Header list of 3usn.pdb file
Complete list - 16 20 Bytes
HEADER HYDROLASE 18-JUN-98 3USN TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 TITLE 2 INHIBITED WITH THE THIADIAZOLE INHIBITOR IPNU-107859, NMR, 1 TITLE 3 STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: STROMELYSIN-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 83(1) - 250(168); COMPND 5 SYNONYM: MATRIX METALLOPROTEINASE-3, PROTEOGLYCANASE; COMPND 6 EC: 3.4.24.17; COMPND 7 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 CELL: FIBROBLAST; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSEE (PSTRO255); SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BL21 KEYWDS HYDROLASE, METALLOPROTEASE EXPDTA SOLUTION NMR AUTHOR B.J.STOCKMAN REVDAT 3 16-MAR-22 3USN 1 REMARK LINK REVDAT 2 24-FEB-09 3USN 1 VERSN REVDAT 1 20-JAN-99 3USN 0 JRNL AUTH B.J.STOCKMAN,D.J.WALDON,J.A.GATES,T.A.SCAHILL, JRNL AUTH 2 D.A.KLOOSTERMAN,S.A.MIZSAK,E.J.JACOBSEN,K.L.BELONGA, JRNL AUTH 3 M.A.MITCHELL,B.MAO,J.D.PETKE,L.GOODMAN,E.A.POWERS, JRNL AUTH 4 S.R.LEDBETTER,P.S.KAYTES,G.VOGELI,V.P.MARSHALL,G.L.PETZOLD, JRNL AUTH 5 R.A.POORMAN JRNL TITL SOLUTION STRUCTURES OF STROMELYSIN COMPLEXED TO THIADIAZOLE JRNL TITL 2 INHIBITORS. JRNL REF PROTEIN SCI. V. 7 2281 1998 JRNL REFN ISSN 0961-8368 JRNL PMID 9827994 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : MSI REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3USN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000179183. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.6 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 : 600 MHZ REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DISCOVER REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION REMARK 210 AND RESTRAINED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 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: 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 HG SER A 63 O ALA A 96 1.35 REMARK 500 O ASN A 132 HG1 THR A 133 1.37 REMARK 500 O GLY A 110 HG1 THR A 111 1.50 REMARK 500 HD2 ASP A 76 O GLY A 79 1.57 REMARK 500 O HIS A 142 HG SER A 143 1.58 REMARK 500 O ASP A 99 H ASP A 101 1.59 REMARK 500 O GLY A 159 HG SER A 162 1.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 14 CG HIS A 14 CD2 0.088 REMARK 500 GLU A 36 CD GLU A 36 OE2 0.126 REMARK 500 TRP A 42 CB TRP A 42 CG 0.112 REMARK 500 GLU A 43 CD GLU A 43 OE2 0.092 REMARK 500 GLU A 44 CD GLU A 44 OE2 0.069 REMARK 500 GLU A 55 CD GLU A 55 OE2 0.072 REMARK 500 GLU A 57 CD GLU A 57 OE2 0.108 REMARK 500 GLU A 68 CD GLU A 68 OE2 0.095 REMARK 500 HIS A 97 CG HIS A 97 CD2 0.090 REMARK 500 GLU A 102 CD GLU A 102 OE2 0.109 REMARK 500 HIS A 119 CG HIS A 119 CD2 0.060 REMARK 500 GLU A 120 CD GLU A 120 OE2 0.092 REMARK 500 HIS A 123 CG HIS A 123 CD2 0.072 REMARK 500 GLU A 134 CD GLU A 134 OE2 0.118 REMARK 500 HIS A 142 CG HIS A 142 CD2 0.056 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 TRP A 10 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES REMARK 500 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES REMARK 500 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 HIS A 14 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 ASP A 25 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 ASP A 25 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 VAL A 31 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES REMARK 500 TRP A 42 CB - CA - C ANGL. DEV. = 14.1 DEGREES REMARK 500 VAL A 45 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES REMARK 500 VAL A 45 CA - CB - CG2 ANGL. DEV. = 15.1 DEGREES REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES REMARK 500 ASP A 59 CB - CG - OD1 ANGL. DEV. = 9.7 DEGREES REMARK 500 ASP A 59 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 SER A 63 N - CA - C ANGL. DEV. = 20.6 DEGREES REMARK 500 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 ASP A 71 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES REMARK 500 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 TYR A 73 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES REMARK 500 ASP A 76 CB - CG - OD1 ANGL. DEV. = 9.9 DEGREES REMARK 500 ASP A 76 CB - CG - OD2 ANGL. DEV. = -10.9 DEGREES REMARK 500 HIS A 84 N - CA - CB ANGL. DEV. = 12.0 DEGREES REMARK 500 HIS A 84 N - CA - C ANGL. DEV. = -19.6 DEGREES REMARK 500 ALA A 85 N - CA - CB ANGL. DEV. = 9.6 DEGREES REMARK 500 GLY A 94 CA - C - N ANGL. DEV. = -16.4 DEGREES REMARK 500 ASP A 95 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 ALA A 96 CB - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 HIS A 97 ND1 - CE1 - NE2 ANGL. DEV. = 12.0 DEGREES REMARK 500 ASP A 99 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES REMARK 500 ASP A 99 CB - CG - OD2 ANGL. DEV. = -12.3 DEGREES REMARK 500 ASP A 100 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 ASP A 100 N - CA - C ANGL. DEV. = -17.2 DEGREES REMARK 500 ASP A 101 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = -11.0 DEGREES REMARK 500 TRP A 104 CD1 - NE1 - CE2 ANGL. DEV. = -6.3 DEGREES REMARK 500 ASP A 107 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 PHE A 114 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 HIS A 119 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 HIS A 123 ND1 - CE1 - NE2 ANGL. DEV. = 12.0 DEGREES REMARK 500 HIS A 142 ND1 - CE1 - NE2 ANGL. DEV. = 9.4 DEGREES REMARK 500 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 PHE A 150 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES REMARK 500 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES REMARK 500 ASP A 155 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES REMARK 500 ASP A 156 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES REMARK 500 ASP A 156 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES 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 ILE A 7 65.75 72.44 REMARK 500 LYS A 12 130.55 -176.37 REMARK 500 VAL A 45 -84.67 -47.34 REMARK 500 THR A 46 -151.09 -120.53 REMARK 500 PRO A 47 46.25 -85.43 REMARK 500 THR A 49 -167.25 -79.83 REMARK 500 PHE A 50 126.24 179.40 REMARK 500 ALA A 58 100.17 -170.90 REMARK 500 ASP A 59 61.21 -63.99 REMARK 500 ILE A 60 75.17 -167.64 REMARK 500 ARG A 67 -61.81 78.23 REMARK 500 HIS A 69 -52.85 -145.33 REMARK 500 ASP A 71 -90.18 -145.55 REMARK 500 PHE A 72 -38.32 -149.07 REMARK 500 ASN A 80 -101.46 62.14 REMARK 500 HIS A 97 91.96 -164.13 REMARK 500 ASP A 101 -90.90 -80.37 REMARK 500 THR A 111 112.04 -164.77 REMARK 500 PHE A 128 -102.90 -96.08 REMARK 500 ASN A 132 -45.14 -139.90 REMARK 500 THR A 133 -65.41 104.20 REMARK 500 ALA A 135 7.80 -68.91 REMARK 500 LEU A 136 -55.56 73.59 REMARK 500 MET A 137 40.23 -71.87 REMARK 500 HIS A 142 -111.44 -90.49 REMARK 500 SER A 143 84.48 -172.79 REMARK 500 LEU A 163 -68.75 -91.24 REMARK 500 PRO A 166 159.28 -40.33 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 HIS A 84 0.08 SIDE CHAIN REMARK 500 TYR A 86 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 THR A 23 -10.36 REMARK 500 SER A 63 14.43 REMARK 500 ASN A 93 12.15 REMARK 500 GLY A 94 18.67 REMARK 500 ASP A 100 -11.07 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 CA A 173 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 25 OD2 REMARK 620 2 ASP A 100 OD1 135.9 REMARK 620 3 GLU A 102 O 67.4 156.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 172 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 59 OD1 REMARK 620 2 GLY A 91 O 57.4 REMARK 620 3 ILE A 92 O 135.6 86.1 REMARK 620 4 ASN A 93 O 58.1 72.6 89.3 REMARK 620 5 GLY A 94 N 89.5 116.6 85.2 44.6 REMARK 620 6 ASP A 95 N 89.1 145.7 127.2 97.1 65.3 REMARK 620 7 ASP A 95 O 138.5 153.3 85.4 132.4 87.8 52.6 REMARK 620 8 ASP A 95 OD2 60.5 64.9 129.2 117.3 144.5 93.6 102.0 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 170 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 69 NE2 REMARK 620 2 ASP A 71 OD2 109.6 REMARK 620 3 HIS A 84 NE2 99.6 67.0 REMARK 620 4 HIS A 97 ND1 110.3 139.7 110.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 171 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 76 OD1 REMARK 620 2 GLY A 77 O 78.4 REMARK 620 3 GLY A 79 O 69.8 105.4 REMARK 620 4 VAL A 81 O 94.8 152.4 96.9 REMARK 620 5 ASP A 99 OD2 73.6 59.0 142.7 93.4 REMARK 620 6 ASP A 101 OD2 123.9 106.0 147.8 55.8 63.5 REMARK 620 7 GLU A 102 OE2 162.2 89.4 101.6 101.9 111.1 71.7 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 169 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 119 NE2 REMARK 620 2 HIS A 123 NE2 93.9 REMARK 620 3 HIS A 129 NE2 127.1 77.9 REMARK 620 4 ATT A 174 S2 114.1 124.6 113.2 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 169 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 170 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 171 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 172 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 173 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATT A 174 DBREF 3USN A 1 168 UNP P08254 MMP3_HUMAN 100 267 SEQRES 1 A 168 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR SEQRES 2 A 168 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU SEQRES 3 A 168 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU SEQRES 4 A 168 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG SEQRES 5 A 168 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA SEQRES 6 A 168 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO SEQRES 7 A 168 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY SEQRES 8 A 168 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP SEQRES 9 A 168 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA SEQRES 10 A 168 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER SEQRES 11 A 168 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER SEQRES 12 A 168 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP SEQRES 13 A 168 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO HET ZN A 169 1 HET ZN A 170 1 HET CA A 171 1 HET CA A 172 1 HET CA A 173 1 HET ATT A 174 36 HETNAM ZN ZINC ION HETNAM CA CALCIUM ION HETNAM ATT 2-[3-(5-MERCAPTO-[1,3,4]THIADIAZOL-2-YL)-UREIDO]-N- HETNAM 2 ATT METHYL-3-PHENYL-PROPIONAMIDE FORMUL 2 ZN 2(ZN 2+) FORMUL 4 CA 3(CA 2+) FORMUL 7 ATT C13 H15 N5 O2 S2 FORMUL 8 HOH *2(H2 O) HELIX 1 1 LYS A 28 VAL A 45 1 18 HELIX 2 2 LEU A 113 LEU A 125 1 13 HELIX 3 3 GLN A 154 LEU A 163 1 10 SHEET 1 A 3 ILE A 62 ALA A 65 0 SHEET 2 A 3 ASP A 95 ASP A 99 1 N ALA A 96 O SER A 63 SHEET 3 A 3 HIS A 84 TYR A 86 -1 N TYR A 86 O ASP A 95 LINK OD2 ASP A 25 CA CA A 173 1555 1555 2.66 LINK OD1 ASP A 59 CA CA A 172 1555 1555 2.97 LINK NE2 HIS A 69 ZN ZN A 170 1555 1555 2.61 LINK OD2 ASP A 71 ZN ZN A 170 1555 1555 2.34 LINK OD1 ASP A 76 CA CA A 171 1555 1555 2.68 LINK O GLY A 77 CA CA A 171 1555 1555 2.67 LINK O GLY A 79 CA CA A 171 1555 1555 2.71 LINK O VAL A 81 CA CA A 171 1555 1555 2.69 LINK NE2 HIS A 84 ZN ZN A 170 1555 1555 2.62 LINK O GLY A 91 CA CA A 172 1555 1555 2.70 LINK O ILE A 92 CA CA A 172 1555 1555 2.57 LINK O ASN A 93 CA CA A 172 1555 1555 3.03 LINK N GLY A 94 CA CA A 172 1555 1555 2.66 LINK N ASP A 95 CA CA A 172 1555 1555 2.59 LINK O ASP A 95 CA CA A 172 1555 1555 3.35 LINK OD2 ASP A 95 CA CA A 172 1555 1555 3.04 LINK ND1 HIS A 97 ZN ZN A 170 1555 1555 2.61 LINK OD2 ASP A 99 CA CA A 171 1555 1555 2.62 LINK OD1 ASP A 100 CA CA A 173 1555 1555 2.66 LINK OD2 ASP A 101 CA CA A 171 1555 1555 2.75 LINK OE2 GLU A 102 CA CA A 171 1555 1555 2.69 LINK O GLU A 102 CA CA A 173 1555 1555 2.64 LINK NE2 HIS A 119 ZN ZN A 169 1555 1555 2.59 LINK NE2 HIS A 123 ZN ZN A 169 1555 1555 2.61 LINK NE2 HIS A 129 ZN ZN A 169 1555 1555 2.61 LINK ZN ZN A 169 S2 ATT A 174 1555 1555 2.67 SITE 1 AC1 4 HIS A 119 HIS A 123 HIS A 129 ATT A 174 SITE 1 AC2 5 HIS A 69 ASP A 71 HIS A 84 TYR A 86 SITE 2 AC2 5 HIS A 97 SITE 1 AC3 7 ASP A 76 GLY A 77 GLY A 79 VAL A 81 SITE 2 AC3 7 ASP A 99 ASP A 101 GLU A 102 SITE 1 AC4 6 ASP A 59 GLY A 91 ILE A 92 ASN A 93 SITE 2 AC4 6 GLY A 94 ASP A 95 SITE 1 AC5 3 ASP A 25 ASP A 100 GLU A 102 SITE 1 AC6 6 PHE A 4 ALA A 83 ALA A 85 GLU A 120 SITE 2 AC6 6 HIS A 123 ZN 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
Complete list - 16 20 Bytes