Header list of 1ycm.pdb file
Complete list - t 20 2 Bytes
HEADER HYDROLASE 22-DEC-04 1YCM
TITLE SOLUTION STRUCTURE OF MATRIX METALLOPROTEINASE 12 (MMP12) IN THE
TITLE 2 PRESENCE OF N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC
TITLE 3 ACID (NNGH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE METALLOELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HME, MATRIX METALLOPROTEINASE-12, MMP-12, MACROPHAGE
COMPND 5 ELASTASE, ME;
COMPND 6 EC: 3.4.24.65;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMP12, HME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MACROPHAGE METALLOELASTASE, MMP-12, SOLUTION STRUCTURE, NNGH, ZINC,
KEYWDS 2 CALCIUM, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 3 GENOMICS, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.BERTINI,V.CALDERONE,M.COSENZA,M.FRAGAI,Y.M.LEE,C.LUCHINAT,
AUTHOR 2 S.MANGANI,B.TERNI,P.TURANO,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 20-OCT-21 1YCM 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1YCM 1 VERSN
REVDAT 1 19-APR-05 1YCM 0
JRNL AUTH I.BERTINI,V.CALDERONE,M.COSENZA,M.FRAGAI,Y.M.LEE,C.LUCHINAT,
JRNL AUTH 2 S.MANGANI,B.TERNI,P.TURANO
JRNL TITL CONFORMATIONAL VARIABILITY OF MATRIX METALLOPROTEINASES:
JRNL TITL 2 BEYOND A SINGLE 3D STRUCTURE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 5334 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15809432
JRNL DOI 10.1073/PNAS.0407106102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, AMBER 6.0
REMARK 3 AUTHORS : BRUNGER (XWINNMR), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YCM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031380.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 0.3 M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM MMP12 U-15N,13C; 10 MM
REMARK 210 DEUTERATED TRIS, 5 MM CACL2, 0.1
REMARK 210 MM ZNCL2, 0.3 M NACL; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ; 700 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, XEASY 1.3, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE
REMARK 210 DYNAMICS, RESIDUE DIPOLAR
REMARK 210 COUPLINGS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING DISTANCE, DIHEDRAL
REMARK 210 ANGLE AND H-BOND RESTRAINTS WITH RESIDUE DIPOLAR COUPLING
REMARK 210 RESTRAINTS
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 HG1 THR A 115 H ASP A 158 1.30
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 3 HIS A 218 CG HIS A 218 CD2 0.070
REMARK 500 5 HIS A 218 CG HIS A 218 CD2 0.063
REMARK 500 15 HIS A 218 CG HIS A 218 CD2 0.067
REMARK 500 16 HIS A 218 CB HIS A 218 CG 0.109
REMARK 500 16 HIS A 218 CG HIS A 218 CD2 0.074
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 HIS A 196 CA - CB - CG ANGL. DEV. = 12.8 DEGREES
REMARK 500 1 THR A 239 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 3 LEU A 160 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 3 ILE A 180 CB - CA - C ANGL. DEV. = 15.8 DEGREES
REMARK 500 3 ILE A 180 N - CA - CB ANGL. DEV. = -17.5 DEGREES
REMARK 500 3 ILE A 180 CA - CB - CG2 ANGL. DEV. = 19.5 DEGREES
REMARK 500 3 HIS A 196 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 3 HIS A 218 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 3 HIS A 218 N - CA - CB ANGL. DEV. = 13.6 DEGREES
REMARK 500 3 HIS A 218 CB - CG - CD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 THR A 239 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 4 HIS A 196 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 4 HIS A 196 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 4 HIS A 222 CA - CB - CG ANGL. DEV. = 11.1 DEGREES
REMARK 500 5 ASP A 124 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 5 VAL A 162 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 5 HIS A 218 N - CA - CB ANGL. DEV. = 17.6 DEGREES
REMARK 500 6 THR A 239 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 7 HIS A 196 CA - CB - CG ANGL. DEV. = 12.2 DEGREES
REMARK 500 9 HIS A 196 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 10 THR A 239 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 10 GLY A 263 CA - C - O ANGL. DEV. = -40.2 DEGREES
REMARK 500 11 LEU A 181 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 12 ASP A 170 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 14 THR A 215 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 15 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 15 HIS A 168 CB - CG - CD2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 15 LEU A 181 CB - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 15 HIS A 218 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 15 HIS A 218 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 15 HIS A 218 CB - CG - CD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 15 THR A 239 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 16 HIS A 218 N - CA - CB ANGL. DEV. = 17.5 DEGREES
REMARK 500 17 THR A 239 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 18 THR A 239 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 19 THR A 239 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 20 THR A 239 N - CA - CB ANGL. DEV. = -11.4 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 1 ARG A 110 73.86 -174.27
REMARK 500 1 LYS A 111 -79.05 58.55
REMARK 500 1 HIS A 112 -72.33 56.34
REMARK 500 1 HIS A 168 137.68 82.01
REMARK 500 1 HIS A 172 69.90 -107.59
REMARK 500 1 ALA A 173 -75.77 -56.59
REMARK 500 1 PRO A 187 89.38 -69.92
REMARK 500 1 PHE A 237 157.34 -48.10
REMARK 500 1 PHE A 248 73.33 45.61
REMARK 500 2 LYS A 111 -57.59 -168.29
REMARK 500 2 HIS A 112 -63.17 63.16
REMARK 500 2 HIS A 172 -72.41 -109.46
REMARK 500 2 ALA A 173 -68.23 63.44
REMARK 500 2 ASP A 175 25.36 -168.98
REMARK 500 2 HIS A 228 95.69 56.14
REMARK 500 2 PHE A 248 71.91 53.05
REMARK 500 2 TYR A 262 -166.59 59.11
REMARK 500 3 ARG A 110 70.62 -69.56
REMARK 500 3 LYS A 111 -179.88 65.24
REMARK 500 3 HIS A 168 54.59 -155.32
REMARK 500 3 HIS A 172 71.94 -111.50
REMARK 500 3 ALA A 173 -72.53 -88.80
REMARK 500 3 ASP A 175 28.12 -178.56
REMARK 500 3 ASP A 198 89.73 -67.24
REMARK 500 3 SER A 230 39.54 -148.79
REMARK 500 3 PHE A 248 116.71 -34.56
REMARK 500 3 LEU A 261 74.13 -60.53
REMARK 500 4 ARG A 110 -56.53 63.64
REMARK 500 4 LYS A 111 -51.13 -151.09
REMARK 500 4 HIS A 112 -78.34 57.90
REMARK 500 4 HIS A 172 -72.85 -123.41
REMARK 500 4 ALA A 173 -77.48 56.21
REMARK 500 4 ASP A 175 10.16 -171.80
REMARK 500 4 ASP A 198 92.51 -62.24
REMARK 500 4 HIS A 206 -154.85 -74.77
REMARK 500 4 PHE A 248 75.50 60.96
REMARK 500 5 LYS A 111 -59.92 -159.41
REMARK 500 5 HIS A 112 -54.33 67.02
REMARK 500 5 MET A 156 72.89 -116.37
REMARK 500 5 HIS A 168 -31.75 -153.73
REMARK 500 5 ALA A 173 -140.22 49.74
REMARK 500 5 ASP A 175 11.55 -158.14
REMARK 500 5 PRO A 187 86.83 -68.57
REMARK 500 5 ASP A 198 96.76 -66.52
REMARK 500 5 HIS A 228 120.08 71.38
REMARK 500 5 SER A 230 29.91 -142.14
REMARK 500 5 PHE A 237 155.49 -48.90
REMARK 500 5 ILE A 245 -23.76 71.78
REMARK 500 5 PHE A 248 82.90 39.43
REMARK 500 6 LYS A 111 -40.21 -163.06
REMARK 500
REMARK 500 THIS ENTRY HAS 202 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 PHE A 174 ASP A 175 9 -148.95
REMARK 500 ALA A 195 HIS A 196 9 -133.89
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 202 0.08 SIDE CHAIN
REMARK 500 1 TYR A 242 0.11 SIDE CHAIN
REMARK 500 2 TYR A 121 0.08 SIDE CHAIN
REMARK 500 2 PHE A 149 0.08 SIDE CHAIN
REMARK 500 2 PHE A 163 0.10 SIDE CHAIN
REMARK 500 2 TYR A 242 0.09 SIDE CHAIN
REMARK 500 2 PHE A 248 0.09 SIDE CHAIN
REMARK 500 3 PHE A 174 0.09 SIDE CHAIN
REMARK 500 3 HIS A 196 0.32 SIDE CHAIN
REMARK 500 4 ARG A 117 0.10 SIDE CHAIN
REMARK 500 5 TYR A 132 0.06 SIDE CHAIN
REMARK 500 5 HIS A 218 0.10 SIDE CHAIN
REMARK 500 5 TYR A 242 0.09 SIDE CHAIN
REMARK 500 5 TYR A 262 0.07 SIDE CHAIN
REMARK 500 6 ARG A 117 0.08 SIDE CHAIN
REMARK 500 6 PHE A 174 0.11 SIDE CHAIN
REMARK 500 6 ASP A 194 0.07 SIDE CHAIN
REMARK 500 7 TYR A 113 0.10 SIDE CHAIN
REMARK 500 7 TYR A 116 0.12 SIDE CHAIN
REMARK 500 7 PHE A 149 0.11 SIDE CHAIN
REMARK 500 7 PHE A 174 0.09 SIDE CHAIN
REMARK 500 8 PHE A 163 0.08 SIDE CHAIN
REMARK 500 8 PHE A 213 0.08 SIDE CHAIN
REMARK 500 8 TYR A 262 0.08 SIDE CHAIN
REMARK 500 9 TYR A 116 0.17 SIDE CHAIN
REMARK 500 9 HIS A 196 0.16 SIDE CHAIN
REMARK 500 9 HIS A 218 0.19 SIDE CHAIN
REMARK 500 10 TYR A 121 0.08 SIDE CHAIN
REMARK 500 10 TYR A 132 0.08 SIDE CHAIN
REMARK 500 10 PHE A 248 0.11 SIDE CHAIN
REMARK 500 11 TYR A 116 0.07 SIDE CHAIN
REMARK 500 11 PHE A 163 0.10 SIDE CHAIN
REMARK 500 11 ASP A 194 0.07 SIDE CHAIN
REMARK 500 12 TYR A 121 0.11 SIDE CHAIN
REMARK 500 12 PHE A 163 0.09 SIDE CHAIN
REMARK 500 12 ASP A 194 0.07 SIDE CHAIN
REMARK 500 13 ARG A 110 0.09 SIDE CHAIN
REMARK 500 13 TYR A 132 0.07 SIDE CHAIN
REMARK 500 13 PHE A 213 0.09 SIDE CHAIN
REMARK 500 14 TYR A 116 0.08 SIDE CHAIN
REMARK 500 14 HIS A 196 0.14 SIDE CHAIN
REMARK 500 14 PHE A 197 0.10 SIDE CHAIN
REMARK 500 14 PHE A 213 0.08 SIDE CHAIN
REMARK 500 15 TYR A 116 0.09 SIDE CHAIN
REMARK 500 15 HIS A 168 0.14 SIDE CHAIN
REMARK 500 15 HIS A 222 0.10 SIDE CHAIN
REMARK 500 15 PHE A 248 0.10 SIDE CHAIN
REMARK 500 16 TYR A 116 0.10 SIDE CHAIN
REMARK 500 16 TYR A 121 0.14 SIDE CHAIN
REMARK 500 16 TYR A 240 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 67 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 CA A 266 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 122 OG1
REMARK 620 2 ASP A 124 OD2 73.9
REMARK 620 3 ASP A 124 OD1 56.1 48.2
REMARK 620 4 GLU A 199 OE2 57.8 131.5 97.1
REMARK 620 5 GLU A 199 O 135.1 148.1 151.6 79.3
REMARK 620 6 GLU A 199 OE1 65.7 139.6 104.5 8.3 71.0
REMARK 620 7 GLU A 201 O 117.8 83.7 131.9 119.9 71.0 115.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 265 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 168 NE2
REMARK 620 2 ASP A 170 OD1 106.3
REMARK 620 3 ASP A 170 OD2 95.3 17.0
REMARK 620 4 HIS A 183 NE2 148.2 94.5 109.6
REMARK 620 5 HIS A 196 ND1 91.1 152.5 144.6 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 267 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 175 OD2
REMARK 620 2 ASP A 175 O 83.0
REMARK 620 3 ASP A 175 OD1 10.0 73.2
REMARK 620 4 GLY A 176 O 104.0 64.5 97.3
REMARK 620 5 GLY A 178 O 67.3 117.1 71.2 70.8
REMARK 620 6 ILE A 180 O 75.3 137.8 84.5 155.9 87.3
REMARK 620 7 ASP A 198 OD1 139.7 75.8 135.5 97.3 153.0 98.1
REMARK 620 8 ASP A 198 OD2 86.0 67.7 84.4 129.2 151.2 75.0 54.3
REMARK 620 9 GLU A 201 OE2 132.7 138.3 140.3 83.4 71.7 80.2 83.1 125.5
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 268 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 190 O
REMARK 620 2 GLY A 192 O 78.9
REMARK 620 3 ASP A 194 OD2 84.1 115.8
REMARK 620 4 ASP A 194 OD1 133.2 105.7 51.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 218 NE2
REMARK 620 2 HIS A 222 NE2 76.8
REMARK 620 3 HIS A 228 NE2 117.2 83.9
REMARK 620 4 NGH A 269 O4 66.7 101.3 174.3
REMARK 620 5 NGH A 269 O5 92.7 147.3 127.6 46.8
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 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGH A 269
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CIRMMP48 RELATED DB: TARGETDB
DBREF 1YCM A 106 263 UNP P39900 MMP12_HUMAN 106 263
SEQADV 1YCM MET A 105 UNP P39900 INITIATING METHIONINE
SEQADV 1YCM ASP A 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQRES 1 A 159 MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR ARG
SEQRES 2 A 159 ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP VAL
SEQRES 3 A 159 ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER ASN
SEQRES 4 A 159 VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY MET
SEQRES 5 A 159 ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS GLY
SEQRES 6 A 159 ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU ALA
SEQRES 7 A 159 HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP ALA
SEQRES 8 A 159 HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER GLY
SEQRES 9 A 159 GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE GLY
SEQRES 10 A 159 HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS ALA
SEQRES 11 A 159 VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN THR
SEQRES 12 A 159 PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN SER
SEQRES 13 A 159 LEU TYR GLY
HET ZN A 264 1
HET ZN A 265 1
HET CA A 266 1
HET CA A 267 1
HET CA A 268 1
HET NGH A 269 40
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NGH N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC
HETNAM 2 NGH ACID
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 NGH C13 H20 N2 O5 S
HELIX 1 1 ASN A 126 THR A 145 1 20
HELIX 2 2 LEU A 212 GLY A 225 1 14
HELIX 3 3 SER A 251 LEU A 261 1 11
SHEET 1 A 5 LYS A 148 LYS A 151 0
SHEET 2 A 5 TYR A 113 ILE A 118 1 N TYR A 116 O SER A 150
SHEET 3 A 5 ILE A 159 ALA A 164 1 O VAL A 161 N ARG A 117
SHEET 4 A 5 ALA A 195 ASP A 198 1 O PHE A 197 N VAL A 162
SHEET 5 A 5 ALA A 182 ALA A 184 -1 N HIS A 183 O HIS A 196
SHEET 1 B 2 TRP A 203 THR A 204 0
SHEET 2 B 2 THR A 210 ASN A 211 1 O THR A 210 N THR A 204
LINK OG1 THR A 122 CA CA A 266 1555 1555 2.55
LINK OD2 ASP A 124 CA CA A 266 1555 1555 2.24
LINK OD1 ASP A 124 CA CA A 266 1555 1555 2.81
LINK NE2 HIS A 168 ZN ZN A 265 1555 1555 2.24
LINK OD1 ASP A 170 ZN ZN A 265 1555 1555 4.14
LINK OD2 ASP A 170 ZN ZN A 265 1555 1555 2.09
LINK OD2 ASP A 175 CA CA A 267 1555 1555 4.36
LINK O ASP A 175 CA CA A 267 1555 1555 2.41
LINK OD1 ASP A 175 CA CA A 267 1555 1555 2.23
LINK O GLY A 176 CA CA A 267 1555 1555 2.46
LINK O GLY A 178 CA CA A 267 1555 1555 2.41
LINK O ILE A 180 CA CA A 267 1555 1555 2.42
LINK NE2 HIS A 183 ZN ZN A 265 1555 1555 2.19
LINK O GLY A 190 CA CA A 268 1555 1555 2.69
LINK O GLY A 192 CA CA A 268 1555 1555 2.42
LINK OD2 ASP A 194 CA CA A 268 1555 1555 2.60
LINK OD1 ASP A 194 CA CA A 268 1555 1555 2.22
LINK ND1 HIS A 196 ZN ZN A 265 1555 1555 2.53
LINK OD1 ASP A 198 CA CA A 267 1555 1555 2.31
LINK OD2 ASP A 198 CA CA A 267 1555 1555 2.40
LINK OE2 GLU A 199 CA CA A 266 1555 1555 4.42
LINK O GLU A 199 CA CA A 266 1555 1555 2.31
LINK OE1 GLU A 199 CA CA A 266 1555 1555 2.25
LINK O GLU A 201 CA CA A 266 1555 1555 2.47
LINK OE2 GLU A 201 CA CA A 267 1555 1555 2.23
LINK NE2 HIS A 218 ZN ZN A 264 1555 1555 2.08
LINK NE2 HIS A 222 ZN ZN A 264 1555 1555 2.08
LINK NE2 HIS A 228 ZN ZN A 264 1555 1555 2.14
LINK ZN ZN A 264 O4 NGH A 269 1555 1555 3.30
LINK ZN ZN A 264 O5 NGH A 269 1555 1555 3.58
SITE 1 AC1 4 HIS A 218 HIS A 222 HIS A 228 NGH A 269
SITE 1 AC2 4 HIS A 168 ASP A 170 HIS A 183 HIS A 196
SITE 1 AC3 4 THR A 122 ASP A 124 GLU A 199 GLU A 201
SITE 1 AC4 6 ASP A 175 GLY A 176 GLY A 178 ILE A 180
SITE 2 AC4 6 ASP A 198 GLU A 201
SITE 1 AC5 4 GLY A 190 ILE A 191 GLY A 192 ASP A 194
SITE 1 AC6 10 LEU A 181 ALA A 182 LEU A 214 THR A 215
SITE 2 AC6 10 HIS A 218 GLU A 219 PRO A 238 THR A 239
SITE 3 AC6 10 TYR A 240 ZN A 264
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 - t 20 2 Bytes