Header list of 1fm1.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 15-AUG-00 1FM1
TITLE SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN COLLAGENASE-3
TITLE 2 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLLAGENASE-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC FRAGMENT;
COMPND 5 SYNONYM: MMP-13;
COMPND 6 EC: 3.4.24.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: HYDROXAMIC ACID INHIBITOR COMPLEX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPROMMP-13
KEYWDS MATRIX METALLOPROTEINASE, HYDROXAMIC ACID, HUMAN COLLAGENASE-3, MMP-
KEYWDS 2 13, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR F.J.MOY,P.K.CHANDA,J.M.CHEN,S.COSMI,W.EDRIS,J.I.LEVIN,R.POWERS
REVDAT 3 23-FEB-22 1FM1 1 REMARK LINK
REVDAT 2 24-FEB-09 1FM1 1 VERSN
REVDAT 1 15-AUG-01 1FM1 0
JRNL AUTH F.J.MOY,P.K.CHANDA,J.M.CHEN,S.COSMI,W.EDRIS,J.I.LEVIN,
JRNL AUTH 2 R.POWERS
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT
JRNL TITL 2 OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED WITH A HYDROXAMIC
JRNL TITL 3 ACID INHIBITOR.
JRNL REF J.MOL.BIOL. V. 302 671 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10986126
JRNL DOI 10.1006/JMBI.2000.4082
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MOY,P.K.CHANDA,S.COSMI,W.EDRIS,J.I.LEVIN,R.POWERS
REMARK 1 TITL 1H, 15N, 13C, AND 13CO ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF COLLAGENASE-3 (MMP-13) COMPLEXED WITH A
REMARK 1 TITL 3 HYDROXAMIC ACID INHIBITOR
REMARK 1 REF J.BIOMOL.NMR V. 17 269 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008305025043
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.84
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES CALCULATED WERE BASED ON
REMARK 3 3280 EXPERIMENTAL NMR RESTRAINTS, CONSISTING OF 2415 APPROXIMATE
REMARK 3 INTERPROTON DISTANCE RESTRAINTS, 47 DISTANCE RESTRAINTS BETWEEN
REMARK 3 MMP-13 AND WAY-151693, 5 INTRAMOLECULAR DISTANCE RESTRAINTS FOR
REMARK 3 WAY-151693, 88 DISTANCE RESTRAINTS FOR 44 BACKBONE HYDROGEN
REMARK 3 BONDS, 391 TORSION ANGLE RESTRAINTS, 103 3JNHA RESTRAINTS 123 CA
REMARK 3 RESTRAINTS AND 108 CB RESTRAINTS. THE STRUCTURE WAS ALSO REFINED
REMARK 3 USING A CONFORMATIONAL DATABASE.
REMARK 4
REMARK 4 1FM1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011701.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10 MM DEUTERATED TRIS-BASE, 100
REMARK 210 MM NACL, 5 MM CACL2, 0.1 MM
REMARK 210 ZNCL2, 2 MM NAN3, 10 MM
REMARK 210 DEUTERATED DTT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM OF U-15N,13C MMP-13 IN AN
REMARK 210 EQUIMOLAR COMPLEX WITH WAY-
REMARK 210 151693 IN A BUFFER CONTAINING 10
REMARK 210 MM DEUTERATED TRIS-BASE, 100 MM
REMARK 210 NACL, 5 MM CACL2, 0.1 MM ZNCL2,
REMARK 210 2 MM NAN3, 10 MM DEUTERATED DTT,
REMARK 210 IN 100% D2O AT PH 6.5 AND 35C; 1
REMARK 210 MM OF U-15N,13C MMP-13 IN AN
REMARK 210 EQUIMOLAR COMPLEX WITH WAY-
REMARK 210 151693 IN A BUFFER CONTAINING 10
REMARK 210 MM DEUTERATED TRIS-BASE, 100 MM
REMARK 210 NACL, 5 MM CACL2, 0.1 MM ZNCL2,
REMARK 210 2 MM NAN3, 10 MM DEUTERATED DTT,
REMARK 210 IN 90% H2O, 10% D2O AT PH 6.5
REMARK 210 AND 35C; 1 MM OF U-15N MMP-13 IN
REMARK 210 AN EQUIMOLAR COMPLEX WITH WAY-
REMARK 210 151693 IN A BUFFER CONTAINING 10
REMARK 210 MM DEUTERATED TRIS-BASE, 100 MM
REMARK 210 NACL, 5 MM CACL2, 0.1 MM ZNCL2,
REMARK 210 2 MM NAN3, 10 MM DEUTERATED DTT,
REMARK 210 IN 90% H2O, 10% D2O AT PH 6.5
REMARK 210 AND 35C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_C13-
REMARK 210 EDITED/FILTERED-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-2
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, X-PLOR 3.84, PIPP
REMARK 210 4.2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE AND
REMARK 210 ISOTOPE FILTERED NMR SPECTROSCOPY.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 TYR A 1
REMARK 465 ASN A 2
REMARK 465 VAL A 3
REMARK 465 PHE A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 PRO A 165
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 O ASP A 99 HE1 TRP A 104 1.52
REMARK 500 OD1 ASP A 128 H HIS A 129 1.55
REMARK 500 HH11 ARG A 18 O GLY A 56 1.55
REMARK 500 OD1 ASP A 132 H GLY A 134 1.58
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 TYR A 22 -167.39 -102.12
REMARK 500 1 LYS A 67 -94.86 -29.92
REMARK 500 1 HIS A 69 9.87 -153.01
REMARK 500 1 PRO A 74 -148.16 -60.98
REMARK 500 1 PRO A 87 161.92 -44.81
REMARK 500 1 PRO A 90 37.44 -70.70
REMARK 500 1 ASN A 91 -130.13 -158.54
REMARK 500 1 HIS A 148 33.05 -154.08
REMARK 500 1 PRO A 152 -179.05 -65.10
REMARK 500 2 TYR A 22 -160.39 -102.71
REMARK 500 2 LYS A 67 -78.97 -15.04
REMARK 500 2 TYR A 73 51.27 -172.30
REMARK 500 2 PRO A 74 160.91 -41.61
REMARK 500 2 PRO A 90 -76.50 -60.44
REMARK 500 2 PRO A 139 14.19 -63.41
REMARK 500 2 SER A 147 -93.13 -176.86
REMARK 500 3 TYR A 22 -161.08 -103.42
REMARK 500 3 PRO A 47 20.54 -72.93
REMARK 500 3 LYS A 67 -78.76 -38.52
REMARK 500 3 PHE A 72 43.65 -73.64
REMARK 500 3 PRO A 87 167.15 -49.67
REMARK 500 3 PRO A 88 73.83 -61.61
REMARK 500 3 PRO A 90 -147.41 -56.04
REMARK 500 3 HIS A 148 29.45 -143.41
REMARK 500 4 PRO A 24 -3.05 -59.22
REMARK 500 4 LYS A 67 -98.01 -17.96
REMARK 500 4 HIS A 69 33.27 -152.89
REMARK 500 4 PRO A 74 -152.67 -60.28
REMARK 500 4 PRO A 90 -153.49 -61.44
REMARK 500 4 MET A 137 24.72 -70.50
REMARK 500 4 PRO A 139 -19.80 -49.55
REMARK 500 4 HIS A 148 27.70 -144.18
REMARK 500 4 PRO A 152 -179.42 -67.81
REMARK 500 5 THR A 23 142.53 -39.86
REMARK 500 5 LYS A 67 -76.48 -21.45
REMARK 500 5 PHE A 72 52.57 -69.75
REMARK 500 5 PRO A 78 -73.19 -74.29
REMARK 500 5 PRO A 88 77.55 -56.29
REMARK 500 5 PRO A 90 -145.90 -57.47
REMARK 500 5 MET A 137 20.88 -69.92
REMARK 500 5 SER A 147 -51.43 -179.78
REMARK 500 6 PRO A 24 -6.94 -57.80
REMARK 500 6 LYS A 67 -77.82 -22.34
REMARK 500 6 PRO A 74 -151.55 -74.12
REMARK 500 6 PRO A 78 -75.11 -73.91
REMARK 500 6 PRO A 88 84.02 -47.48
REMARK 500 6 PRO A 90 -95.88 -76.55
REMARK 500 6 MET A 137 20.92 -72.09
REMARK 500 6 HIS A 148 30.69 -147.62
REMARK 500 7 LYS A 67 -77.99 -38.33
REMARK 500
REMARK 500 THIS ENTRY HAS 208 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 167 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 HIS A 84 NE2 130.8
REMARK 620 3 HIS A 97 ND1 135.5 82.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 168 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 76 OD1
REMARK 620 2 GLY A 77 O 79.1
REMARK 620 3 PRO A 78 O 115.3 62.5
REMARK 620 4 SER A 79 O 51.4 77.1 69.7
REMARK 620 5 LEU A 81 O 126.1 135.2 117.8 147.5
REMARK 620 6 LEU A 81 N 76.0 154.9 132.2 89.2 61.9
REMARK 620 7 ASP A 99 OD2 129.0 87.6 100.6 164.5 47.6 106.1
REMARK 620 8 GLU A 102 OE2 162.5 93.1 47.7 111.8 70.2 111.6 65.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 166 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119 NE2
REMARK 620 2 HIS A 123 NE2 75.6
REMARK 620 3 HIS A 129 NE2 123.5 89.4
REMARK 620 4 WAY A 169 O13 103.1 102.6 133.4
REMARK 620 5 WAY A 169 O11 140.2 144.0 73.0 71.3
REMARK 620 N 1 2 3 4
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 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WAY A 169
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FLS RELATED DB: PDB
REMARK 900 1FLS CONTAINS THE RESTRAINED MINIMIZED AVERAGE STRUCTURE CALCULATED
REMARK 900 FROM THE ENSEMBLE OF 30 STRUCTURES.
DBREF 1FM1 A 1 165 UNP P45452 MMP13_HUMAN 104 268
SEQRES 1 A 165 TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET
SEQRES 2 A 165 ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET
SEQRES 3 A 165 THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE
SEQRES 4 A 165 LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG
SEQRES 5 A 165 LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY
SEQRES 6 A 165 ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 165 SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN
SEQRES 8 A 165 TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP
SEQRES 9 A 165 THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 165 ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER
SEQRES 11 A 165 LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR
SEQRES 12 A 165 THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL
SEQRES 13 A 165 GLN GLY ILE GLN SER LEU TYR GLY PRO
HET ZN A 166 1
HET ZN A 167 1
HET CA A 168 1
HET WAY A 169 51
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM WAY N-HYDROXY-2-[(4-METHOXY-BENZENESULFONYL)-PYRIDIN-3-
HETNAM 2 WAY YLMETHYL-AMINO]-3-METHYL-BENZAMIDE
HETSYN WAY WAY-151693
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA CA 2+
FORMUL 5 WAY C21 H21 N3 O5 S
HELIX 1 1 THR A 27 VAL A 45 1 19
HELIX 2 2 LEU A 113 LEU A 125 1 13
HELIX 3 3 PRO A 152 GLY A 164 1 13
SHEET 1 A 5 ASN A 49 ARG A 52 0
SHEET 2 A 5 ASN A 14 ILE A 19 1 N LEU A 15 O ASN A 49
SHEET 3 A 5 ILE A 60 GLY A 65 1 N ILE A 60 O THR A 16
SHEET 4 A 5 ALA A 96 ASP A 99 1 N ALA A 96 O MET A 61
SHEET 5 A 5 ALA A 83 ALA A 85 -1 O HIS A 84 N HIS A 97
SHEET 1 B 2 TRP A 104 THR A 105 0
SHEET 2 B 2 TYR A 111 ASN A 112 1 O TYR A 111 N THR A 105
LINK NE2 HIS A 69 ZN ZN A 167 1555 1555 2.28
LINK OD1 ASP A 76 CA CA A 168 1555 1555 2.97
LINK O GLY A 77 CA CA A 168 1555 1555 2.87
LINK O PRO A 78 CA CA A 168 1555 1555 2.99
LINK O SER A 79 CA CA A 168 1555 1555 2.93
LINK O LEU A 81 CA CA A 168 1555 1555 2.87
LINK N LEU A 81 CA CA A 168 1555 1555 3.05
LINK NE2 HIS A 84 ZN ZN A 167 1555 1555 2.08
LINK ND1 HIS A 97 ZN ZN A 167 1555 1555 2.15
LINK OD2 ASP A 99 CA CA A 168 1555 1555 2.98
LINK OE2 GLU A 102 CA CA A 168 1555 1555 2.97
LINK NE2 HIS A 119 ZN ZN A 166 1555 1555 2.02
LINK NE2 HIS A 123 ZN ZN A 166 1555 1555 2.14
LINK NE2 HIS A 129 ZN ZN A 166 1555 1555 2.10
LINK ZN ZN A 166 O13 WAY A 169 1555 1555 1.88
LINK ZN ZN A 166 O11 WAY A 169 1555 1555 2.43
SITE 1 AC1 4 HIS A 119 HIS A 123 HIS A 129 WAY A 169
SITE 1 AC2 4 HIS A 69 ASP A 71 HIS A 84 HIS A 97
SITE 1 AC3 8 ASP A 76 GLY A 77 PRO A 78 SER A 79
SITE 2 AC3 8 GLY A 80 LEU A 81 ASP A 99 GLU A 102
SITE 1 AC4 9 GLY A 80 LEU A 81 LEU A 82 LEU A 115
SITE 2 AC4 9 HIS A 119 HIS A 123 HIS A 129 PRO A 139
SITE 3 AC4 9 ZN A 166
CRYST1 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
Complete list - b 23 2 Bytes