Header list of 1umt.pdb file
Complete list - 25 20 Bytes
HEADER HYDROLASE/HYDROLASE INHIBITOR 31-OCT-95 1UMT TITLE STROMELYSIN-1 CATALYTIC DOMAIN WITH HYDROPHOBIC INHIBITOR BOUND, PH TITLE 2 7.0, 32OC, 20 MM CACL2, 15% ACETONITRILE; NMR AVERAGE OF 20 TITLE 3 STRUCTURES MINIMIZED WITH RESTRAINTS COMPND MOL_ID: 1; COMPND 2 MOLECULE: STROMELYSIN-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN RESIDUES 83 - 256; COMPND 5 SYNONYM: MATRIX METALLOPROTEINASE-3, MMP-3; 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 GENE: HUMAN STROMELYSIN-1 CATALYTIC; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEMEX-D; SOURCE 9 EXPRESSION_SYSTEM_GENE: HUMAN STROMELYSIN-1 CATALYTIC DOMAIN; SOURCE 10 OTHER_DETAILS: INDUCTION BY M13 WITH T7 RNA POLYMERASE KEYWDS ZINC HYDROLASE, METZINCIN, MATRIX METALLOPROTEINASE, HYDROLASE- KEYWDS 2 HYDROLASE INHIBITOR COMPLEX EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR S.R.VAN DOREN,A.V.KUROCHKIN,W.HU,E.R.P.ZUIDERWEG REVDAT 4 13-JUL-11 1UMT 1 VERSN REVDAT 3 24-FEB-09 1UMT 1 VERSN REVDAT 2 15-FEB-05 1UMT 1 JRNL HET REVDAT 1 08-MAR-96 1UMT 0 JRNL AUTH S.R.VAN DOREN,A.V.KUROCHKIN,W.HU,Q.Z.YE,L.L.JOHNSON, JRNL AUTH 2 D.J.HUPE,E.R.ZUIDERWEG JRNL TITL SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JRNL TITL 2 STROMELYSIN COMPLEXED WITH A HYDROPHOBIC INHIBITOR. JRNL REF PROTEIN SCI. V. 4 2487 1995 JRNL REFN ISSN 0961-8368 JRNL PMID 8580839 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.R.VAN DOREN,A.V.KUROCHKIN,Q.-Z.YE,L.L.JOHNSON,D.J.HUPE, REMARK 1 AUTH 2 E.R.P.ZUIDERWEG REMARK 1 TITL ASSIGNMENTS FOR THE MAIN-CHAIN NUCLEAR MAGNETIC RESONANCES REMARK 1 TITL 2 AND DELINEATION OF THE SECONDARY STRUCTURE OF THE CATALYTIC REMARK 1 TITL 3 DOMAIN OF HUMAN STROMELYSIN-1 AS OBTAINED FROM REMARK 1 TITL 4 TRIPLE-RESONANCE 3D NMR EXPERIMENTS REMARK 1 REF BIOCHEMISTRY V. 32 13109 1993 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 DISTANCE GEOMETRY (DGII INTERFACED TO INSIGHTII) FOLLOWED REMARK 3 BY OPTIMIZATION USING SIMULATED ANNEALING WITHOUT A REMARK 3 PHYSICAL FORCEFIELD WAS USED TO GENERATE 39 STARTING REMARK 3 STRUCTURES. THESE 39 STRUCTURES WERE FURTHER REFINED BY REMARK 3 RESTRAINED MOLECULAR DYNAMICS AND RESTRAINED MINIMIZATION REMARK 3 USING DISCOVER AND THE AMBER FORCEFIELD. THE 20 BEST REMARK 3 STRUCTURES WITH LOWEST ENERGY AND FEWEST ABERRATIONS IN REMARK 3 WELL-DEFINED REGIONS WERE SELECTED. RESTRAINTS INCLUDE REMARK 3 1336 INTERRESIDUE NOES, 55 PHI TORSION RESTRAINTS, 42 REMARK 3 HYDROGEN BONDS, 15 METAL TO LIGAND DISTANCES, AND PEPTIDE REMARK 3 BOND TORSION RESTRAINTS TO MAINTAIN PLANARITY. THE REMARK 3 COMPLETE RESTRAINT LIST IS AVAILABLE AS PDB ENTRY REMARK 3 1UMT-MR. THE MEAN LARGEST NOE VIOLATION IS 0.64 +/- 0.07 REMARK 3 ANGSTROM. FOR RESIDUES 83 THROUGH 250, THE MEAN BACKBONE REMARK 3 (N, CA, C', O) RMSD TO THE AVERAGE IS 0.91 +/- 0.06 REMARK 3 ANGSTROM. THE MEAN RMSD OF ALL HEAVY ATOMS TO THE AVERAGE REMARK 3 IS 1.42 +/- 0.06 ANGSTROM. THIS ENSEMBLE WAS AVERAGED AND REMARK 3 MINIMIZED WITH RESTRAINTS TO GENERATE THIS MODEL. REMARK 3 REMARK 3 RESIDUES 249 (167) - 256 (174) AT THE C-TERMINUS ARE REMARK 3 DYNAMICALLY DISORDERED IN SOLUTION, JUDGING FROM THEIR REMARK 3 LONG T2S AND LACK OF NOES. THESE RESIDUES HAVE BEEN REMARK 3 OMITTED FROM THE MODEL. REMARK 4 REMARK 4 1UMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0-1.5 MM [U-99% 13C; U-99% REMARK 210 15N] DOUBLE LABELED SCD, 10 MM REMARK 210 TRIS-D11.HCL, 20 MM CACL2, 15% REMARK 210 ACETONITRILE-D3, 92% H2O/8% D2O; REMARK 210 0.6 MM [U-99% 13C; U-99% 15N] REMARK 210 DOUBLE LABELED SCD, 10 MM TRIS- REMARK 210 D11.HCL, 20 MM CACL2, 15% REMARK 210 ACETONITRILE-D3, 92% H2O/8% D2O; REMARK 210 0.6 MM [U-99% 15N] N15 LABELED REMARK 210 SCD, 10 MM TRIS-D11.HCL, 20 MM REMARK 210 CACL2, 15% ACETONITRILE-D3, 92% REMARK 210 H2O/8% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HSQC; 3D CT-HNCA; 3D CT- REMARK 210 HN(CO)CA; 3D CT-HN(CA)HA; 3D HCCH REMARK 210 -TOCSY; 3D CBCA(CO)NH; HCH; HMQC- REMARK 210 J; 3D NOESY-HSQC; HSQC-NOESY; REMARK 210 HBHA(CO)NH; 13C-RESOLVED FSCT- REMARK 210 HSMQC-NOESY; HALF-FILTERED NOESY; REMARK 210 FILTERED TOCSY; 3D CT-HA(CACO)NH; REMARK 210 3D CT-HA(CA)CO(N)H; 3D CT-HNCO; REMARK 210 2D 15N HSQC; 3D 15N-RESOLVED REMARK 210 NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, DGII REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 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 RES C SSSEQI REMARK 465 PRO A 249 REMARK 465 PRO A 250 REMARK 465 ASP A 251 REMARK 465 SER A 252 REMARK 465 PRO A 253 REMARK 465 GLU A 254 REMARK 465 THR A 255 REMARK 465 PRO A 256 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 H THR A 230 H ARG A 231 1.50 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 ALA A 116 CB - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 PRO A 129 C - N - CA ANGL. DEV. = 12.2 DEGREES REMARK 500 MET A 143 CA - CB - CG ANGL. DEV. = 12.2 DEGREES REMARK 500 VAL A 148 CG1 - CB - CG2 ANGL. DEV. = 14.0 DEGREES REMARK 500 PRO A 160 N - CA - CB ANGL. DEV. = 13.4 DEGREES REMARK 500 LEU A 164 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES REMARK 500 HIS A 166 CB - CA - C ANGL. DEV. = 13.7 DEGREES REMARK 500 ILE A 174 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 ASP A 181 CA - CB - CG ANGL. DEV. = 16.9 DEGREES REMARK 500 GLY A 192 N - CA - C ANGL. DEV. = -23.5 DEGREES REMARK 500 LEU A 197 CB - CG - CD1 ANGL. DEV. = -12.0 DEGREES REMARK 500 ILE A 203 CA - CB - CG1 ANGL. DEV. = 11.5 DEGREES REMARK 500 TYR A 223 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES REMARK 500 TYR A 246 CB - CG - CD2 ANGL. DEV. = -4.4 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 ARG A 84 -161.54 -70.80 REMARK 500 THR A 85 173.36 61.59 REMARK 500 PHE A 86 159.52 47.91 REMARK 500 ILE A 89 148.18 83.22 REMARK 500 PRO A 90 -141.82 -43.06 REMARK 500 LYS A 91 41.11 -74.96 REMARK 500 TRP A 92 90.68 -177.95 REMARK 500 ARG A 93 26.83 -74.96 REMARK 500 THR A 95 48.23 -92.25 REMARK 500 HIS A 96 76.45 -158.40 REMARK 500 VAL A 102 -71.23 -54.04 REMARK 500 ASN A 103 -151.80 -97.66 REMARK 500 TYR A 104 127.40 -171.35 REMARK 500 PRO A 106 46.52 -86.01 REMARK 500 ASP A 107 -69.85 -90.02 REMARK 500 VAL A 117 -76.32 -52.75 REMARK 500 GLU A 118 -36.13 -28.26 REMARK 500 PRO A 129 -27.38 -1.62 REMARK 500 GLU A 137 163.77 179.50 REMARK 500 VAL A 148 -45.47 173.05 REMARK 500 ARG A 149 87.24 -57.73 REMARK 500 GLU A 150 76.00 32.34 REMARK 500 ASP A 153 -94.91 -144.44 REMARK 500 PHE A 154 -84.79 -120.94 REMARK 500 PHE A 157 28.44 34.24 REMARK 500 ASN A 162 -140.00 119.14 REMARK 500 LEU A 164 8.06 -179.88 REMARK 500 ALA A 169 -169.72 -62.22 REMARK 500 ASN A 175 113.38 -22.13 REMARK 500 ASP A 181 89.18 -41.07 REMARK 500 GLU A 184 -170.67 -61.49 REMARK 500 TRP A 186 140.80 -36.48 REMARK 500 THR A 187 -160.49 -172.83 REMARK 500 LYS A 188 83.39 -174.13 REMARK 500 ASP A 189 41.41 -99.87 REMARK 500 THR A 190 -31.49 85.81 REMARK 500 THR A 191 -123.40 -144.30 REMARK 500 PHE A 210 115.77 -26.88 REMARK 500 HIS A 211 133.01 64.16 REMARK 500 SER A 212 -166.86 -170.56 REMARK 500 ALA A 213 83.06 -151.23 REMARK 500 THR A 215 -73.53 -64.79 REMARK 500 TYR A 220 153.88 -48.77 REMARK 500 LEU A 222 -176.70 -170.88 REMARK 500 TYR A 223 40.58 -80.03 REMARK 500 LEU A 226 -64.55 -24.08 REMARK 500 ASP A 228 134.49 57.26 REMARK 500 THR A 230 -33.20 -151.97 REMARK 500 ARG A 231 67.18 -163.14 REMARK 500 PHE A 232 5.44 -69.52 REMARK 500 REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR A 128 PRO A 129 137.36 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 PHE A 146 0.08 SIDE CHAIN REMARK 500 TYR A 168 0.07 SIDE CHAIN REMARK 500 PHE A 180 0.16 SIDE CHAIN REMARK 500 PHE A 196 0.26 SIDE CHAIN REMARK 500 TYR A 223 0.40 SIDE CHAIN REMARK 500 TYR A 246 0.25 SIDE CHAIN 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 1 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 211 NE2 REMARK 620 2 HIS A 201 NE2 161.7 REMARK 620 3 HIS A 205 NE2 100.1 80.1 REMARK 620 4 0DS A 261 O21 111.9 82.9 120.5 REMARK 620 5 0DS A 261 O3 78.8 97.5 169.1 69.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 2 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 179 ND1 REMARK 620 2 HIS A 151 NE2 93.9 REMARK 620 3 ASP A 153 OD2 101.3 80.6 REMARK 620 4 HIS A 166 NE2 127.1 135.6 103.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 3 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 184 OE2 REMARK 620 2 VAL A 163 O 124.4 REMARK 620 3 GLY A 159 O 61.1 164.6 REMARK 620 4 GLY A 161 O 81.3 131.9 60.8 REMARK 620 5 ASP A 181 OD2 67.9 87.8 81.4 139.8 REMARK 620 6 ASP A 158 OD1 139.3 63.5 102.6 125.5 73.1 REMARK 620 N 1 2 3 4 5 REMARK 630 REMARK 630 MOLECULE TYPE: NULL REMARK 630 MOLECULE NAME: N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4- REMARK 630 METHYLPENTANOYL}-L-LEUCYL-L-PHENYLALANINAMIDE REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 630 REMARK 630 M RES C SSSEQI REMARK 630 0DS A 261 REMARK 630 SOURCE: NULL REMARK 630 TAXONOMY: NULL REMARK 630 SUBCOMP: 2HM LEU PHE NH2 REMARK 630 DETAILS: NULL 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 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0DS A 261 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1UMS RELATED DB: PDB DBREF 1UMT A 83 256 UNP P08254 MM03_HUMAN 100 273 SEQRES 1 A 174 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR SEQRES 2 A 174 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU SEQRES 3 A 174 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU SEQRES 4 A 174 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG SEQRES 5 A 174 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA SEQRES 6 A 174 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO SEQRES 7 A 174 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY SEQRES 8 A 174 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP SEQRES 9 A 174 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA SEQRES 10 A 174 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER SEQRES 11 A 174 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER SEQRES 12 A 174 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP SEQRES 13 A 174 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO ASP SEQRES 14 A 174 SER PRO GLU THR PRO HET ZN A 1 1 HET ZN A 2 1 HET CA A 3 1 HET 0DS A 261 68 HETNAM ZN ZINC ION HETNAM CA CALCIUM ION HETNAM 0DS N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4- HETNAM 2 0DS METHYLPENTANOYL}-L-LEUCYL-L-PHENYLALANINAMIDE HETSYN 0DS ICI U24522 FORMUL 2 ZN 2(ZN 2+) FORMUL 4 CA CA 2+ FORMUL 5 0DS C23 H36 N4 O5 HELIX 1 A LYS A 110 VAL A 127 1AMPHIPATHIC 18 HELIX 2 B LEU A 195 SER A 206 1HIS LIGANDS TO CATALYTIC ZN 12 HELIX 3 C GLN A 236 TYR A 246 1 11 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 ALA A 147 1 O ILE A 142 N ARG A 100 SHEET 4 A 5 ASP A 177 ASP A 181 1 N ALA A 178 O MET A 143 SHEET 5 A 5 ALA A 165 TYR A 168 -1 N HIS A 166 O HIS A 179 LINK ZN ZN A 1 NE2 HIS A 211 1555 1555 2.30 LINK ZN ZN A 1 NE2 HIS A 201 1555 1555 2.30 LINK ZN ZN A 1 NE2 HIS A 205 1555 1555 2.30 LINK ZN ZN A 2 ND1 HIS A 179 1555 1555 2.31 LINK ZN ZN A 2 NE2 HIS A 151 1555 1555 2.32 LINK ZN ZN A 2 OD2 ASP A 153 1555 1555 2.29 LINK ZN ZN A 2 NE2 HIS A 166 1555 1555 2.32 LINK CA CA A 3 OE2 GLU A 184 1555 1555 2.29 LINK CA CA A 3 O VAL A 163 1555 1555 2.60 LINK CA CA A 3 O GLY A 159 1555 1555 2.58 LINK CA CA A 3 O GLY A 161 1555 1555 2.59 LINK CA CA A 3 OD2 ASP A 181 1555 1555 2.30 LINK CA CA A 3 OD1 ASP A 158 1555 1555 2.29 LINK ZN ZN A 1 O21 0DS A 261 1555 1555 2.29 LINK ZN ZN A 1 O3 0DS A 261 1555 1555 2.29 CISPEP 1 PHE A 86 PRO A 87 0 -20.42 SITE 1 AC1 4 HIS A 201 HIS A 205 HIS A 211 0DS A 261 SITE 1 AC2 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179 SITE 1 AC3 8 ASP A 158 GLY A 159 GLY A 161 ASN A 162 SITE 2 AC3 8 VAL A 163 LEU A 164 ASP A 181 GLU A 184 SITE 1 AC4 12 ZN A 1 TYR A 155 ASN A 162 VAL A 163 SITE 2 AC4 12 THR A 191 LEU A 197 VAL A 198 HIS A 201 SITE 3 AC4 12 HIS A 211 TYR A 220 PRO A 221 LEU A 222 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 - 25 20 Bytes