Header list of 2srt.pdb file
Complete list - p 29 2 Bytes
HEADER HYDROLASE/HYDROLASE INHIBITOR 22-MAR-95 2SRT
TITLE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED
TITLE 2 WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMELYSIN-1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.24.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: HUMAN STROMELYSIN-1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRO-SFSTR;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN STROMELYSIN-1
KEYWDS METZINCIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR P.R.GOOLEY,J.F.O'CONNELL
REVDAT 5 29-SEP-21 2SRT 1 REMARK HET HETNAM FORMUL
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 29-FEB-12 2SRT 1 JRNL VERSN HEADER
REVDAT 3 24-FEB-09 2SRT 1 VERSN
REVDAT 2 01-APR-03 2SRT 1 JRNL
REVDAT 1 10-JUL-95 2SRT 0
SPRSDE 10-JUL-95 2SRT 1SRT
JRNL AUTH P.R.GOOLEY,J.F.O'CONNELL,A.I.MARCY,G.C.CUCA,S.P.SALOWE,
JRNL AUTH 2 B.L.BUSH,J.D.HERMES,C.K.ESSER,W.K.HAGMANN,J.P.SPRINGER,
JRNL AUTH 3 B.A.JOHNSON
JRNL TITL THE NMR STRUCTURE OF THE INHIBITED CATALYTIC DOMAIN OF HUMAN
JRNL TITL 2 STROMELYSIN-1.
JRNL REF NAT.STRUCT.BIOL. V. 1 111 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7656014
JRNL DOI 10.1038/NSB0294-111
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.GOOLEY,B.A.JOHNSON,A.I.MARCY,G.C.CUCA,S.P.SALOWE,
REMARK 1 AUTH 2 W.K.HAGMANN,C.K.ESSER,J.P.SPRINGER
REMARK 1 TITL SECONDARY STRUCTURE AND ZINC LIGATION OF HUMAN RECOMBINANT
REMARK 1 TITL 2 SHORT-FORM STROMELYSIN BY MULTIDIMENSIONAL HETERONUCLEAR NMR
REMARK 1 REF BIOCHEMISTRY V. 32 13098 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, FANTOM
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), VON
REMARK 3 FREYBERG,SCHAUMANN,BRAUN (FANTOM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2SRT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178651.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 THR A 85 -126.30 -116.86
REMARK 500 1 PHE A 86 170.21 178.28
REMARK 500 1 ILE A 89 115.96 67.15
REMARK 500 1 LYS A 91 123.23 176.91
REMARK 500 1 ASP A 107 -48.04 -157.75
REMARK 500 1 ARG A 149 -149.70 41.35
REMARK 500 1 HIS A 151 48.10 -156.66
REMARK 500 1 ASP A 153 -160.10 46.04
REMARK 500 1 TYR A 155 67.59 -155.31
REMARK 500 1 PHE A 157 170.73 -52.39
REMARK 500 1 ASP A 158 103.47 -170.23
REMARK 500 1 ASN A 162 -152.14 51.34
REMARK 500 1 VAL A 163 116.99 -37.08
REMARK 500 1 ASP A 183 49.91 -89.74
REMARK 500 1 ASP A 189 -179.79 -170.32
REMARK 500 1 THR A 191 -43.17 -156.58
REMARK 500 1 ASN A 194 115.04 -33.77
REMARK 500 1 ALA A 213 56.50 -103.49
REMARK 500 1 PRO A 221 48.63 -75.04
REMARK 500 1 PHE A 232 152.00 -44.57
REMARK 500 1 TYR A 246 -94.10 -143.72
REMARK 500 2 THR A 85 -114.09 -119.69
REMARK 500 2 PHE A 86 170.38 175.86
REMARK 500 2 ILE A 89 112.13 66.20
REMARK 500 2 LYS A 91 123.85 172.40
REMARK 500 2 ASP A 107 -48.57 -158.75
REMARK 500 2 ARG A 149 -134.91 35.66
REMARK 500 2 HIS A 151 43.31 -166.41
REMARK 500 2 ASP A 153 -157.46 43.59
REMARK 500 2 TYR A 155 77.50 -155.02
REMARK 500 2 ASP A 158 117.82 164.83
REMARK 500 2 ASN A 162 -162.54 45.72
REMARK 500 2 VAL A 163 112.12 -34.26
REMARK 500 2 LEU A 207 -95.84 -78.25
REMARK 500 2 PHE A 210 -68.04 -152.74
REMARK 500 2 SER A 212 -99.04 -91.36
REMARK 500 2 ALA A 213 -48.61 173.81
REMARK 500 2 TYR A 246 -90.06 -112.26
REMARK 500 2 SER A 252 76.95 -151.63
REMARK 500 3 PHE A 86 170.80 -53.69
REMARK 500 3 ILE A 89 96.63 55.89
REMARK 500 3 LYS A 91 123.41 172.56
REMARK 500 3 ASP A 107 -47.70 -162.63
REMARK 500 3 ARG A 149 -153.74 33.52
REMARK 500 3 ASP A 153 -164.45 178.22
REMARK 500 3 PHE A 154 64.69 -107.29
REMARK 500 3 TYR A 155 64.23 -156.99
REMARK 500 3 PHE A 157 -131.37 -85.22
REMARK 500 3 ASP A 158 104.25 74.89
REMARK 500 3 ASN A 162 -156.36 56.50
REMARK 500
REMARK 500 THIS ENTRY HAS 510 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 134 0.09 SIDE CHAIN
REMARK 500 1 ARG A 149 0.10 SIDE CHAIN
REMARK 500 2 ARG A 100 0.11 SIDE CHAIN
REMARK 500 2 ARG A 134 0.08 SIDE CHAIN
REMARK 500 2 ARG A 231 0.12 SIDE CHAIN
REMARK 500 3 ARG A 233 0.15 SIDE CHAIN
REMARK 500 4 ARG A 93 0.08 SIDE CHAIN
REMARK 500 4 ARG A 134 0.09 SIDE CHAIN
REMARK 500 4 ARG A 149 0.14 SIDE CHAIN
REMARK 500 4 ARG A 233 0.10 SIDE CHAIN
REMARK 500 5 ARG A 84 0.08 SIDE CHAIN
REMARK 500 5 ARG A 93 0.14 SIDE CHAIN
REMARK 500 6 ARG A 93 0.10 SIDE CHAIN
REMARK 500 7 ARG A 233 0.11 SIDE CHAIN
REMARK 500 8 ARG A 233 0.10 SIDE CHAIN
REMARK 500 9 ARG A 134 0.13 SIDE CHAIN
REMARK 500 9 ARG A 149 0.19 SIDE CHAIN
REMARK 500 10 ARG A 100 0.10 SIDE CHAIN
REMARK 500 10 ARG A 231 0.14 SIDE CHAIN
REMARK 500 11 ARG A 100 0.09 SIDE CHAIN
REMARK 500 11 ARG A 134 0.17 SIDE CHAIN
REMARK 500 12 ARG A 93 0.08 SIDE CHAIN
REMARK 500 12 ARG A 149 0.13 SIDE CHAIN
REMARK 500 13 ARG A 84 0.11 SIDE CHAIN
REMARK 500 14 ARG A 84 0.14 SIDE CHAIN
REMARK 500 14 ARG A 231 0.09 SIDE CHAIN
REMARK 500 15 ARG A 149 0.09 SIDE CHAIN
REMARK 500 15 ARG A 231 0.09 SIDE CHAIN
REMARK 500 16 ARG A 149 0.17 SIDE CHAIN
REMARK 500 17 ARG A 84 0.11 SIDE CHAIN
REMARK 500 17 ARG A 134 0.12 SIDE CHAIN
REMARK 500 18 ARG A 233 0.09 SIDE CHAIN
REMARK 500 19 ARG A 100 0.08 SIDE CHAIN
REMARK 500 19 ARG A 149 0.09 SIDE CHAIN
REMARK 500 20 ARG A 149 0.17 SIDE CHAIN
REMARK 500 21 ARG A 84 0.15 SIDE CHAIN
REMARK 500 21 ARG A 134 0.14 SIDE CHAIN
REMARK 500 21 ARG A 149 0.10 SIDE CHAIN
REMARK 500 21 ARG A 231 0.09 SIDE CHAIN
REMARK 500 21 ARG A 233 0.16 SIDE CHAIN
REMARK 500 22 ARG A 93 0.09 SIDE CHAIN
REMARK 500 22 ARG A 149 0.11 SIDE CHAIN
REMARK 500 23 ARG A 93 0.09 SIDE CHAIN
REMARK 500 23 ARG A 231 0.11 SIDE CHAIN
REMARK 500 24 ARG A 84 0.08 SIDE CHAIN
REMARK 500 24 ARG A 93 0.12 SIDE CHAIN
REMARK 500 24 ARG A 149 0.16 SIDE CHAIN
REMARK 500 25 ARG A 93 0.14 SIDE CHAIN
REMARK 500 25 ARG A 149 0.10 SIDE CHAIN
REMARK 500 26 ARG A 149 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 57 PLANE DEVIATIONS.
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 258 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 151 NE2
REMARK 620 2 HIS A 166 NE2 97.2
REMARK 620 3 HIS A 179 ND1 90.1 110.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 257 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 201 NE2
REMARK 620 2 HIS A 205 NE2 108.7
REMARK 620 3 HIS A 211 NE2 106.8 129.4
REMARK 620 4 8MI A 256 O4 109.5 123.1 74.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: S2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: S3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8MI A 256
DBREF 2SRT A 83 255 UNP P08254 MMP3_HUMAN 100 272
SEQRES 1 A 173 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR
SEQRES 2 A 173 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU
SEQRES 3 A 173 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU
SEQRES 4 A 173 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG
SEQRES 5 A 173 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA
SEQRES 6 A 173 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 173 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY
SEQRES 8 A 173 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP
SEQRES 9 A 173 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 173 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER
SEQRES 11 A 173 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER
SEQRES 12 A 173 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP
SEQRES 13 A 173 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO ASP
SEQRES 14 A 173 SER PRO GLU THR
HET ZN A 257 1
HET ZN A 258 1
HET 8MI A 256 70
HETNAM ZN ZINC ION
HETNAM 8MI N-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-
HETNAM 2 8MI ARGININE-N-PHENYLAMIDE
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 8MI C25 H35 N6 O4 1+
HELIX 1 1 LYS A 110 GLU A 125 1 16
HELIX 2 2 LEU A 195 LEU A 207 1 13
HELIX 3 3 LEU A 229 ARG A 231 5 3
HELIX 4 4 GLN A 236 LEU A 245 1 10
SHEET 1 A 5 THR A 131 ARG A 134 0
SHEET 2 A 5 HIS A 96 ILE A 101 1 N LEU A 97 O THR A 131
SHEET 3 A 5 ILE A 142 PHE A 146 1 N ILE A 142 O ARG A 100
SHEET 4 A 5 ALA A 178 PHE A 180 1 N ALA A 178 O SER A 145
SHEET 5 A 5 ALA A 165 ALA A 167 -1 N HIS A 166 O HIS A 179
LINK NE2 HIS A 151 ZN ZN A 258 1555 1555 2.03
LINK NE2 HIS A 166 ZN ZN A 258 1555 1555 2.22
LINK ND1 HIS A 179 ZN ZN A 258 1555 1555 2.25
LINK NE2 HIS A 201 ZN ZN A 257 1555 1555 2.06
LINK NE2 HIS A 205 ZN ZN A 257 1555 1555 2.23
LINK NE2 HIS A 211 ZN ZN A 257 1555 1555 2.17
LINK O4 8MI A 256 ZN ZN A 257 1555 1555 2.05
SITE 1 S1 8 LEU A 164 LEU A 197 VAL A 198 HIS A 201
SITE 2 S1 8 LEU A 218 TYR A 220 LEU A 222 TYR A 223
SITE 1 S2 1 ASP A 183
SITE 1 S3 3 ASN A 162 LEU A 164 TYR A 223
SITE 1 AC1 4 HIS A 201 HIS A 205 HIS A 211 8MI A 256
SITE 1 AC2 4 HIS A 151 TYR A 155 HIS A 166 HIS A 179
SITE 1 AC3 11 ASN A 162 LEU A 164 ALA A 165 LEU A 197
SITE 2 AC3 11 HIS A 201 HIS A 211 LEU A 218 TYR A 220
SITE 3 AC3 11 LEU A 222 TYR A 223 ZN A 257
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
Complete list - p 29 2 Bytes