Header list of 1b8t.pdb file
Complete list - v 3 2 Bytes
HEADER CONTRACTILE 02-FEB-99 1B8T TITLE SOLUTION STRUCTURE OF THE CHICKEN CRP1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (CRP1); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIM-DOMAIN PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 TISSUE: MUSCLE; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET5; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET5 KEYWDS LIM DOMAIN, CRP, MUSCLE DIFFERENTIATION, CONTRACTILE EXPDTA SOLUTION NMR NUMMDL 37 AUTHOR X.YAO,G.C.PEREZ-ALVARADO,H.A.LOUIS,P.POMIES,C.HATT,M.F.SUMMERS, AUTHOR 2 M.C.BECKERLE REVDAT 3 03-NOV-21 1B8T 1 REMARK REVDAT 2 24-FEB-09 1B8T 1 VERSN REVDAT 1 06-MAY-99 1B8T 0 JRNL AUTH X.YAO,G.C.PEREZ-ALVARADO,H.A.LOUIS,P.POMIES,C.HATT, JRNL AUTH 2 M.F.SUMMERS,M.C.BECKERLE JRNL TITL SOLUTION STRUCTURE OF THE CHICKEN CYSTEINE-RICH PROTEIN, JRNL TITL 2 CRP1, A DOUBLE-LIM PROTEIN IMPLICATED IN MUSCLE JRNL TITL 3 DIFFERENTIATION. JRNL REF BIOCHEMISTRY V. 38 5701 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10231520 JRNL DOI 10.1021/BI982036Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT, BRAUN AND WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1B8T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-99. REMARK 100 THE DEPOSITION ID IS D_1000000432. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; NOESY; COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : OMEGA PSG REMARK 210 SPECTROMETER MANUFACTURER : GE REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW REMARK 210 METHOD USED : DYANA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 37 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 37 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR DATA ON THE REMARK 210 TWO INDIVIDUAL DOMAINS OF CRP1 AND N15-EDITED NOESY AND TOCSY REMARK 210 DATA ON N15-LABELED CRP1. REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 ASN A 3 154.67 179.01 REMARK 500 1 TRP A 4 -63.91 -176.52 REMARK 500 1 VAL A 12 -66.19 -95.13 REMARK 500 1 GLN A 14 28.29 83.76 REMARK 500 1 TYR A 18 48.50 -81.40 REMARK 500 1 PHE A 19 86.98 46.32 REMARK 500 1 ALA A 20 -53.44 -148.04 REMARK 500 1 GLU A 21 -53.80 -129.71 REMARK 500 1 GLU A 22 69.70 35.97 REMARK 500 1 GLU A 26 108.32 -38.91 REMARK 500 1 PHE A 35 85.73 -66.73 REMARK 500 1 VAL A 39 -70.89 -101.78 REMARK 500 1 LYS A 41 23.35 82.99 REMARK 500 1 THR A 47 -161.66 -66.92 REMARK 500 1 LYS A 59 -72.37 -39.51 REMARK 500 1 LYS A 69 -63.98 -104.98 REMARK 500 1 LEU A 80 147.52 -172.14 REMARK 500 1 ASP A 83 140.00 179.56 REMARK 500 1 GLU A 86 126.54 -178.19 REMARK 500 1 SER A 87 137.63 -179.44 REMARK 500 1 GLN A 110 141.46 179.14 REMARK 500 1 LYS A 111 131.44 -176.80 REMARK 500 1 SER A 115 164.77 56.98 REMARK 500 1 GLN A 123 -173.91 -57.60 REMARK 500 1 TYR A 126 89.43 -167.13 REMARK 500 1 ALA A 127 170.42 64.25 REMARK 500 1 ALA A 128 -55.57 78.11 REMARK 500 1 GLU A 129 53.46 -148.79 REMARK 500 1 PHE A 143 96.57 -34.80 REMARK 500 1 ALA A 146 33.39 -88.14 REMARK 500 1 LYS A 147 -46.97 -135.46 REMARK 500 1 GLU A 153 -67.16 -134.42 REMARK 500 1 SER A 154 -64.49 -168.98 REMARK 500 1 ASN A 173 -39.20 -39.49 REMARK 500 1 SER A 191 132.87 -174.35 REMARK 500 2 VAL A 12 -66.40 -94.40 REMARK 500 2 GLN A 14 28.56 83.14 REMARK 500 2 PHE A 19 173.30 52.40 REMARK 500 2 ALA A 20 -61.85 73.27 REMARK 500 2 GLU A 22 126.67 -38.87 REMARK 500 2 GLU A 26 102.57 -40.03 REMARK 500 2 PHE A 35 90.87 -67.98 REMARK 500 2 VAL A 39 -75.38 -98.33 REMARK 500 2 SER A 46 178.72 76.74 REMARK 500 2 THR A 47 -148.95 -62.93 REMARK 500 2 THR A 48 18.56 54.60 REMARK 500 2 HIS A 52 109.41 -168.56 REMARK 500 2 LYS A 59 -72.66 -39.23 REMARK 500 2 GLU A 86 159.15 179.41 REMARK 500 2 ASP A 116 -151.15 -152.91 REMARK 500 REMARK 500 THIS ENTRY HAS 1409 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 193 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 10 SG REMARK 620 2 CYS A 13 SG 91.0 REMARK 620 3 HIS A 31 ND1 89.5 93.4 REMARK 620 4 CYS A 34 SG 127.1 116.1 129.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 194 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 37 SG REMARK 620 2 CYS A 40 SG 86.6 REMARK 620 3 CYS A 58 SG 112.7 142.9 REMARK 620 4 CYS A 61 SG 105.6 119.0 87.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 195 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 118 SG REMARK 620 2 CYS A 121 SG 88.4 REMARK 620 3 HIS A 139 ND1 87.3 87.7 REMARK 620 4 CYS A 142 SG 131.3 131.4 116.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 196 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 145 SG REMARK 620 2 CYS A 148 SG 93.1 REMARK 620 3 CYS A 166 SG 119.8 103.5 REMARK 620 4 CYS A 169 SG 104.1 144.0 95.1 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 193 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 194 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 195 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 196 DBREF 1B8T A 1 192 UNP P67966 CSRP1_CHICK 1 192 SEQRES 1 A 192 MET PRO ASN TRP GLY GLY GLY LYS LYS CYS GLY VAL CYS SEQRES 2 A 192 GLN LYS ALA VAL TYR PHE ALA GLU GLU VAL GLN CYS GLU SEQRES 3 A 192 GLY SER SER PHE HIS LYS SER CYS PHE LEU CYS MET VAL SEQRES 4 A 192 CYS LYS LYS ASN LEU ASP SER THR THR VAL ALA VAL HIS SEQRES 5 A 192 GLY ASP GLU ILE TYR CYS LYS SER CYS TYR GLY LYS LYS SEQRES 6 A 192 TYR GLY PRO LYS GLY LYS GLY LYS GLY MET GLY ALA GLY SEQRES 7 A 192 THR LEU SER THR ASP LYS GLY GLU SER LEU GLY ILE LYS SEQRES 8 A 192 TYR GLU GLU GLY GLN SER HIS ARG PRO THR ASN PRO ASN SEQRES 9 A 192 ALA SER ARG MET ALA GLN LYS VAL GLY GLY SER ASP GLY SEQRES 10 A 192 CYS PRO ARG CYS GLY GLN ALA VAL TYR ALA ALA GLU LYS SEQRES 11 A 192 VAL ILE GLY ALA GLY LYS SER TRP HIS LYS SER CYS PHE SEQRES 12 A 192 ARG CYS ALA LYS CYS GLY LYS SER LEU GLU SER THR THR SEQRES 13 A 192 LEU ALA ASP LYS ASP GLY GLU ILE TYR CYS LYS GLY CYS SEQRES 14 A 192 TYR ALA LYS ASN PHE GLY PRO LYS GLY PHE GLY PHE GLY SEQRES 15 A 192 GLN GLY ALA GLY ALA LEU ILE HIS SER GLN HET ZN A 193 1 HET ZN A 194 1 HET ZN A 195 1 HET ZN A 196 1 HETNAM ZN ZINC ION FORMUL 2 ZN 4(ZN 2+) HELIX 1 1 LYS A 59 GLY A 67 1 9 HELIX 2 2 LYS A 167 PHE A 174 1 8 SHEET 1 A 2 VAL A 23 CYS A 25 0 SHEET 2 A 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 B 2 VAL A 49 HIS A 52 0 SHEET 2 B 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 C 2 LYS A 130 GLY A 133 0 SHEET 2 C 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 D 2 LEU A 157 LYS A 160 0 SHEET 2 D 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 E 2 VAL A 23 CYS A 25 0 SHEET 2 E 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 F 2 VAL A 49 HIS A 52 0 SHEET 2 F 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 G 2 LYS A 130 GLY A 133 0 SHEET 2 G 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 H 2 LEU A 157 LYS A 160 0 SHEET 2 H 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 I 2 VAL A 23 CYS A 25 0 SHEET 2 I 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 J 2 VAL A 49 HIS A 52 0 SHEET 2 J 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 K 2 VAL A 131 GLY A 133 0 SHEET 2 K 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 L 2 LEU A 157 LYS A 160 0 SHEET 2 L 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 M 2 VAL A 23 CYS A 25 0 SHEET 2 M 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 N 2 VAL A 49 HIS A 52 0 SHEET 2 N 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 O 2 VAL A 131 GLY A 133 0 SHEET 2 O 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 P 2 LEU A 157 LYS A 160 0 SHEET 2 P 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 Q 2 GLU A 22 CYS A 25 0 SHEET 2 Q 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 R 2 VAL A 49 HIS A 52 0 SHEET 2 R 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 S 2 VAL A 131 GLY A 133 0 SHEET 2 S 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 T 2 LEU A 157 LYS A 160 0 SHEET 2 T 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 U 2 VAL A 23 CYS A 25 0 SHEET 2 U 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 V 2 VAL A 49 HIS A 52 0 SHEET 2 V 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 W 2 VAL A 131 GLY A 133 0 SHEET 2 W 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 X 2 LEU A 157 LYS A 160 0 SHEET 2 X 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 Y 2 VAL A 23 CYS A 25 0 SHEET 2 Y 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 Z 2 VAL A 49 HIS A 52 0 SHEET 2 Z 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AA 2 VAL A 131 GLY A 133 0 SHEET 2 AA 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 AB 2 LEU A 157 LYS A 160 0 SHEET 2 AB 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AC 2 GLU A 22 CYS A 25 0 SHEET 2 AC 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 AD 2 VAL A 49 HIS A 52 0 SHEET 2 AD 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AE 2 VAL A 131 GLY A 133 0 SHEET 2 AE 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 AF 2 LEU A 157 LYS A 160 0 SHEET 2 AF 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AG 2 GLU A 22 CYS A 25 0 SHEET 2 AG 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 AH 2 VAL A 49 HIS A 52 0 SHEET 2 AH 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AI 2 VAL A 131 GLY A 133 0 SHEET 2 AI 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 AJ 2 LEU A 157 LYS A 160 0 SHEET 2 AJ 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AK 2 GLU A 22 CYS A 25 0 SHEET 2 AK 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 AL 2 VAL A 49 HIS A 52 0 SHEET 2 AL 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AM 2 VAL A 131 GLY A 133 0 SHEET 2 AM 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 AN 2 LEU A 157 LYS A 160 0 SHEET 2 AN 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AO 2 VAL A 23 CYS A 25 0 SHEET 2 AO 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 AP 2 VAL A 49 HIS A 52 0 SHEET 2 AP 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AQ 2 LYS A 130 GLY A 133 0 SHEET 2 AQ 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 AR 2 LEU A 157 LYS A 160 0 SHEET 2 AR 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AS 2 VAL A 23 CYS A 25 0 SHEET 2 AS 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 AT 2 VAL A 49 HIS A 52 0 SHEET 2 AT 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AU 2 LYS A 130 GLY A 133 0 SHEET 2 AU 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 AV 2 LEU A 157 LYS A 160 0 SHEET 2 AV 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 AW 2 VAL A 23 CYS A 25 0 SHEET 2 AW 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 AX 2 VAL A 49 HIS A 52 0 SHEET 2 AX 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 AY 2 VAL A 131 GLY A 133 0 SHEET 2 AY 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 AZ 2 LEU A 157 LYS A 160 0 SHEET 2 AZ 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BA 2 VAL A 23 CYS A 25 0 SHEET 2 BA 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 BB 2 VAL A 49 HIS A 52 0 SHEET 2 BB 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BC 2 VAL A 131 GLY A 133 0 SHEET 2 BC 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 BD 2 LEU A 157 LYS A 160 0 SHEET 2 BD 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BE 2 GLU A 22 CYS A 25 0 SHEET 2 BE 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 BF 2 VAL A 49 HIS A 52 0 SHEET 2 BF 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BG 2 VAL A 131 GLY A 133 0 SHEET 2 BG 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 BH 2 LEU A 157 LYS A 160 0 SHEET 2 BH 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BI 2 VAL A 23 CYS A 25 0 SHEET 2 BI 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 BJ 2 VAL A 49 HIS A 52 0 SHEET 2 BJ 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BK 2 VAL A 131 GLY A 133 0 SHEET 2 BK 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 BL 2 LEU A 157 LYS A 160 0 SHEET 2 BL 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BM 2 VAL A 23 CYS A 25 0 SHEET 2 BM 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 BN 2 VAL A 49 HIS A 52 0 SHEET 2 BN 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BO 2 LYS A 130 GLY A 133 0 SHEET 2 BO 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 BP 2 LEU A 157 LYS A 160 0 SHEET 2 BP 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BQ 2 VAL A 23 CYS A 25 0 SHEET 2 BQ 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 BR 2 VAL A 49 HIS A 52 0 SHEET 2 BR 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BS 2 VAL A 131 GLY A 133 0 SHEET 2 BS 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 BT 2 LEU A 157 LYS A 160 0 SHEET 2 BT 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BU 2 GLU A 22 CYS A 25 0 SHEET 2 BU 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 BV 2 VAL A 49 HIS A 52 0 SHEET 2 BV 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 BW 2 LYS A 130 GLY A 133 0 SHEET 2 BW 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 BX 2 LEU A 157 LYS A 160 0 SHEET 2 BX 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 BY 2 GLU A 22 CYS A 25 0 SHEET 2 BY 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 BZ 2 VAL A 49 HIS A 52 0 SHEET 2 BZ 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CA 2 VAL A 131 GLY A 133 0 SHEET 2 CA 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 CB 2 LEU A 157 LYS A 160 0 SHEET 2 CB 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CC 2 VAL A 23 CYS A 25 0 SHEET 2 CC 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 CD 2 VAL A 49 HIS A 52 0 SHEET 2 CD 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CE 2 LYS A 130 GLY A 133 0 SHEET 2 CE 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 CF 2 LEU A 157 LYS A 160 0 SHEET 2 CF 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CG 2 VAL A 23 CYS A 25 0 SHEET 2 CG 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 CH 2 VAL A 49 HIS A 52 0 SHEET 2 CH 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CI 2 LYS A 130 GLY A 133 0 SHEET 2 CI 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 CJ 2 LEU A 157 LYS A 160 0 SHEET 2 CJ 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CK 2 VAL A 23 CYS A 25 0 SHEET 2 CK 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 CL 2 VAL A 49 HIS A 52 0 SHEET 2 CL 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CM 2 VAL A 131 GLY A 133 0 SHEET 2 CM 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 CN 2 LEU A 157 LYS A 160 0 SHEET 2 CN 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CO 2 GLY A 114 GLY A 117 0 SHEET 2 CO 2 ALA A 124 TYR A 126 -1 N VAL A 125 O SER A 115 SHEET 1 CP 2 GLU A 22 CYS A 25 0 SHEET 2 CP 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 CQ 2 VAL A 49 HIS A 52 0 SHEET 2 CQ 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CR 2 VAL A 131 GLY A 133 0 SHEET 2 CR 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 CS 2 LEU A 157 LYS A 160 0 SHEET 2 CS 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CT 2 VAL A 23 CYS A 25 0 SHEET 2 CT 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 CU 2 VAL A 49 HIS A 52 0 SHEET 2 CU 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 CV 2 SER A 115 GLY A 117 0 SHEET 2 CV 2 ALA A 124 TYR A 126 -1 N VAL A 125 O ASP A 116 SHEET 1 CW 2 VAL A 131 GLY A 133 0 SHEET 2 CW 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 CX 2 LEU A 157 LYS A 160 0 SHEET 2 CX 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 CY 2 VAL A 23 CYS A 25 0 SHEET 2 CY 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 CZ 2 VAL A 49 HIS A 52 0 SHEET 2 CZ 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DA 2 LYS A 130 GLY A 133 0 SHEET 2 DA 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 DB 2 LEU A 157 LYS A 160 0 SHEET 2 DB 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 DC 2 GLU A 22 CYS A 25 0 SHEET 2 DC 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 DD 2 VAL A 49 HIS A 52 0 SHEET 2 DD 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DE 2 VAL A 131 GLY A 133 0 SHEET 2 DE 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 DF 2 LEU A 157 LYS A 160 0 SHEET 2 DF 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 DG 2 VAL A 23 CYS A 25 0 SHEET 2 DG 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 DH 2 VAL A 49 HIS A 52 0 SHEET 2 DH 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DI 2 LYS A 130 GLY A 133 0 SHEET 2 DI 2 LYS A 136 HIS A 139 -1 N TRP A 138 O VAL A 131 SHEET 1 DJ 2 LEU A 157 LYS A 160 0 SHEET 2 DJ 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 DK 2 VAL A 23 CYS A 25 0 SHEET 2 DK 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 DL 2 VAL A 49 HIS A 52 0 SHEET 2 DL 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DM 2 VAL A 131 GLY A 133 0 SHEET 2 DM 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 DN 2 LEU A 157 LYS A 160 0 SHEET 2 DN 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 DO 2 GLU A 22 CYS A 25 0 SHEET 2 DO 2 SER A 28 HIS A 31 -1 N PHE A 30 O VAL A 23 SHEET 1 DP 2 VAL A 49 HIS A 52 0 SHEET 2 DP 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DQ 2 VAL A 131 GLY A 133 0 SHEET 2 DQ 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 DR 2 LEU A 157 LYS A 160 0 SHEET 2 DR 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 SHEET 1 DS 2 VAL A 23 CYS A 25 0 SHEET 2 DS 2 SER A 28 PHE A 30 -1 N PHE A 30 O VAL A 23 SHEET 1 DT 2 VAL A 49 HIS A 52 0 SHEET 2 DT 2 GLU A 55 CYS A 58 -1 N TYR A 57 O ALA A 50 SHEET 1 DU 2 VAL A 131 GLY A 133 0 SHEET 2 DU 2 LYS A 136 TRP A 138 -1 N TRP A 138 O VAL A 131 SHEET 1 DV 2 LEU A 157 LYS A 160 0 SHEET 2 DV 2 GLU A 163 CYS A 166 -1 N TYR A 165 O ALA A 158 LINK SG CYS A 10 ZN ZN A 193 1555 1555 2.30 LINK SG CYS A 13 ZN ZN A 193 1555 1555 2.36 LINK ND1 HIS A 31 ZN ZN A 193 1555 1555 2.04 LINK SG CYS A 34 ZN ZN A 193 1555 1555 2.35 LINK SG CYS A 37 ZN ZN A 194 1555 1555 2.30 LINK SG CYS A 40 ZN ZN A 194 1555 1555 2.36 LINK SG CYS A 58 ZN ZN A 194 1555 1555 2.27 LINK SG CYS A 61 ZN ZN A 194 1555 1555 2.36 LINK SG CYS A 118 ZN ZN A 195 1555 1555 2.30 LINK SG CYS A 121 ZN ZN A 195 1555 1555 2.38 LINK ND1 HIS A 139 ZN ZN A 195 1555 1555 2.07 LINK SG CYS A 142 ZN ZN A 195 1555 1555 2.38 LINK SG CYS A 145 ZN ZN A 196 1555 1555 2.30 LINK SG CYS A 148 ZN ZN A 196 1555 1555 2.34 LINK SG CYS A 166 ZN ZN A 196 1555 1555 2.33 LINK SG CYS A 169 ZN ZN A 196 1555 1555 2.36 SITE 1 AC1 4 CYS A 10 CYS A 13 HIS A 31 CYS A 34 SITE 1 AC2 4 CYS A 37 CYS A 40 CYS A 58 CYS A 61 SITE 1 AC3 4 CYS A 118 CYS A 121 HIS A 139 CYS A 142 SITE 1 AC4 4 CYS A 145 CYS A 148 CYS A 166 CYS A 169 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
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