Header list of 1ums.pdb file
Complete list - p 23 2 Bytes
HEADER HYDROLASE/HYDROLASE INHIBITOR 31-OCT-95 1UMS TITLE STROMELYSIN-1 CATALYTIC DOMAIN WITH HYDROPHOBIC INHIBITOR BOUND, PH TITLE 2 7.0, 32OC, 20 MM CACL2, 15% ACETONITRILE; NMR ENSEMBLE OF 20 TITLE 3 STRUCTURES 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 NUMMDL 20 AUTHOR S.R.VAN DOREN,A.V.KUROCHKIN,W.HU,E.R.P.ZUIDERWEG REVDAT 4 23-SEP-20 1UMS 1 REMARK LINK REVDAT 3 24-FEB-09 1UMS 1 VERSN REVDAT 2 15-FEB-05 1UMS 1 JRNL HET REVDAT 1 08-MAR-96 1UMS 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 : DGII, DISCOVER REMARK 3 AUTHORS : HAVEL (DGII), BIOSYM TECHNOLOGIES, INC. (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UMS 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_1000176954. 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 : 20 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 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 1-20 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 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 17 HIS A 201 CG HIS A 201 CD2 0.064 REMARK 500 18 PRO A 156 CD PRO A 156 N -0.088 REMARK 500 18 GLY A 159 CA GLY A 159 C 0.107 REMARK 500 18 SER A 244 CA SER A 244 CB -0.109 REMARK 500 19 TYR A 155 CE1 TYR A 155 CZ 0.085 REMARK 500 19 SER A 212 CB SER A 212 OG -0.083 REMARK 500 19 SER A 235 CA SER A 235 CB -0.094 REMARK 500 20 HIS A 201 CG HIS A 201 CD2 0.064 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 1 TYR A 104 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 1 ALA A 116 CB - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 1 PRO A 129 C - N - CA ANGL. DEV. = 12.3 DEGREES REMARK 500 1 PRO A 160 N - CA - CB ANGL. DEV. = 12.2 DEGREES REMARK 500 1 VAL A 163 CG1 - CB - CG2 ANGL. DEV. = 10.8 DEGREES REMARK 500 1 LEU A 164 CB - CG - CD2 ANGL. DEV. = 13.0 DEGREES REMARK 500 1 HIS A 166 CB - CA - C ANGL. DEV. = 14.5 DEGREES REMARK 500 1 HIS A 166 CA - CB - CG ANGL. DEV. = 11.4 DEGREES REMARK 500 1 ALA A 169 C - N - CA ANGL. DEV. = 16.1 DEGREES REMARK 500 1 TRP A 186 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 1 GLY A 192 N - CA - C ANGL. DEV. = -30.1 DEGREES REMARK 500 1 HIS A 224 C - N - CA ANGL. DEV. = 16.2 DEGREES REMARK 500 1 ASP A 238 CB - CA - C ANGL. DEV. = 20.4 DEGREES REMARK 500 1 TYR A 246 N - CA - CB ANGL. DEV. = -11.8 DEGREES REMARK 500 1 TYR A 246 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 1 TYR A 246 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES REMARK 500 1 TYR A 246 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES REMARK 500 2 VAL A 102 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES REMARK 500 2 ASN A 103 C - N - CA ANGL. DEV. = 15.2 DEGREES REMARK 500 2 ALA A 116 CB - CA - C ANGL. DEV. = 12.4 DEGREES REMARK 500 2 PRO A 129 C - N - CA ANGL. DEV. = 12.5 DEGREES REMARK 500 2 PHE A 146 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES REMARK 500 2 PHE A 146 CB - CG - CD1 ANGL. DEV. = -10.1 DEGREES REMARK 500 2 VAL A 148 CG1 - CB - CG2 ANGL. DEV. = 13.2 DEGREES REMARK 500 2 PRO A 160 N - CA - CB ANGL. DEV. = 11.7 DEGREES REMARK 500 2 LEU A 164 CB - CG - CD2 ANGL. DEV. = 10.8 DEGREES REMARK 500 2 HIS A 166 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 2 HIS A 166 CA - CB - CG ANGL. DEV. = 11.3 DEGREES REMARK 500 2 ASP A 181 CA - CB - CG ANGL. DEV. = 20.9 DEGREES REMARK 500 2 TRP A 186 CB - CA - C ANGL. DEV. = 13.2 DEGREES REMARK 500 2 GLY A 192 N - CA - C ANGL. DEV. = -24.1 DEGREES REMARK 500 2 ILE A 203 CA - CB - CG1 ANGL. DEV. = 11.7 DEGREES REMARK 500 2 ALA A 217 N - CA - CB ANGL. DEV. = -10.7 DEGREES REMARK 500 2 TYR A 246 CA - CB - CG ANGL. DEV. = 13.8 DEGREES REMARK 500 2 TYR A 246 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 3 TYR A 104 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 3 ALA A 116 CB - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 3 TRP A 124 CA - CB - CG ANGL. DEV. = 12.7 DEGREES REMARK 500 3 PRO A 129 C - N - CA ANGL. DEV. = 13.0 DEGREES REMARK 500 3 PRO A 160 N - CA - CB ANGL. DEV. = 11.0 DEGREES REMARK 500 3 LEU A 164 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES REMARK 500 3 HIS A 166 CB - CA - C ANGL. DEV. = 13.7 DEGREES REMARK 500 3 THR A 191 CA - CB - CG2 ANGL. DEV. = -12.1 DEGREES REMARK 500 3 GLY A 192 C - N - CA ANGL. DEV. = 27.0 DEGREES REMARK 500 3 GLY A 192 N - CA - C ANGL. DEV. = -21.7 DEGREES REMARK 500 3 ILE A 203 CA - CB - CG1 ANGL. DEV. = 11.5 DEGREES REMARK 500 3 PHE A 210 C - N - CA ANGL. DEV. = 17.5 DEGREES REMARK 500 3 HIS A 224 C - N - CA ANGL. DEV. = 18.1 DEGREES REMARK 500 3 TYR A 246 CA - CB - CG ANGL. DEV. = 16.5 DEGREES REMARK 500 3 TYR A 246 CB - CG - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 560 ANGLE DEVIATIONS. 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 ARG A 84 -141.17 -93.85 REMARK 500 1 THR A 85 168.92 57.14 REMARK 500 1 PHE A 86 161.05 44.21 REMARK 500 1 ILE A 89 154.41 91.07 REMARK 500 1 PRO A 90 -153.30 -33.50 REMARK 500 1 LYS A 91 48.38 -83.15 REMARK 500 1 THR A 95 50.93 -117.85 REMARK 500 1 HIS A 96 84.23 -168.88 REMARK 500 1 VAL A 102 -70.81 -43.03 REMARK 500 1 PRO A 106 34.63 -82.91 REMARK 500 1 VAL A 117 -79.16 -56.68 REMARK 500 1 GLU A 118 -37.15 -29.03 REMARK 500 1 VAL A 127 -71.08 -69.60 REMARK 500 1 PRO A 129 -26.27 -9.82 REMARK 500 1 LEU A 135 103.53 -37.23 REMARK 500 1 GLU A 137 167.74 159.58 REMARK 500 1 ALA A 140 -154.32 -133.54 REMARK 500 1 ALA A 147 -82.67 -167.61 REMARK 500 1 VAL A 148 65.48 -38.14 REMARK 500 1 GLU A 150 87.81 151.68 REMARK 500 1 PHE A 154 -85.33 -135.08 REMARK 500 1 PHE A 157 43.97 39.47 REMARK 500 1 ASN A 162 -148.35 115.61 REMARK 500 1 LEU A 164 -25.76 -170.27 REMARK 500 1 ALA A 169 178.22 15.51 REMARK 500 1 PRO A 170 -113.93 -70.29 REMARK 500 1 ASN A 175 108.98 -24.34 REMARK 500 1 ASP A 181 94.78 -43.50 REMARK 500 1 GLU A 184 -174.47 -67.73 REMARK 500 1 TRP A 186 140.45 -29.70 REMARK 500 1 THR A 187 -38.92 -144.17 REMARK 500 1 ASP A 189 57.63 -114.21 REMARK 500 1 THR A 190 -42.65 97.93 REMARK 500 1 THR A 191 -81.35 179.54 REMARK 500 1 SER A 206 -71.75 -50.12 REMARK 500 1 LEU A 209 52.21 -90.78 REMARK 500 1 HIS A 211 124.86 56.69 REMARK 500 1 SER A 212 -164.63 -165.39 REMARK 500 1 ALA A 217 162.42 -46.98 REMARK 500 1 TYR A 220 105.56 -54.48 REMARK 500 1 PRO A 221 53.33 -98.43 REMARK 500 1 LEU A 222 109.79 178.58 REMARK 500 1 TYR A 223 99.56 -30.88 REMARK 500 1 HIS A 224 41.39 179.24 REMARK 500 1 THR A 227 20.73 -78.16 REMARK 500 1 ARG A 231 79.15 -159.07 REMARK 500 1 ARG A 233 93.70 58.10 REMARK 500 1 LEU A 234 -172.92 -62.58 REMARK 500 1 ASN A 240 -3.68 -57.14 REMARK 500 1 TYR A 246 10.59 -49.91 REMARK 500 REMARK 500 THIS ENTRY HAS 1135 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 1 140.08 REMARK 500 TYR A 155 PRO A 156 1 -148.80 REMARK 500 TYR A 220 PRO A 221 1 -140.00 REMARK 500 THR A 128 PRO A 129 2 140.45 REMARK 500 THR A 128 PRO A 129 3 137.29 REMARK 500 TYR A 220 PRO A 221 3 -130.22 REMARK 500 THR A 128 PRO A 129 4 131.14 REMARK 500 TYR A 155 PRO A 156 4 -141.81 REMARK 500 GLY A 159 PRO A 160 4 -137.37 REMARK 500 ALA A 169 PRO A 170 4 -114.94 REMARK 500 THR A 128 PRO A 129 5 143.79 REMARK 500 THR A 128 PRO A 129 6 136.67 REMARK 500 TYR A 220 PRO A 221 6 -134.65 REMARK 500 THR A 128 PRO A 129 7 141.81 REMARK 500 TYR A 220 PRO A 221 7 -130.82 REMARK 500 ILE A 89 PRO A 90 8 -137.00 REMARK 500 THR A 128 PRO A 129 8 143.14 REMARK 500 GLY A 159 PRO A 160 8 -138.43 REMARK 500 THR A 128 PRO A 129 10 137.84 REMARK 500 ILE A 89 PRO A 90 11 148.35 REMARK 500 THR A 128 PRO A 129 11 143.18 REMARK 500 THR A 128 PRO A 129 12 141.31 REMARK 500 GLY A 159 PRO A 160 12 -145.56 REMARK 500 THR A 128 PRO A 129 13 139.16 REMARK 500 TYR A 155 PRO A 156 13 -104.29 REMARK 500 ALA A 169 PRO A 170 13 -54.19 REMARK 500 TYR A 220 PRO A 221 13 -138.77 REMARK 500 THR A 128 PRO A 129 14 137.86 REMARK 500 TYR A 220 PRO A 221 14 -134.90 REMARK 500 THR A 128 PRO A 129 15 142.51 REMARK 500 THR A 128 PRO A 129 16 141.90 REMARK 500 TYR A 155 PRO A 156 16 -103.93 REMARK 500 ILE A 89 PRO A 90 17 -120.10 REMARK 500 THR A 128 PRO A 129 17 139.00 REMARK 500 THR A 128 PRO A 129 18 137.94 REMARK 500 ALA A 169 PRO A 170 18 -40.47 REMARK 500 TYR A 220 PRO A 221 18 -124.32 REMARK 500 THR A 105 PRO A 106 19 -148.47 REMARK 500 THR A 128 PRO A 129 19 142.69 REMARK 500 TYR A 155 PRO A 156 19 -116.59 REMARK 500 THR A 128 PRO A 129 20 128.85 REMARK 500 TYR A 220 PRO A 221 20 -129.90 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 PHE A 83 0.09 SIDE CHAIN REMARK 500 1 PHE A 146 0.09 SIDE CHAIN REMARK 500 1 TYR A 155 0.15 SIDE CHAIN REMARK 500 1 HIS A 166 0.12 SIDE CHAIN REMARK 500 1 TYR A 220 0.06 SIDE CHAIN REMARK 500 1 TYR A 223 0.08 SIDE CHAIN REMARK 500 1 PHE A 232 0.11 SIDE CHAIN REMARK 500 1 TYR A 246 0.14 SIDE CHAIN REMARK 500 2 TYR A 104 0.10 SIDE CHAIN REMARK 500 2 PHE A 132 0.08 SIDE CHAIN REMARK 500 2 PHE A 146 0.49 SIDE CHAIN REMARK 500 2 HIS A 166 0.10 SIDE CHAIN REMARK 500 2 TYR A 168 0.10 SIDE CHAIN REMARK 500 2 TYR A 246 0.16 SIDE CHAIN REMARK 500 3 PHE A 132 0.10 SIDE CHAIN REMARK 500 3 TYR A 136 0.09 SIDE CHAIN REMARK 500 3 HIS A 166 0.08 SIDE CHAIN REMARK 500 3 PHE A 180 0.09 SIDE CHAIN REMARK 500 3 PHE A 196 0.25 SIDE CHAIN REMARK 500 3 TYR A 223 0.16 SIDE CHAIN REMARK 500 3 TYR A 246 0.10 SIDE CHAIN REMARK 500 4 PHE A 83 0.11 SIDE CHAIN REMARK 500 4 TYR A 136 0.11 SIDE CHAIN REMARK 500 4 PHE A 146 0.12 SIDE CHAIN REMARK 500 4 TYR A 168 0.08 SIDE CHAIN REMARK 500 4 PHE A 196 0.15 SIDE CHAIN REMARK 500 4 TYR A 223 0.10 SIDE CHAIN REMARK 500 4 TYR A 246 0.10 SIDE CHAIN REMARK 500 5 PHE A 83 0.10 SIDE CHAIN REMARK 500 5 TYR A 99 0.11 SIDE CHAIN REMARK 500 5 PHE A 146 0.10 SIDE CHAIN REMARK 500 5 PHE A 157 0.13 SIDE CHAIN REMARK 500 5 PHE A 196 0.27 SIDE CHAIN REMARK 500 5 TYR A 223 0.29 SIDE CHAIN REMARK 500 5 TYR A 246 0.18 SIDE CHAIN REMARK 500 6 TYR A 99 0.07 SIDE CHAIN REMARK 500 6 TYR A 136 0.07 SIDE CHAIN REMARK 500 6 HIS A 166 0.11 SIDE CHAIN REMARK 500 6 TYR A 168 0.12 SIDE CHAIN REMARK 500 6 TYR A 223 0.09 SIDE CHAIN REMARK 500 6 PHE A 232 0.09 SIDE CHAIN REMARK 500 6 TYR A 246 0.16 SIDE CHAIN REMARK 500 7 TYR A 136 0.10 SIDE CHAIN REMARK 500 7 PHE A 146 0.07 SIDE CHAIN REMARK 500 7 HIS A 151 0.10 SIDE CHAIN REMARK 500 7 TYR A 168 0.09 SIDE CHAIN REMARK 500 7 TYR A 223 0.37 SIDE CHAIN REMARK 500 7 PHE A 232 0.09 SIDE CHAIN REMARK 500 7 TYR A 246 0.18 SIDE CHAIN REMARK 500 8 PHE A 132 0.09 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 173 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 1 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 201 NE2 REMARK 620 2 HIS A 205 NE2 78.8 REMARK 620 3 HIS A 211 NE2 151.0 88.0 REMARK 620 4 0DS A 261 O21 91.3 133.5 116.1 REMARK 620 5 0DS A 261 O3 90.4 155.5 91.3 67.9 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 151 NE2 REMARK 620 2 ASP A 153 OD2 77.7 REMARK 620 3 HIS A 166 NE2 126.6 125.9 REMARK 620 4 HIS A 179 ND1 94.0 92.9 126.1 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 ASP A 158 OD1 REMARK 620 2 GLY A 159 O 138.4 REMARK 620 3 GLY A 161 O 112.1 61.2 REMARK 620 4 VAL A 163 O 62.7 158.9 117.0 REMARK 620 5 ASP A 181 OD2 75.0 103.5 163.7 79.2 REMARK 620 6 GLU A 184 OE2 126.2 87.3 115.9 74.7 65.7 REMARK 620 7 GLU A 184 OE1 132.5 53.9 110.1 114.2 58.8 43.8 REMARK 620 N 1 2 3 4 5 6 REMARK 630 REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR 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 1 0DS A 261 REMARK 630 2 0DS A 261 REMARK 630 3 0DS A 261 REMARK 630 4 0DS A 261 REMARK 630 5 0DS A 261 REMARK 630 6 0DS A 261 REMARK 630 7 0DS A 261 REMARK 630 8 0DS A 261 REMARK 630 9 0DS A 261 REMARK 630 10 0DS A 261 REMARK 630 11 0DS A 261 REMARK 630 12 0DS A 261 REMARK 630 13 0DS A 261 REMARK 630 14 0DS A 261 REMARK 630 15 0DS A 261 REMARK 630 16 0DS A 261 REMARK 630 17 0DS A 261 REMARK 630 18 0DS A 261 REMARK 630 19 0DS A 261 REMARK 630 20 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: 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 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 DBREF 1UMS 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 201 1555 1555 2.31 LINK ZN ZN A 1 NE2 HIS A 205 1555 1555 2.31 LINK ZN ZN A 1 NE2 HIS A 211 1555 1555 2.31 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 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 ZN ZN A 2 ND1 HIS A 179 1555 1555 2.31 LINK CA CA A 3 OD1 ASP A 158 1555 1555 2.29 LINK CA CA A 3 O GLY A 159 1555 1555 2.57 LINK CA CA A 3 O GLY A 161 1555 1555 2.59 LINK CA CA A 3 O VAL A 163 1555 1555 2.57 LINK CA CA A 3 OD2 ASP A 181 1555 1555 2.32 LINK CA CA A 3 OE2 GLU A 184 1555 1555 2.29 LINK CA CA A 3 OE1 GLU A 184 1555 1555 3.20 CISPEP 1 PHE A 86 PRO A 87 1 -19.15 CISPEP 2 LEU A 108 PRO A 109 1 18.89 CISPEP 3 PHE A 86 PRO A 87 2 -9.98 CISPEP 4 PHE A 86 PRO A 87 3 -11.61 CISPEP 5 PHE A 86 PRO A 87 5 -11.22 CISPEP 6 PHE A 86 PRO A 87 6 -20.84 CISPEP 7 PHE A 86 PRO A 87 7 -18.38 CISPEP 8 GLY A 171 PRO A 172 7 12.25 CISPEP 9 PHE A 86 PRO A 87 8 -13.34 CISPEP 10 ILE A 89 PRO A 90 9 -10.63 CISPEP 11 PHE A 86 PRO A 87 10 -19.26 CISPEP 12 PHE A 86 PRO A 87 11 -12.03 CISPEP 13 PHE A 86 PRO A 87 12 -10.56 CISPEP 14 PHE A 86 PRO A 87 13 -9.26 CISPEP 15 PHE A 86 PRO A 87 14 -8.59 CISPEP 16 PHE A 86 PRO A 87 15 -8.28 CISPEP 17 PHE A 86 PRO A 87 16 -13.96 CISPEP 18 PHE A 86 PRO A 87 17 2.72 CISPEP 19 GLY A 171 PRO A 172 17 -5.87 CISPEP 20 PHE A 86 PRO A 87 18 -10.69 CISPEP 21 TYR A 155 PRO A 156 18 -13.28 CISPEP 22 GLY A 171 PRO A 172 18 -15.86 CISPEP 23 PHE A 86 PRO A 87 19 -22.25 CISPEP 24 PHE A 86 PRO A 87 20 -14.61 SITE 1 S1' 6 LEU A 164 VAL A 198 HIS A 201 PRO A 221 SITE 2 S1' 6 LEU A 222 TYR A 223 SITE 1 S2' 5 ASN A 162 VAL A 163 LEU A 164 ALA A 165 SITE 2 S2' 5 LEU A 222 SITE 1 S3' 4 LEU A 164 THR A 193 LEU A 222 TYR A 223 SITE 1 AC1 5 TYR A 155 HIS A 201 HIS A 205 HIS A 211 SITE 2 AC1 5 0DS A 261 SITE 1 AC2 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179 SITE 1 AC3 7 ASP A 158 GLY A 159 GLY A 161 ASN A 162 SITE 2 AC3 7 VAL A 163 ASP A 181 GLU A 184 SITE 1 AC4 11 ZN A 1 TYR A 155 PRO A 156 ASN A 162 SITE 2 AC4 11 VAL A 163 HIS A 201 HIS A 211 PRO A 221 SITE 3 AC4 11 LEU A 222 TYR A 223 HIS A 224 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 23 2 Bytes