A 1 parallel REMARK 960 A 2_A 3_A 1 parallel REMARK 960 A 3_A 4_A 1 parallel REMARK 960 A 4_A 5_A 1 parallel REMARK 960 A 5_A 6_A 1 parallel REMARK 960 B 1_B 2_B 1 anti-parallel REMARK 960 B 2_B 3_B 1 anti-parallel REMARK 960 C 1_C 2_C 1 anti-parallel REMARK 960 C 2_C 3_C 1 anti-parallel REMARK 960 D 1_D 2_D 1 parallel REMARK 960 D 2_D 3_D 1 parallel REMARK 960 D 3_D 4_D 1 parallel REMARK 960 D 4_D 5_D 1 parallel REMARK 960 D 5_D 6_D 1 parallel REMARK 960 E 1_E 2_E 1 anti-parallel REMARK 960 E 2_E 3_E 1 anti-parallel REMARK 960 F 1_F 2_F 1 anti-parallel REMARK 960 F 2_F 3_F 1 anti-parallel REMARK 960 G 1_G 2_G 1 parallel REMARK 960 G 2_G 3_G 1 parallel REMARK 960 G 3_G 4_G 1 parallel REMARK 960 G 4_G 5_G 1 parallel REMARK 960 G 5_G 6_G 1 parallel REMARK 960 H 1_H 2_H 1 anti-parallel REMARK 960 H 2_H 3_H 1 anti-parallel REMARK 960 I 1_I 2_I 1 anti-parallel REMARK 960 I 2_I 3_I 1 anti-parallel REMARK 960 J 1_J 2_J 1 parallel REMARK 960 J 2_J 3_J 1 parallel REMARK 960 J 3_J 4_J 1 parallel REMARK 960 J 4_J 5_J 1 parallel REMARK 960 J 5_J 6_J 1 parallel REMARK 960 K 1_K 2_K 1 anti-parallel REMARK 960 K 2_K 3_K 1 anti-parallel REMARK 960 L 1_L 2_L 1 anti-parallel REMARK 960 L 2_L 3_L 1 anti-parallel REMARK 960 REMARK 960 loop_ REMARK 960 _struct_sheet_range.sheet_id REMARK 960 _struct_sheet_range.id REMARK 960 _struct_sheet_range.beg_label_comp_id REMARK 960 _struct_sheet_range.beg_label_asym_id REMARK 960 _struct_sheet_range.beg_auth_seq_id REMARK 960 _struct_sheet_range.end_label_comp_id REMARK 960 _struct_sheet_range.end_label_asym_id REMARK 960 _struct_sheet_range.end_auth_seq_id REMARK 960 _struct_sheet_range.beg_label_seq_id REMARK 960 _struct_sheet_range.end_label_seq_id REMARK 960 A 1_A VAL A 163 GLY A 165 REMARK 960 143 145 REMARK 960 A 2_A VAL A 137 VAL A 140 REMARK 960 117 120 REMARK 960 A 3_A VAL A 92 SER A 95 REMARK 960 72 75 REMARK 960 A 4_A LYS A 23 ILE A 27 REMARK 960 3 7 REMARK 960 A 5_A ASP A 48 ILE A 52 REMARK 960 28 32 REMARK 960 A 6_A ASN A 78 ILE A 81 REMARK 960 58 61 REMARK 960 B 1_B TYR A 193 LEU A 195 REMARK 960 173 175 REMARK 960 B 2_B PHE A 203 VAL A 211 REMARK 960 183 191 REMARK 960 B 3_B GLN A 214 PRO A 215 REMARK 960 194 195 REMARK 960 C 1_C ALA A 269 ARG A 276 REMARK 960 249 256 REMARK 960 C 2_C TYR A 283 GLY A 291 REMARK 960 263 271 REMARK 960 C 3_C GLY A 294 GLU A 298 REMARK 960 274 278 REMARK 960 D 1_D VAL B 163 GLY B 165 REMARK 960 143 145 REMARK 960 D 2_D VAL B 137 VAL B 140 REMARK 960 117 120 REMARK 960 D 3_D VAL B 92 SER B 95 REMARK 960 72 75 REMARK 960 D 4_D LYS B 23 ILE B 27 REMARK 960 3 7 REMARK 960 D 5_D ASP B 48 ILE B 52 REMARK 960 28 32 REMARK 960 D 6_D ASN B 78 ILE B 81 REMARK 960 58 61 REMARK 960 E 1_E TYR B 193 LEU B 195 REMARK 960 173 175 REMARK 960 E 2_E PHE B 203 VAL B 211 REMARK 960 183 191 REMARK 960 E 3_E GLN B 214 PRO B 215 REMARK 960 194 195 REMARK 960 F 1_F ALA B 269 ASN B 275 REMARK 960 249 255 REMARK 960 F 2_F LEU B 284 GLY B 291 REMARK 960 264 271 REMARK 960 F 3_F GLY B 294 GLU B 298 REMARK 960 274 278 REMARK 960 G 1_G VAL C 163 GLY C 165 REMARK 960 143 145 REMARK 960 G 2_G VAL C 137 VAL C 140 REMARK 960 117 120 REMARK 960 G 3_G VAL C 92 SER C 95 REMARK 960 72 75 REMARK 960 G 4_G LYS C 23 ILE C 27 REMARK 960 3 7 REMARK 960 G 5_G ASP C 48 ILE C 52 REMARK 960 28 32 REMARK 960 G 6_G ASN C 78 ILE C 81 REMARK 960 58 61 REMARK 960 H 1_H TYR C 193 LEU C 195 REMARK 960 173 175 REMARK 960 H 2_H PHE C 203 VAL C 211 REMARK 960 183 191 REMARK 960 H 3_H GLN C 214 PRO C 215 REMARK 960 194 195 REMARK 960 I 1_I ALA C 269 ARG C 276 REMARK 960 249 256 REMARK 960 I 2_I TYR C 283 GLY C 291 REMARK 960 263 271 REMARK 960 I 3_I GLY C 294 GLU C 298 REMARK 960 274 278 REMARK 960 J 1_J VAL D 163 GLY D 165 REMARK 960 143 145 REMARK 960 J 2_J VAL D 137 VAL D 140 REMARK 960 117 120 REMARK 960 J 3_J VAL D 92 SER D 95 REMARK 960 72 75 REMARK 960 J 4_J LYS D 23 ILE D 27 REMARK 960 3 7 REMARK 960 J 5_J ASP D 48 ILE D 52 REMARK 960 28 32 REMARK 960 J 6_J ASN D 78 ILE D 81 REMARK 960 58 61 REMARK 960 K 1_K TYR D 193 LEU D 195 REMARK 960 173 175 REMARK 960 K 2_K PHE D 203 VAL D 211 REMARK 960 183 191 REMARK 960 K 3_K GLN D 214 PRO D 215 REMARK 960 194 195 REMARK 960 L 1_L ALA D 269 ARG D 276 REMARK 960 249 256 REMARK 960 L 2_L TYR D 283 GLY D 291 REMARK 960 263 271 REMARK 960 L 3_L GLY D 294 GLU D 298 REMARK 960 274 278 REMARK 960 REMARK 960 REMARK 960 REMARK 960 ######################## REMARK 960 # # REMARK 960 # PUBL_MANUSCRIPT_INCL # REMARK 960 # # REMARK 960 ######################## REMARK 960 REMARK 960 REMARK 960 REMARK 960 loop_ REMARK 960 _publ_manuscript_incl.entry_id REMARK 960 _publ_manuscript_incl.extra_item REMARK 960 _publ_manuscript_incl.extra_info REMARK 960 _publ_manuscript_incl.extra_defn REMARK 960 1HYH REMARK 960 '_struct_conn.ptnr1_atom_site_id' REMARK 960 '_atom_site.id of partner 1 of structure connection' REMARK 960 no REMARK 960 REMARK 960 1HYH REMARK 960 '_struct_conn.ptnr2_atom_site_id' REMARK 960 '_atom_site.id of partner 2 of structure connection' REMARK 960 no REMARK 960 REMARK 960 ############################################### REMARK 960 # This file was converted automatically from # REMARK 960 # PDB format to mmCIF format by the program # REMARK 960 # pdb2cif version 2.3.6 15 Jun 98 # REMARK 960 # by # REMARK 960 # Phil Bourne, Herbert J. Bernstein and # REMARK 960 # Frances C. Bernstein # REMARK 960 # # REMARK 960 # This work was supported in part by IUCr # REMARK 960 # (for HJB), US NSF, PHS, NIH, NCRR, NIGMS, # REMARK 960 # NLM and DOE (for FCB prior to 1998), and # REMARK 960 # and NSFgrant no. BIR 9310154 (for PEB) # REMARK 960 # # REMARK 960 # # REMARK 960 # Conversion from PDB format to mmCIF is a # REMARK 960 # complex process. This file should be # REMARK 960 # reviewed carefully before use. # REMARK 960 # # REMARK 960 # Even though the authors of pdb2cif have # REMARK 960 # made a good faith effort to ensure that # REMARK 960 # pdb2cif performs according to its # REMARK 960 # documentation, and we would greatly # REMARK 960 # appreciate hearing of any problems you # REMARK 960 # may encounter, the program pdb2cif and # REMARK 960 # any files created by pdb2cif are provided # REMARK 960 # **AS IS** without any warrantee as to # REMARK 960 # correctness, merchantability or fitness # REMARK 960 # for any particular or general use. # REMARK 960 # # REMARK 960 # THE RESPONSIBILITY FOR ANY ADVERSE # REMARK 960 # CONSEQUENCES FROM THE USE OF THE PROGRAM # REMARK 960 # PDB2CIF OR ANY FILE OR FILES CREATED BY # REMARK 960 # LIES SOLELY WITH THE USERS OF THE PROGRAM # REMARK 960 # AND FILE OR FILES AND NOT WITH AUTHORS OF # REMARK 960 # PDB2CIF # REMARK 960 # # REMARK 960 # The program pdb2cif is available from # REMARK 960 # the IUCr and its mirrors (see # REMARK 960 # http://www.iucr.org/iucr-top/cif # REMARK 960 # /software/pdb2cif) or # REMARK 960 # SDSC (see # REMARK 960 # http://www.sdsc.edu/pb/pdb2cif/pdb2cif) or # REMARK 960 # NDB and its mirrors (see # REMARK 960 # http://ndbserver.rutgers.edu/NDB/mmcif # REMARK 960 # /software/pdb2cif) # REMARK 960 # and the NDB mirror sites # REMARK 960 # # REMARK 960 # See H. Bernstein, F. Bernstein, # REMARK 960 # P. E. Bourne CIF Applications. VIII. # REMARK 960 # pdb2cif: Translating PDB Entries into # REMARK 960 # mmCIF Format, J. Appl. Cryst., # REMARK 960 # to appear, 1998. # REMARK 960 # Please report problems to: # REMARK 960 # yaya@bernstein-plus-sons.com # REMARK 960 # # REMARK 960 ############################################### REMARK 960 REMARK 960 REMARK 960 REMARK 960 # REMARK records parsed = 230; REMARK 960 ## specified by PDB REMARK 960 # FTNOTE records parsed = 8; REMARK 960 ## specified by PDB REMARK 960 # HET records parsed = 8; REMARK 960 ## specified by PDB REMARK 960 # HELIX records parsed = 40; REMARK 960 ## specified by PDB REMARK 960 # SHEET records parsed = 48; REMARK 960 ## specified by PDB REMARK 960 # TURN records parsed = 0; REMARK 960 ## specified by PDB REMARK 960 # SITE records parsed = 0; REMARK 960 ## specified by PDB REMARK 960 # AT+HET records parsed = 9319; REMARK 960 ## specified by PDB REMARK 960 # TER records parsed = 4; REMARK 960 ## specified by PDB REMARK 960 # CONECT records parsed = 196; REMARK 960 ## specified by PDB REMARK 960 # SEQRES records parsed = 96; REMARK 960 ## specified by PDB REMARK 960 # Total of 10005 records processed from PDB file REMARK 960 # DATABASE_PDB_REMARK: Only text in colum REMARK 960 #ns 12-70 retained REMARK 960 # STRUCT_NCS_OPER: Domain information needed REMARK 960 # ATOM_SITE: Het group NAD; atom type AP REMARK 960 # converted to P REMARK 960 # ATOM_SITE: Het group NAD; atom type AO REMARK 960 # converted to O REMARK 960 # ATOM_SITE: Het group NAD; atom type AC REMARK 960 # converted to C REMARK 960 # ATOM_SITE: Het group NAD; atom type AN REMARK 960 # converted to N REMARK 960 # ATOM_SITE: Het group NAD; atom type NP REMARK 960 # converted to P REMARK 960 # ATOM_SITE: Het group NAD; atom type NO REMARK 960 # converted to O REMARK 960 # ATOM_SITE: Het group NAD; atom type NC REMARK 960 # converted to C REMARK 960 # ATOM_SITE: Het group NAD; atom type NN REMARK 960 # converted to N REMARK 960 # PUBL_MANUSCRIPT_INCL: Tokens _struct_co REMARK 960 #nn.ptnrn_atom_site_id used SEQRES 1 A 309 ALA ARG LYS ILE GLY ILE ILE GLY LEU GLY ASN VAL GLY SEQRES 2 A 309 ALA ALA VAL ALA HIS GLY LEU ILE ALA GLN GLY VAL ALA SEQRES 3 A 309 ASP ASP TYR VAL PHE ILE ASP ALA ASN GLU ALA LYS VAL SEQRES 4 A 309 LYS ALA ASP GLN ILE ASP PHE GLN ASP ALA MET ALA ASN SEQRES 5 A 309 LEU GLU ALA HIS GLY ASN ILE VAL ILE ASN ASP TRP ALA SEQRES 6 A 309 ALA LEU ALA ASP ALA ASP VAL VAL ILE SER THR LEU GLY SEQRES 7 A 309 ASN ILE LYS LEU GLN GLN ASP ASN PRO THR GLY ASP ARG SEQRES 8 A 309 PHE ALA GLU LEU LYS PHE THR SER SER MET VAL GLN SER SEQRES 9 A 309 VAL GLY THR ASN LEU LYS GLU SER GLY PHE HIS GLY VAL SEQRES 10 A 309 LEU VAL VAL ILE SER ASN PRO VAL ASP VAL ILE THR ALA SEQRES 11 A 309 LEU PHE GLN HIS VAL THR GLY PHE PRO ALA HIS LYS VAL SEQRES 12 A 309 ILE GLY THR GLY THR LEU LEU ASP THR ALA ARG MET GLN SEQRES 13 A 309 ARG ALA VAL GLY GLU ALA PHE ASP LEU ASP PRO ARG SER SEQRES 14 A 309 VAL SER GLY TYR ASN LEU GLY GLU HIS GLY ASN SER GLN SEQRES 15 A 309 PHE VAL ALA TRP SER THR VAL ARG VAL MET GLY GLN PRO SEQRES 16 A 309 ILE VAL THR LEU ALA ASP ALA GLY ASP ILE ASP LEU ALA SEQRES 17 A 309 ALA ILE GLU GLU GLU ALA ARG LYS GLY GLY PHE THR VAL SEQRES 18 A 309 LEU ASN GLY LYS GLY TYR THR SER TYR GLY VAL ALA THR SEQRES 19 A 309 SER ALA ILE ARG ILE ALA LYS ALA VAL MET ALA ASP ALA SEQRES 20 A 309 HIS ALA GLU LEU VAL VAL SER ASN ARG ARG ASP ASP MET SEQRES 21 A 309 GLY MET TYR LEU SER TYR PRO ALA ILE ILE GLY ARG ASP SEQRES 22 A 309 GLY VAL LEU ALA GLU THR THR LEU ASP LEU THR THR ASP SEQRES 23 A 309 GLU GLN GLU LYS LEU LEU GLN SER ARG ASP TYR ILE GLN SEQRES 24 A 309 GLN ARG PHE ASP GLU ILE VAL ASP THR LEU SEQRES 1 B 309 ALA ARG LYS ILE GLY ILE ILE GLY LEU GLY ASN VAL GLY SEQRES 2 B 309 ALA ALA VAL ALA HIS GLY LEU ILE ALA GLN GLY VAL ALA SEQRES 3 B 309 ASP ASP TYR VAL PHE ILE ASP ALA ASN GLU ALA LYS VAL SEQRES 4 B 309 LYS ALA ASP GLN ILE ASP PHE GLN ASP ALA MET ALA ASN SEQRES 5 B 309 LEU GLU ALA HIS GLY ASN ILE VAL ILE ASN ASP TRP ALA SEQRES 6 B 309 ALA LEU ALA ASP ALA ASP VAL VAL ILE SER THR LEU GLY SEQRES 7 B 309 ASN ILE LYS LEU GLN GLN ASP ASN PRO THR GLY ASP ARG SEQRES 8 B 309 PHE ALA GLU LEU LYS PHE THR SER SER MET VAL GLN SER SEQRES 9 B 309 VAL GLY THR ASN LEU LYS GLU SER GLY PHE HIS GLY VAL SEQRES 10 B 309 LEU VAL VAL ILE SER ASN PRO VAL ASP VAL ILE THR ALA SEQRES 11 B 309 LEU PHE GLN HIS VAL THR GLY PHE PRO ALA HIS LYS VAL SEQRES 12 B 309 ILE GLY THR GLY THR LEU LEU ASP THR ALA ARG MET GLN SEQRES 13 B 309 ARG ALA VAL GLY GLU ALA PHE ASP LEU ASP PRO ARG SER SEQRES 14 B 309 VAL SER GLY TYR ASN LEU GLY GLU HIS GLY ASN SER GLN SEQRES 15 B 309 PHE VAL ALA TRP SER THR VAL ARG VAL MET GLY GLN PRO SEQRES 16 B 309 ILE VAL THR LEU ALA ASP ALA GLY ASP ILE ASP LEU ALA SEQRES 17 B 309 ALA ILE GLU GLU GLU ALA ARG LYS GLY GLY PHE THR VAL SEQRES 18 B 309 LEU ASN GLY LYS GLY TYR THR SER TYR GLY VAL ALA THR SEQRES 19 B 309 SER ALA ILE ARG ILE ALA LYS ALA VAL MET ALA ASP ALA SEQRES 20 B 309 HIS ALA GLU LEU VAL VAL SER ASN ARG ARG ASP ASP MET SEQRES 21 B 309 GLY MET TYR LEU SER TYR PRO ALA ILE ILE GLY ARG ASP SEQRES 22 B 309 GLY VAL LEU ALA GLU THR THR LEU ASP LEU THR THR ASP SEQRES 23 B 309 GLU GLN GLU LYS LEU LEU GLN SER ARG ASP TYR ILE GLN SEQRES 24 B 309 GLN ARG PHE ASP GLU ILE VAL ASP THR LEU SEQRES 1 C 309 ALA ARG LYS ILE GLY ILE ILE GLY LEU GLY ASN VAL GLY SEQRES 2 C 309 ALA ALA VAL ALA HIS GLY LEU ILE ALA GLN GLY VAL ALA SEQRES 3 C 309 ASP ASP TYR VAL PHE ILE ASP ALA ASN GLU ALA LYS VAL SEQRES 4 C 309 LYS ALA ASP GLN ILE ASP PHE GLN ASP ALA MET ALA ASN SEQRES 5 C 309 LEU GLU ALA HIS GLY ASN ILE VAL ILE ASN ASP TRP ALA SEQRES 6 C 309 ALA LEU ALA ASP ALA ASP VAL VAL ILE SER THR LEU GLY SEQRES 7 C 309 ASN ILE LYS LEU GLN GLN ASP ASN PRO THR GLY ASP ARG SEQRES 8 C 309 PHE ALA GLU LEU LYS PHE THR SER SER MET VAL GLN SER SEQRES 9 C 309 VAL GLY THR ASN LEU LYS GLU SER GLY PHE HIS GLY VAL SEQRES 10 C 309 LEU VAL VAL ILE SER ASN PRO VAL ASP VAL ILE THR ALA SEQRES 11 C 309 LEU PHE GLN HIS VAL THR GLY PHE PRO ALA HIS LYS VAL SEQRES 12 C 309 ILE GLY THR GLY THR LEU LEU ASP THR ALA ARG MET GLN SEQRES 13 C 309 ARG ALA VAL GLY GLU ALA PHE ASP LEU ASP PRO ARG SER SEQRES 14 C 309 VAL SER GLY TYR ASN LEU GLY GLU HIS GLY ASN SER GLN SEQRES 15 C 309 PHE VAL ALA TRP SER THR VAL ARG VAL MET GLY GLN PRO SEQRES 16 C 309 ILE VAL THR LEU ALA ASP ALA GLY ASP ILE ASP LEU ALA SEQRES 17 C 309 ALA ILE GLU GLU GLU ALA ARG LYS GLY GLY PHE THR VAL SEQRES 18 C 309 LEU ASN GLY LYS GLY TYR THR SER TYR GLY VAL ALA THR SEQRES 19 C 309 SER ALA ILE ARG ILE ALA LYS ALA VAL MET ALA ASP ALA SEQRES 20 C 309 HIS ALA GLU LEU VAL VAL SER ASN ARG ARG ASP ASP MET SEQRES 21 C 309 GLY MET TYR LEU SER TYR PRO ALA ILE ILE GLY ARG ASP SEQRES 22 C 309 GLY VAL LEU ALA GLU THR THR LEU ASP LEU THR THR ASP SEQRES 23 C 309 GLU GLN GLU LYS LEU LEU GLN SER ARG ASP TYR ILE GLN SEQRES 24 C 309 GLN ARG PHE ASP GLU ILE VAL ASP THR LEU SEQRES 1 D 309 ALA ARG LYS ILE GLY ILE ILE GLY LEU GLY ASN VAL GLY SEQRES 2 D 309 ALA ALA VAL ALA HIS GLY LEU ILE ALA GLN GLY VAL ALA SEQRES 3 D 309 ASP ASP TYR VAL PHE ILE ASP ALA ASN GLU ALA LYS VAL SEQRES 4 D 309 LYS ALA ASP GLN ILE ASP PHE GLN ASP ALA MET ALA ASN SEQRES 5 D 309 LEU GLU ALA HIS GLY ASN ILE VAL ILE ASN ASP TRP ALA SEQRES 6 D 309 ALA LEU ALA ASP ALA ASP VAL VAL ILE SER THR LEU GLY SEQRES 7 D 309 ASN ILE LYS LEU GLN GLN ASP ASN PRO THR GLY ASP ARG SEQRES 8 D 309 PHE ALA GLU LEU LYS PHE THR SER SER MET VAL GLN SER SEQRES 9 D 309 VAL GLY THR ASN LEU LYS GLU SER GLY PHE HIS GLY VAL SEQRES 10 D 309 LEU VAL VAL ILE SER ASN PRO VAL ASP VAL ILE THR ALA SEQRES 11 D 309 LEU PHE GLN HIS VAL THR GLY PHE PRO ALA HIS LYS VAL SEQRES 12 D 309 ILE GLY THR GLY THR LEU LEU ASP THR ALA ARG MET GLN SEQRES 13 D 309 ARG ALA VAL GLY GLU ALA PHE ASP LEU ASP PRO ARG SER SEQRES 14 D 309 VAL SER GLY TYR ASN LEU GLY GLU HIS GLY ASN SER GLN SEQRES 15 D 309 PHE VAL ALA TRP SER THR VAL ARG VAL MET GLY GLN PRO SEQRES 16 D 309 ILE VAL THR LEU ALA ASP ALA GLY ASP ILE ASP LEU ALA SEQRES 17 D 309 ALA ILE GLU GLU GLU ALA ARG LYS GLY GLY PHE THR VAL SEQRES 18 D 309 LEU ASN GLY LYS GLY TYR THR SER TYR GLY VAL ALA THR SEQRES 19 D 309 SER ALA ILE ARG ILE ALA LYS ALA VAL MET ALA ASP ALA SEQRES 20 D 309 HIS ALA GLU LEU VAL VAL SER ASN ARG ARG ASP ASP MET SEQRES 21 D 309 GLY MET TYR LEU SER TYR PRO ALA ILE ILE GLY ARG ASP SEQRES 22 D 309 GLY VAL LEU ALA GLU THR THR LEU ASP LEU THR THR ASP SEQRES 23 D 309 GLU GLN GLU LYS LEU LEU GLN SER ARG ASP TYR ILE GLN SEQRES 24 D 309 GLN ARG PHE ASP GLU ILE VAL ASP THR LEU CRYST1 135.900 135.900 205.900 90.00 90.00 120.00 P 32 2 1 24 ORIGX1 -.841744 -.495301 .214789 69.78027 ORIGX2 .488184 -.528440 .694573 -.23980 ORIGX3 -.230524 .689510 .686614 .40915 SCALE1 -.004120 -.005889 .004531 .51242 SCALE2 .004148 -.004490 .005902 -.00204 SCALE3 -.001119 .003348 .003334 .00199 ATOM 1 N ALA A 21 -2.163 -.548 18.406 1.00 13.29 N ATOM 2 CA ALA A 21 -2.514 .202 17.123 1.00 13.29 C ATOM 3 C ALA A 21 -1.459 1.263 16.952 1.00 13.29 C ATOM 4 O ALA A 21 -.680 1.472 17.901 1.00 13.29 O ATOM 5 CB ALA A 21 -3.905 .720 17.229 1.00 13.38 C ATOM 6 N ARG A 22 -1.420 1.894 15.751 1.00 11.39 N ATOM 7 CA ARG A 22 -.383 2.934 15.515 1.00 11.39 C ATOM 8 C ARG A 22 -.948 4.316 15.725 1.00 11.39 C ATOM 9 O ARG A 22 -2.061 4.613 15.278 1.00 11.39 O ATOM 10 CB ARG A 22 .148 2.808 14.106 1.00 13.03 C ATOM 11 CG ARG A 22 1.097 1.672 13.842 1.00 13.03 C ATOM 12 CD ARG A 22 1.317 1.488 12.388 1.00 13.03 C ATOM 13 NE ARG A 22 2.075 .368 11.952 1.00 13.03 N ATOM 14 CZ ARG A 22 2.120 -.037 10.657 1.00 13.03 C ATOM 15 NH1 ARG A 22 1.462 .617 9.712 1.00 13.03 N ATOM 16 NH2 ARG A 22 2.789 -1.121 10.331 1.00 13.03 N ATOM 17 N LYS A 23 -.238 5.173 16.412 1.00 11.92 N ATOM 18 CA LYS A 23 -.684 6.530 16.683 1.00 11.92 C ATOM 19 C LYS A 23 .462 7.500 16.446 1.00 11.92 C ATOM 20 O LYS A 23 1.535 7.330 17.042 1.00 11.92 O ATOM 21 CB LYS A 23 -1.183 6.682 18.130 1.00 12.16 C ATOM 22 CG LYS A 23 -1.499 8.154 18.401 1.00 12.16 C ATOM 23 CD LYS A 23 -1.959 8.342 19.814 1.00 12.16 C ATOM 24 CE LYS A 23 -3.413 7.920 19.959 1.00 12.16 C ATOM 25 NZ LYS A 23 -3.888 8.570 21.225 1.00 12.16 N ATOM 26 N ILE A 24 .207 8.515 15.612 1.00 11.72 N ATOM 27 CA ILE A 24 1.216 9.511 15.286 1.00 11.72 C ATOM 28 C ILE A 24 .708 10.911 15.583 1.00 11.72 C ATOM 29 O ILE A 24 -.442 11.241 15.305 1.00 11.72 O ATOM 30 CB ILE A 24 1.599 9.445 13.789 1.00 14.25 C ATOM 31 CG1 ILE A 24 2.253 8.099 13.472 1.00 14.25 C ATOM 32 CG2 ILE A 24 2.616 10.515 13.406 1.00 14.25 C ATOM 33 CD1 ILE A 24 2.282 7.758 11.988 1.00 14.25 C ATOM 34 N GLY A 25 1.557 11.707 16.225 1.00 9.64 N ATOM 35 CA GLY A 25 1.210 13.076 16.538 1.00 9.64 C ATOM 36 C GLY A 25 2.000 13.997 15.623 1.00 9.64 C ATOM 37 O GLY A 25 3.163 13.723 15.354 1.00 9.64 O ATOM 38 N ILE A 26 1.358 15.058 15.079 1.00 11.27 N ATOM 39 CA ILE A 26 2.065 16.011 14.200 1.00 11.27 C ATOM 40 C ILE A 26 1.871 17.401 14.770 1.00 11.27 C ATOM 41 O ILE A 26 .734 17.827 14.904 1.00 11.27 O ATOM 42 CB ILE A 26 1.569 15.987 12.749 1.00 11.51 C ATOM 43 CG1 ILE A 26 1.651 14.593 12.152 1.00 11.51 C ATOM 44 CG2 ILE A 26 2.427 16.911 11.899 1.00 11.51 C ATOM 45 CD1 ILE A 26 1.023 14.392 10.815 1.00 11.51 C ATOM 46 N ILE A 27 2.955 18.068 15.149 1.00 13.25 N ATOM 47 CA ILE A 27 2.911 19.395 15.732 1.00 13.25 C ATOM 48 C ILE A 27 3.328 20.404 14.666 1.00 13.25 C ATOM 49 O ILE A 27 4.491 20.406 14.248 1.00 13.25 O ATOM 50 CB ILE A 27 3.822 19.508 16.954 1.00 13.30 C ATOM 51 CG1 ILE A 27 3.458 18.412 17.966 1.00 13.30 C ATOM 52 CG2 ILE A 27 3.677 20.868 17.637 1.00 13.30 C ATOM 53 CD1 ILE A 27 4.346 18.353 19.165 1.00 13.30 C ATOM 54 N GLY A 28 2.374 21.224 14.233 1.00 13.63 N ATOM 55 CA GLY A 28 2.648 22.252 13.198 1.00 13.63 C ATOM 56 C GLY A 28 2.122 21.739 11.880 1.00 13.63 C ATOM 57 O GLY A 28 2.843 21.003 11.261 1.00 13.63 O ATOM 58 N LEU A 29 .901 22.046 11.495 1.00 15.23 N ATOM 59 CA LEU A 29 .292 21.589 10.282 1.00 15.23 C ATOM 60 C LEU A 29 .399 22.659 9.188 1.00 15.23 C ATOM 61 O LEU A 29 -.621 23.212 8.794 1.00 15.23 O ATOM 62 CB LEU A 29 -1.193 21.216 10.481 1.00 14.94 C ATOM 63 CG LEU A 29 -1.570 19.754 10.776 1.00 14.94 C ATOM 64 CD1 LEU A 29 -1.284 18.790 9.659 1.00 14.94 C ATOM 65 CD2 LEU A 29 -.799 19.262 12.016 1.00 14.94 C ATOM 66 N GLY A 30 1.595 22.924 8.725 1.00 15.54 N ATOM 67 CA GLY A 30 1.884 23.850 7.674 1.00 15.54 C ATOM 68 C GLY A 30 2.174 23.079 6.404 1.00 15.54 C ATOM 69 O GLY A 30 1.620 21.970 6.233 1.00 15.54 O ATOM 70 N ASN A 31 3.012 23.596 5.520 1.00 13.35 N ATOM 71 CA ASN A 31 3.298 22.889 4.279 1.00 13.35 C ATOM 72 C ASN A 31 3.898 21.513 4.535 1.00 13.35 C ATOM 73 O ASN A 31 3.502 20.579 3.877 1.00 13.35 O ATOM 74 CB ASN A 31 4.319 23.598 3.374 1.00 13.93 C ATOM 75 CG ASN A 31 3.783 24.968 2.970 1.00 13.93 C ATOM 76 OD1 ASN A 31 2.752 24.976 2.287 1.00 13.93 O ATOM 77 ND2 ASN A 31 4.445 26.054 3.330 1.00 13.93 N ATOM 78 N VAL A 32 4.865 21.424 5.408 1.00 13.75 N ATOM 79 CA VAL A 32 5.520 20.143 5.681 1.00 13.75 C ATOM 80 C VAL A 32 4.629 19.275 6.522 1.00 13.75 C ATOM 81 O VAL A 32 4.351 18.128 6.163 1.00 13.75 O ATOM 82 CB VAL A 32 6.847 20.384 6.408 1.00 12.57 C ATOM 83 CG1 VAL A 32 7.572 19.064 6.601 1.00 12.57 C ATOM 84 CG2 VAL A 32 7.744 21.283 5.613 1.00 12.57 C ATOM 85 N GLY A 33 4.100 19.746 7.642 1.00 12.43 N ATOM 86 CA GLY A 33 3.271 18.874 8.471 1.00 12.43 C ATOM 87 C GLY A 33 2.085 18.283 7.778 1.00 12.43 C ATOM 88 O GLY A 33 1.749 17.118 7.968 1.00 12.43 O ATOM 89 N ALA A 34 1.414 19.055 6.951 1.00 11.36 N ATOM 90 CA ALA A 34 .251 18.604 6.174 1.00 11.36 C ATOM 91 C ALA A 34 .647 17.647 5.107 1.00 11.36 C ATOM 92 O ALA A 34 -.121 16.687 4.800 1.00 11.36 O ATOM 93 CB ALA A 34 -.463 19.870 5.649 1.00 10.98 C ATOM 94 N ALA A 35 1.849 17.713 4.538 1.00 10.76 N ATOM 95 CA ALA A 35 2.330 16.749 3.537 1.00 10.76 C ATOM 96 C ALA A 35 2.675 15.434 4.233 1.00 10.76 C ATOM 97 O ALA A 35 2.478 14.347 3.665 1.00 10.76 O ATOM 98 CB ALA A 35 3.564 17.205 2.772 1.00 8.81 C ATOM 99 N VAL A 36 3.197 15.516 5.465 1.00 11.59 N ATOM 100 CA VAL A 36 3.504 14.317 6.289 1.00 11.59 C ATOM 101 C VAL A 36 2.202 13.585 6.530 1.00 11.59 C ATOM 102 O VAL A 36 2.088 12.377 6.294 1.00 11.59 O ATOM 103 CB VAL A 36 4.150 14.682 7.614 1.00 11.11 C ATOM 104 CG1 VAL A 36 4.256 13.500 8.551 1.00 11.11 C ATOM 105 CG2 VAL A 36 5.590 15.216 7.326 1.00 11.11 C ATOM 106 N ALA A 37 1.203 14.315 6.989 1.00 11.90 N ATOM 107 CA ALA A 37 -.125 13.745 7.248 1.00 11.90 C ATOM 108 C ALA A 37 -.699 13.160 6.004 1.00 11.90 C ATOM 109 O ALA A 37 -1.235 11.992 6.001 1.00 11.90 O ATOM 110 CB ALA A 37 -1.016 14.879 7.742 1.00 11.32 C ATOM 111 N HIS A 38 -.648 13.827 4.846 1.00 12.79 N ATOM 112 CA HIS A 38 -1.220 13.245 3.622 1.00 12.79 C ATOM 113 C HIS A 38 -.475 12.010 3.174 1.00 12.79 C ATOM 114 O HIS A 38 -1.067 11.022 2.662 1.00 12.79 O ATOM 115 CB HIS A 38 -1.245 14.341 2.536 1.00 12.58 C ATOM 116 CG HIS A 38 -2.041 13.936 1.325 1.00 12.58 C ATOM 117 ND1 HIS A 38 -1.882 14.541 .067 1.00 12.58 N ATOM 118 CD2 HIS A 38 -2.999 12.980 1.199 1.00 12.58 C ATOM 119 CE1 HIS A 38 -2.726 13.918 -.755 1.00 12.58 C ATOM 120 NE2 HIS A 38 -3.402 12.955 -.097 1.00 12.58 N ATOM 121 N GLY A 39 .830 11.996 3.310 1.00 13.48 N ATOM 122 CA GLY A 39 1.627 10.797 2.936 1.00 13.48 C ATOM 123 C GLY A 39 1.273 9.590 3.800 1.00 13.48 C ATOM 124 O GLY A 39 1.197 8.478 3.282 1.00 13.48 O ATOM 125 N LEU A 40 1.074 9.791 5.118 1.00 12.16 N ATOM 126 CA LEU A 40 .692 8.737 6.038 1.00 12.16 C ATOM 127 C LEU A 40 -.746 8.341 5.750 1.00 12.16 C ATOM 128 O LEU A 40 -.975 7.143 5.535 1.00 12.16 O ATOM 129 CB LEU A 40 .738 9.227 7.472 1.00 9.60 C ATOM 130 CG LEU A 40 2.150 9.538 8.000 1.00 9.60 C ATOM 131 CD1 LEU A 40 2.057 10.338 9.253 1.00 9.60 C ATOM 132 CD2 LEU A 40 2.894 8.229 8.232 1.00 9.60 C ATOM 133 N ILE A 41 -1.645 9.336 5.681 1.00 14.06 N ATOM 134 CA ILE A 41 -3.074 8.927 5.455 1.00 14.06 C ATOM 135 C ILE A 41 -3.324 8.256 4.139 1.00 14.06 C ATOM 136 O ILE A 41 -4.132 7.302 4.031 1.00 14.06 O ATOM 137 CB ILE A 41 -3.949 10.210 5.650 1.00 12.15 C ATOM 138 CG1 ILE A 41 -4.066 10.503 7.126 1.00 12.15 C ATOM 139 CG2 ILE A 41 -5.332 10.037 5.037 1.00 12.15 C ATOM 140 CD1 ILE A 41 -4.542 11.851 7.531 1.00 12.15 C ATOM 141 N ALA A 42 -2.634 8.663 3.065 1.00 16.97 N ATOM 142 CA ALA A 42 -2.797 8.083 1.739 1.00 16.97 C ATOM 143 C ALA A 42 -2.401 6.611 1.729 1.00 16.97 C ATOM 144 O ALA A 42 -2.973 5.797 1.008 1.00 16.97 O ATOM 145 CB ALA A 42 -1.984 8.917 .743 1.00 15.79 C ATOM 146 N GLN A 43 -1.414 6.194 2.511 1.00 19.98 N ATOM 147 CA GLN A 43 -1.035 4.790 2.565 1.00 19.98 C ATOM 148 C GLN A 43 -1.723 4.082 3.742 1.00 19.98 C ATOM 149 O GLN A 43 -1.536 2.865 3.919 1.00 19.98 O ATOM 150 CB GLN A 43 .460 4.612 2.759 1.00 23.69 C ATOM 151 CG GLN A 43 1.349 5.392 1.920 1.00 23.69 C ATOM 152 CD GLN A 43 2.811 5.311 2.329 1.00 23.69 C ATOM 153 OE1 GLN A 43 3.437 4.307 2.031 1.00 23.69 O ATOM 154 NE2 GLN A 43 3.291 6.384 2.943 1.00 23.69 N ATOM 155 N GLY A 44 -2.442 4.785 4.590 1.00 18.31 N ATOM 156 CA GLY A 44 -3.080 4.099 5.729 1.00 18.31 C ATOM 157 C GLY A 44 -2.037 3.577 6.689 1.00 18.31 C ATOM 158 O GLY A 44 -2.179 2.436 7.114 1.00 18.31 O ATOM 159 N VAL A 45 -1.031 4.350 7.004 1.00 15.91 N ATOM 160 CA VAL A 45 .033 3.905 7.880 1.00 15.91 C ATOM 161 C VAL A 45 -.395 3.829 9.345 1.00 15.91 C ATOM 162 O VAL A 45 -.077 2.831 9.978 1.00 15.91 O ATOM 163 CB VAL A 45 1.292 4.813 7.795 1.00 13.29 C ATOM 164 CG1 VAL A 45 2.338 4.374 8.802 1.00 13.29 C ATOM 165 CG2 VAL A 45 1.890 4.725 6.396 1.00 13.29 C ATOM 166 N ALA A 46 -1.034 4.849 9.881 1.00 12.24 N ATOM 167 CA ALA A 46 -1.434 4.878 11.262 1.00 12.24 C ATOM 168 C ALA A 46 -2.938 4.691 11.423 1.00 12.24 C ATOM 169 O ALA A 46 -3.699 4.700 10.465 1.00 12.24 O ATOM 170 CB ALA A 46 -1.033 6.202 11.914 1.00 11.35 C ATOM 171 N ASP A 47 -3.339 4.448 12.676 1.00 10.80 N ATOM 172 CA ASP A 47 -4.753 4.270 12.952 1.00 10.80 C ATOM 173 C ASP A 47 -5.298 5.566 13.496 1.00 10.80 C ATOM 174 O ASP A 47 -6.376 5.975 13.149 1.00 10.80 O ATOM 175 CB ASP A 47 -4.943 3.121 13.957 1.00 11.06 C ATOM 176 CG ASP A 47 -4.468 1.808 13.393 1.00 11.06 C ATOM 177 OD1 ASP A 47 -5.102 1.291 12.447 1.00 11.06 O ATOM 178 OD2 ASP A 47 -3.435 1.293 13.885 1.00 11.06 O ATOM 179 N ASP A 48 -4.556 6.206 14.398 1.00 11.80 N ATOM 180 CA ASP A 48 -4.927 7.420 15.080 1.00 11.80 C ATOM 181 C ASP A 48 -3.890 8.513 14.857 1.00 11.80 C ATOM 182 O ASP A 48 -2.690 8.246 14.954 1.00 11.80 O ATOM 183 CB ASP A 48 -5.049 7.182 16.590 1.00 15.59 C ATOM 184 CG ASP A 48 -6.059 6.128 16.953 1.00 15.59 C ATOM 185 OD1 ASP A 48 -7.231 6.142 16.522 1.00 15.59 O ATOM 186 OD2 ASP A 48 -5.697 5.169 17.686 1.00 15.59 O ATOM 187 N TYR A 49 -4.389 9.748 14.549 1.00 9.37 N ATOM 188 CA TYR A 49 -3.504 10.866 14.319 1.00 9.37 C ATOM 189 C TYR A 49 -3.899 12.024 15.222 1.00 9.37 C ATOM 190 O TYR A 49 -5.084 12.182 15.525 1.00 9.37 O ATOM 191 CB TYR A 49 -3.530 11.434 12.863 1.00 2.00 C ATOM 192 CG TYR A 49 -3.225 10.454 11.751 1.00 2.00 C ATOM 193 CD1 TYR A 49 -4.254 9.609 11.225 1.00 2.00 C ATOM 194 CD2 TYR A 49 -1.957 10.308 11.307 1.00 2.00 C ATOM 195 CE1 TYR A 49 -3.982 8.700 10.243 1.00 2.00 C ATOM 196 CE2 TYR A 49 -1.689 9.371 10.330 1.00 2.00 C ATOM 197 CZ TYR A 49 -2.686 8.614 9.792 1.00 2.00 C ATOM 198 OH TYR A 49 -2.348 7.711 8.769 1.00 2.00 O ATOM 199 N VAL A 50 -2.909 12.787 15.688 1.00 10.64 N ATOM 200 CA VAL A 50 -3.216 13.926 16.552 1.00 10.64 C ATOM 201 C VAL A 50 -2.586 15.127 15.853 1.00 10.64 C ATOM 202 O VAL A 50 -1.365 15.088 15.661 1.00 10.64 O ATOM 203 CB VAL A 50 -2.657 13.819 17.957 1.00 10.36 C ATOM 204 CG1 VAL A 50 -3.040 14.983 18.864 1.00 10.36 C ATOM 205 CG2 VAL A 50 -3.184 12.549 18.654 1.00 10.36 C ATOM 206 N PHE A 51 -3.419 16.109 15.452 1.00 11.52 N ATOM 207 CA PHE A 51 -2.858 17.284 14.729 1.00 11.52 C ATOM 208 C PHE A 51 -2.811 18.401 15.740 1.00 11.52 C ATOM 209 O PHE A 51 -3.808 18.576 16.439 1.00 11.52 O ATOM 210 CB PHE A 51 -3.685 17.710 13.541 1.00 12.35 C ATOM 211 CG PHE A 51 -3.715 16.817 12.334 1.00 12.35 C ATOM 212 CD1 PHE A 51 -2.881 15.719 12.247 1.00 12.35 C ATOM 213 CD2 PHE A 51 -4.573 17.037 11.259 1.00 12.35 C ATOM 214 CE1 PHE A 51 -2.912 14.831 11.195 1.00 12.35 C ATOM 215 CE2 PHE A 51 -4.581 16.149 10.195 1.00 12.35 C ATOM 216 CZ PHE A 51 -3.760 15.051 10.131 1.00 12.35 C ATOM 217 N ILE A 52 -1.707 19.084 15.897 1.00 12.91 N ATOM 218 CA ILE A 52 -1.625 20.177 16.854 1.00 12.91 C ATOM 219 C ILE A 52 -1.051 21.403 16.128 1.00 12.91 C ATOM 220 O ILE A 52 -.021 21.279 15.456 1.00 12.91 O ATOM 221 CB ILE A 52 -.732 19.849 18.072 1.00 14.51 C ATOM 222 CG1 ILE A 52 -1.375 18.747 18.939 1.00 14.51 C ATOM 223 CG2 ILE A 52 -.486 21.086 18.913 1.00 14.51 C ATOM 224 CD1 ILE A 52 -.638 18.275 20.151 1.00 14.51 C ATOM 225 N ASP A 53 -1.726 22.548 16.252 1.00 14.65 N ATOM 226 CA ASP A 53 -1.195 23.747 15.608 1.00 14.65 C ATOM 227 C ASP A 53 -1.645 24.957 16.402 1.00 14.65 C ATOM 228 O ASP A 53 -2.782 24.871 16.884 1.00 14.65 O ATOM 229 CB ASP A 53 -1.697 23.920 14.184 1.00 15.67 C ATOM 230 CG ASP A 53 -.824 24.844 13.362 1.00 15.67 C ATOM 231 OD1 ASP A 53 -.739 26.036 13.688 1.00 15.67 O ATOM 232 OD2 ASP A 53 -.155 24.371 12.437 1.00 15.67 O ATOM 233 N ALA A 54 -.832 25.970 16.511 1.00 18.17 N ATOM 234 CA ALA A 54 -1.184 27.167 17.257 1.00 18.17 C ATOM 235 C ALA A 54 -2.343 27.887 16.578 1.00 18.17 C ATOM 236 O ALA A 54 -3.229 28.524 17.203 1.00 18.17 O ATOM 237 CB ALA A 54 .041 28.064 17.356 1.00 15.54 C ATOM 238 N ASN A 55 -2.372 27.833 15.256 1.00 20.42 N ATOM 239 CA ASN A 55 -3.440 28.436 14.491 1.00 20.42 C ATOM 240 C ASN A 55 -4.585 27.451 14.463 1.00 20.42 C ATOM 241 O ASN A 55 -4.543 26.457 13.750 1.00 20.42 O ATOM 242 CB ASN A 55 -2.953 28.744 13.083 1.00 22.10 C ATOM 243 CG ASN A 55 -3.986 29.367 12.172 1.00 22.10 C ATOM 244 OD1 ASN A 55 -5.098 29.729 12.531 1.00 22.10 O ATOM 245 ND2 ASN A 55 -3.650 29.480 10.911 1.00 22.10 N ATOM 246 N GLU A 56 -5.595 27.727 15.269 1.00 24.09 N ATOM 247 CA GLU A 56 -6.752 26.846 15.375 1.00 24.09 C ATOM 248 C GLU A 56 -7.554 26.660 14.115 1.00 24.09 C ATOM 249 O GLU A 56 -7.858 25.524 13.746 1.00 24.09 O ATOM 250 CB GLU A 56 -7.726 27.421 16.423 1.00 31.60 C ATOM 251 CG GLU A 56 -7.140 27.381 17.788 1.00 31.60 C ATOM 252 CD GLU A 56 -7.888 26.487 18.779 1.00 31.60 C ATOM 253 OE1 GLU A 56 -9.156 26.463 18.712 1.00 31.60 O ATOM 254 OE2 GLU A 56 -7.155 25.869 19.629 1.00 31.60 O ATOM 255 N ALA A 57 -7.920 27.729 13.425 1.00 21.65 N ATOM 256 CA ALA A 57 -8.734 27.577 12.198 1.00 21.65 C ATOM 257 C ALA A 57 -8.022 26.744 11.152 1.00 21.65 C ATOM 258 O ALA A 57 -8.706 25.970 10.460 1.00 21.65 O ATOM 259 CB ALA A 57 -9.084 28.949 11.648 1.00 21.28 C ATOM 260 N LYS A 58 -6.710 26.845 11.016 1.00 19.24 N ATOM 261 CA LYS A 58 -5.962 26.082 10.037 1.00 19.24 C ATOM 262 C LYS A 58 -6.019 24.585 10.290 1.00 19.24 C ATOM 263 O LYS A 58 -6.341 23.790 9.419 1.00 19.24 O ATOM 264 CB LYS A 58 -4.476 26.440 10.045 1.00 20.22 C ATOM 265 CG LYS A 58 -3.709 26.400 8.780 1.00 20.22 C ATOM 266 CD LYS A 58 -4.007 25.229 7.871 1.00 20.22 C ATOM 267 CE LYS A 58 -3.004 25.127 6.734 1.00 20.22 C ATOM 268 NZ LYS A 58 -2.467 23.713 6.535 1.00 20.22 N ATOM 269 N VAL A 59 -5.689 24.187 11.528 1.00 19.32 N ATOM 270 CA VAL A 59 -5.676 22.761 11.857 1.00 19.32 C ATOM 271 C VAL A 59 -7.060 22.144 11.773 1.00 19.32 C ATOM 272 O VAL A 59 -7.245 21.017 11.277 1.00 19.32 O ATOM 273 CB VAL A 59 -5.028 22.567 13.245 1.00 18.23 C ATOM 274 CG1 VAL A 59 -5.946 22.914 14.383 1.00 18.23 C ATOM 275 CG2 VAL A 59 -4.611 21.113 13.323 1.00 18.23 C ATOM 276 N LYS A 60 -8.085 22.875 12.154 1.00 19.35 N ATOM 277 CA LYS A 60 -9.473 22.379 12.050 1.00 19.35 C ATOM 278 C LYS A 60 -9.857 22.250 10.599 1.00 19.35 C ATOM 279 O LYS A 60 -10.592 21.337 10.206 1.00 19.35 O ATOM 280 CB LYS A 60 -10.350 23.321 12.853 1.00 27.47 C ATOM 281 CG LYS A 60 -11.826 23.172 12.778 1.00 27.47 C ATOM 282 CD LYS A 60 -12.331 21.758 12.748 1.00 27.47 C ATOM 283 CE LYS A 60 -13.270 21.430 13.932 1.00 27.47 C ATOM 284 NZ LYS A 60 -12.877 20.141 14.669 1.00 27.47 N ATOM 285 N ALA A 61 -9.354 23.129 9.713 1.00 17.57 N ATOM 286 CA ALA A 61 -9.599 23.058 8.282 1.00 17.57 C ATOM 287 C ALA A 61 -9.020 21.807 7.670 1.00 17.57 C ATOM 288 O ALA A 61 -9.689 21.119 6.876 1.00 17.57 O ATOM 289 CB ALA A 61 -8.956 24.242 7.545 1.00 17.55 C ATOM 290 N ASP A 62 -7.787 21.478 8.067 1.00 17.73 N ATOM 291 CA ASP A 62 -7.115 20.263 7.602 1.00 17.73 C ATOM 292 C ASP A 62 -7.766 18.995 8.152 1.00 17.73 C ATOM 293 O ASP A 62 -7.857 17.967 7.471 1.00 17.73 O ATOM 294 CB ASP A 62 -5.631 20.263 8.010 1.00 19.91 C ATOM 295 CG ASP A 62 -4.790 21.086 7.072 1.00 19.91 C ATOM 296 OD1 ASP A 62 -5.080 21.165 5.842 1.00 19.91 O ATOM 297 OD2 ASP A 62 -3.798 21.706 7.468 1.00 19.91 O ATOM 298 N GLN A 63 -8.237 19.021 9.404 1.00 15.66 N ATOM 299 CA GLN A 63 -8.911 17.862 9.979 1.00 15.66 C ATOM 300 C GLN A 63 -10.148 17.510 9.178 1.00 15.66 C ATOM 301 O GLN A 63 -10.315 16.364 8.752 1.00 15.66 O ATOM 302 CB GLN A 63 -9.315 18.198 11.422 1.00 16.11 C ATOM 303 CG GLN A 63 -10.196 17.098 11.964 1.00 16.11 C ATOM 304 CD GLN A 63 -10.721 17.368 13.342 1.00 16.11 C ATOM 305 OE1 GLN A 63 -11.154 18.475 13.644 1.00 16.11 O ATOM 306 NE2 GLN A 63 -10.763 16.330 14.165 1.00 16.11 N ATOM 307 N ILE A 64 -11.009 18.502 8.953 1.00 14.64 N ATOM 308 CA ILE A 64 -12.241 18.302 8.184 1.00 14.64 C ATOM 309 C ILE A 64 -11.967 17.851 6.751 1.00 14.64 C ATOM 310 O ILE A 64 -12.597 16.948 6.200 1.00 14.64 O ATOM 311 CB ILE A 64 -13.079 19.579 8.102 1.00 17.40 C ATOM 312 CG1 ILE A 64 -13.457 20.182 9.461 1.00 17.40 C ATOM 313 CG2 ILE A 64 -14.371 19.260 7.339 1.00 17.40 C ATOM 314 CD1 ILE A 64 -14.357 19.224 10.252 1.00 17.40 C ATOM 315 N ASP A 65 -11.025 18.494 6.099 1.00 14.05 N ATOM 316 CA ASP A 65 -10.686 18.159 4.698 1.00 14.05 C ATOM 317 C ASP A 65 -10.226 16.740 4.600 1.00 14.05 C ATOM 318 O ASP A 65 -10.606 16.045 3.648 1.00 14.05 O ATOM 319 CB ASP A 65 -9.651 19.174 4.194 1.00 14.22 C ATOM 320 CG ASP A 65 -9.500 19.222 2.694 1.00 14.22 C ATOM 321 OD1 ASP A 65 -10.389 18.725 1.956 1.00 14.22 O ATOM 322 OD2 ASP A 65 -8.477 19.747 2.226 1.00 14.22 O ATOM 323 N PHE A 66 -9.456 16.248 5.578 1.00 12.92 N ATOM 324 CA PHE A 66 -9.017 14.834 5.629 1.00 12.92 C ATOM 325 C PHE A 66 -10.173 13.896 5.951 1.00 12.92 C ATOM 326 O PHE A 66 -10.333 12.822 5.345 1.00 12.92 O ATOM 327 CB PHE A 66 -7.918 14.632 6.665 1.00 9.14 C ATOM 328 CG PHE A 66 -6.535 14.916 6.134 1.00 9.14 C ATOM 329 CD1 PHE A 66 -6.029 14.226 5.077 1.00 9.14 C ATOM 330 CD2 PHE A 66 -5.728 15.856 6.781 1.00 9.14 C ATOM 331 CE1 PHE A 66 -4.761 14.517 4.572 1.00 9.14 C ATOM 332 CE2 PHE A 66 -4.461 16.138 6.301 1.00 9.14 C ATOM 333 CZ PHE A 66 -3.981 15.445 5.223 1.00 9.14 C ATOM 334 N GLN A 67 -11.056 14.325 6.851 1.00 13.69 N ATOM 335 CA GLN A 67 -12.233 13.540 7.187 1.00 13.69 C ATOM 336 C GLN A 67 -13.206 13.454 6.044 1.00 13.69 C ATOM 337 O GLN A 67 -13.989 12.483 5.960 1.00 13.69 O ATOM 338 CB GLN A 67 -12.943 14.153 8.413 1.00 15.57 C ATOM 339 CG GLN A 67 -12.089 14.081 9.648 1.00 15.57 C ATOM 340 CD GLN A 67 -12.757 14.662 10.860 1.00 15.57 C ATOM 341 OE1 GLN A 67 -12.483 14.202 12.028 1.00 15.57 O ATOM 342 NE2 GLN A 67 -13.594 15.663 10.721 1.00 15.57 N