HEADER HYDROLASE 13-MAY-11 2YIG
TITLE MMP13 IN COMPLEX WITH A NOVEL SELECTIVE NON ZINC BINDING INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLLAGENASE 3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 104-274;
COMPND 5 SYNONYM: MATRIX METALLOPROTEINASE-13, MMP-13;
COMPND 6 EC: 3.4.24.-;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7#3.3
KEYWDS HYDROLASE, COLLAGENASE 3, MMP-13, MATRIXMETALLOPROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GERHARDT,D.HARGREAVES
REVDAT 3 12-JUL-17 2YIG 1
REVDAT 2 13-JUL-11 2YIG 1 REVDAT JRNL
REVDAT 1 29-JUN-11 2YIG 0
JRNL AUTH C.D.SAVI,A.D.MORLEY,A.TING,I.NASH,K.KARABELAS,C.M.WOOD,
JRNL AUTH 2 M.JAMES,S.J.NORRIS,G.KAROUTCHI,N.RANKINE,G.HAMLIN,
JRNL AUTH 3 P.A.MACFAUL,D.RYAN,S.V.BAKER,D.HARGREAVES,S.GERHARDT
JRNL TITL SELECTIVE NON ZINC BINDING INHIBITORS OF MMP13.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 4215 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21669521
JRNL DOI 10.1016/J.BMCL.2011.05.075
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0113
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 34539
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1830
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2415
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 79
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : -0.63000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2818 ; 0.021 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3833 ; 1.835 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 6.448 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;36.251 ;24.015
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 403 ;14.226 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;21.660 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 377 ; 0.147 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2306 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 104 A 272
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8610 3.8206 15.7458
REMARK 3 T TENSOR
REMARK 3 T11: 0.0182 T22: 0.0055
REMARK 3 T33: 0.0059 T12: 0.0025
REMARK 3 T13: -0.0060 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.9611 L22: 0.8088
REMARK 3 L33: 1.6235 L12: 0.0753
REMARK 3 L13: -0.7408 L23: 0.0888
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: 0.0375 S13: -0.0079
REMARK 3 S21: -0.0866 S22: 0.0255 S23: -0.0082
REMARK 3 S31: 0.0376 S32: -0.0011 S33: -0.0106
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 104 B 269
REMARK 3 ORIGIN FOR THE GROUP (A): 55.9048 -4.0168 25.9177
REMARK 3 T TENSOR
REMARK 3 T11: 0.0350 T22: 0.0185
REMARK 3 T33: 0.0358 T12: -0.0016
REMARK 3 T13: -0.0011 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.7895 L22: 0.7171
REMARK 3 L33: 1.2188 L12: -0.1593
REMARK 3 L13: 0.0455 L23: -0.0309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: 0.0554 S13: -0.0362
REMARK 3 S21: -0.1493 S22: -0.0058 S23: -0.0265
REMARK 3 S31: 0.0497 S32: 0.0508 S33: -0.0306
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES FROM SER A 250 TO PHE A 252 ARE DISORDERED.
REMARK 3 NCS TYPE: LOCAL, GROUP A 104-268, B 104-268, COUNT 211, RMS 0.15,
REMARK 3 WEIGHT 0.05.
REMARK 4
REMARK 4 2YIG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1290048292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36370
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 67.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-27% PEG 3350, 1.5 M AMMONIUM
REMARK 280 FORMATE, 0.1 M TRIS/HCL PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.20850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.03700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.20850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.03700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 250
REMARK 465 HIS A 251
REMARK 465 PRO A 273
REMARK 465 ASN A 274
REMARK 465 ASP B 270
REMARK 465 GLU B 271
REMARK 465 ASP B 272
REMARK 465 PRO B 273
REMARK 465 ASN B 274
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 249 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O HOH A 474 O HOH A 523 2.05
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 187 NE2 HIS A 187 CD2 -0.098
REMARK 500 HIS A 226 NE2 HIS A 226 CD2 -0.077
REMARK 500 HIS B 157 NE2 HIS B 157 CD2 -0.080
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 155 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 270 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG B 155 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 179 CB - CG - OD1 ANGL. DEV. = 5.5 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 LYS A 170 -128.95 40.63
REMARK 500 SER A 182 -155.75 50.52
REMARK 500 ASN A 194 -115.29 57.82
REMARK 500 SER A 210 -159.97 -145.06
REMARK 500 LYS B 170 -133.19 48.19
REMARK 500 PHE B 175 19.96 56.83
REMARK 500 TYR B 176 71.11 -111.14
REMARK 500 SER B 182 -164.66 78.73
REMARK 500 ASN B 194 -119.10 58.13
REMARK 500 SER B 210 -117.14 -123.04
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 NA A 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 128 OD2
REMARK 620 2 ASP A 203 O 164.7
REMARK 620 3 ASP A 203 OD1 99.4 68.8
REMARK 620 4 GLU A 205 O 84.5 90.8 111.6
REMARK 620 5 HOH B 476 O 123.8 71.2 116.0 116.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 162 O
REMARK 620 2 ASN A 194 O 168.9
REMARK 620 3 GLY A 196 O 95.1 93.3
REMARK 620 4 ASP A 198 OD1 87.0 99.8 93.1
REMARK 620 5 HOH A 464 O 90.6 83.5 81.1 173.4
REMARK 620 6 HOH A 431 O 89.6 80.7 167.9 98.4 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 172 NE2
REMARK 620 2 ASP A 174 OD2 114.0
REMARK 620 3 HIS A 187 NE2 124.1 105.6
REMARK 620 4 HIS A 200 ND1 105.0 97.0 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 179 OD1
REMARK 620 2 GLY A 180 O 86.2
REMARK 620 3 SER A 182 O 85.2 86.1
REMARK 620 4 LEU A 184 O 88.1 174.2 94.7
REMARK 620 5 ASP A 202 OD2 94.5 86.8 172.9 92.4
REMARK 620 6 GLU A 205 OE2 167.5 95.4 82.5 90.4 98.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 222 NE2
REMARK 620 2 HIS A 226 NE2 102.1
REMARK 620 3 HIS A 232 NE2 108.7 101.6
REMARK 620 4 HOH A 480 O 116.3 109.3 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 128 OD2
REMARK 620 2 ASP B 203 O 168.5
REMARK 620 3 ASP B 203 OD1 114.1 69.2
REMARK 620 4 GLU B 205 O 83.9 84.6 110.7
REMARK 620 5 HOH A 533 O 109.2 78.7 110.1 126.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 162 O
REMARK 620 2 ASN B 194 O 170.9
REMARK 620 3 GLY B 196 O 93.3 95.7
REMARK 620 4 ASP B 198 OD1 83.5 97.1 90.5
REMARK 620 5 HOH B 414 O 90.1 90.7 80.9 169.0
REMARK 620 6 HOH B 416 O 91.6 79.3 171.5 96.9 92.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 172 NE2
REMARK 620 2 ASP B 174 OD2 113.1
REMARK 620 3 HIS B 187 NE2 114.0 114.5
REMARK 620 4 HIS B 200 ND1 108.9 93.4 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 179 OD1
REMARK 620 2 GLY B 180 O 86.2
REMARK 620 3 SER B 182 O 87.7 90.7
REMARK 620 4 LEU B 184 O 89.5 175.7 88.8
REMARK 620 5 ASP B 202 OD2 92.0 86.7 177.3 93.9
REMARK 620 6 GLU B 205 OE2 174.5 94.3 86.8 89.9 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 222 NE2
REMARK 620 2 HIS B 226 NE2 103.7
REMARK 620 3 HIS B 232 NE2 110.3 98.5
REMARK 620 4 HOH B 500 O 116.9 110.3 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 307 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 504 O
REMARK 620 2 HOH A 543 O 141.0
REMARK 620 3 HOH A 481 O 109.8 108.0
REMARK 620 4 HOH A 551 O 78.8 84.5 102.3
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 5EL A 1273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5EL B 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA M 811
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EUB RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COLLAGENASE-3
REMARK 900 (MMP- 13) COMPLEXED TO A POTENT NON- PEPTIDIC SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1FLS RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMANCOLLAGENASE-3
REMARK 900 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR
REMARK 900 RELATED ID: 1XUR RELATED DB: PDB
REMARK 900 MATRIX METALLOPROTEINASE-13 COMPLEXED WITH NON-ZINC BINDINGINHIBITOR
REMARK 900 RELATED ID: 1YOU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP- 13COMPLEXED WITH
REMARK 900 A POTENT PYRIMIDINETRIONE INHIBITOR
REMARK 900 RELATED ID: 1FM1 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMANCOLLAGENASE-3
REMARK 900 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR
REMARK 900 RELATED ID: 456C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-
REMARK 900 ETHER SULPHONE BASED HYDROXAMIC ACID
REMARK 900 RELATED ID: 830C RELATED DB: PDB
REMARK 900 COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID
REMARK 900 RELATED ID: 1UC1 RELATED DB: PDB
REMARK 900 HOMOLOGY PREDICTED HUMAN COLLAGENASE 3
REMARK 900 RELATED ID: 1XUC RELATED DB: PDB
REMARK 900 MATRIX METALLOPROTEINASE-13 COMPLEXED WITH NON-ZINC BINDING
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1PEX RELATED DB: PDB
REMARK 900 COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN
REMARK 900 RELATED ID: 1ZTQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP- 13COMPLEXED WITH
REMARK 900 WAY-033
REMARK 900 RELATED ID: 2D1N RELATED DB: PDB
REMARK 900 COLLAGENASE-3 (MMP-13) COMPLEXED TO A HYDROXAMIC ACID INHIBITOR
REMARK 900 RELATED ID: 1XUD RELATED DB: PDB
REMARK 900 MATRIX METALLOPROTEINASE-13 COMPLEXED WITH NON-ZINC BINDING
REMARK 900 INHIBITOR
DBREF 2YIG A 104 274 UNP P45452 MMP13_HUMAN 104 274
DBREF 2YIG B 104 274 UNP P45452 MMP13_HUMAN 104 274
SEQRES 1 A 171 TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET
SEQRES 2 A 171 ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET
SEQRES 3 A 171 THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE
SEQRES 4 A 171 LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG
SEQRES 5 A 171 LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY
SEQRES 6 A 171 ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 171 SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN
SEQRES 8 A 171 TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP
SEQRES 9 A 171 THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 171 ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER
SEQRES 11 A 171 LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR
SEQRES 12 A 171 THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL
SEQRES 13 A 171 GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP
SEQRES 14 A 171 PRO ASN
SEQRES 1 B 171 TYR ASN VAL PHE PRO ARG THR LEU LYS TRP SER LYS MET
SEQRES 2 B 171 ASN LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP MET
SEQRES 3 B 171 THR HIS SER GLU VAL GLU LYS ALA PHE LYS LYS ALA PHE
SEQRES 4 B 171 LYS VAL TRP SER ASP VAL THR PRO LEU ASN PHE THR ARG
SEQRES 5 B 171 LEU HIS ASP GLY ILE ALA ASP ILE MET ILE SER PHE GLY
SEQRES 6 B 171 ILE LYS GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 B 171 SER GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO ASN
SEQRES 8 B 171 TYR GLY GLY ASP ALA HIS PHE ASP ASP ASP GLU THR TRP
SEQRES 9 B 171 THR SER SER SER LYS GLY TYR ASN LEU PHE LEU VAL ALA
SEQRES 10 B 171 ALA HIS GLU PHE GLY HIS SER LEU GLY LEU ASP HIS SER
SEQRES 11 B 171 LYS ASP PRO GLY ALA LEU MET PHE PRO ILE TYR THR TYR
SEQRES 12 B 171 THR GLY LYS SER HIS PHE MET LEU PRO ASP ASP ASP VAL
SEQRES 13 B 171 GLN GLY ILE GLN SER LEU TYR GLY PRO GLY ASP GLU ASP
SEQRES 14 B 171 PRO ASN
HET 5EL A 301 34
HET ZN A 302 1
HET CA A 303 1
HET ZN A 304 1
HET CA A 305 1
HET NA A 306 1
HET NA A 307 1
HET 5EL B 301 34
HET ZN B 302 1
HET ZN B 303 1
HET CA B 304 1
HET CA B 305 1
HET NA B 306 1
HETNAM 5EL 4-(4-{[(3S)-3-HYDROXY-1-AZABICYCLO[2.2.2]OCT-3-
HETNAM 2 5EL YL]ETHYNYL}PHENOXY)-N-(PYRIDIN-4-YLMETHYL)BENZAMIDE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
FORMUL 3 5EL 2(C28 H27 N3 O3)
FORMUL 4 ZN 4(ZN 2+)
FORMUL 5 CA 4(CA 2+)
FORMUL 8 NA 3(NA 1+)
FORMUL 16 HOH *297(H2 O)
HELIX 1 1 THR A 130 ASP A 147 1 18
HELIX 2 2 LEU A 216 GLY A 229 1 14
HELIX 3 3 PRO A 255 GLY A 267 1 13
HELIX 4 4 THR B 130 ASP B 147 1 18
HELIX 5 5 LEU B 216 GLY B 229 1 14
HELIX 6 6 PRO B 255 GLY B 267 1 13
SHEET 1 AA 2 ASN A 105 VAL A 106 0
SHEET 2 AA 2 LEU B 230 ASP B 231 -1 O ASP B 231 N ASN A 105
SHEET 1 AB 5 ASN A 152 LEU A 156 0
SHEET 2 AB 5 ASN A 117 ILE A 122 1 O LEU A 118 N THR A 154
SHEET 3 AB 5 ILE A 163 GLY A 168 1 O ILE A 163 N ARG A 121
SHEET 4 AB 5 ALA A 199 ASP A 202 1 O ALA A 199 N SER A 166
SHEET 5 AB 5 ALA A 186 ALA A 188 -1 O HIS A 187 N HIS A 200
SHEET 1 AC 2 TRP A 207 THR A 208 0
SHEET 2 AC 2 TYR A 214 ASN A 215 1 O TYR A 214 N THR A 208
SHEET 1 BA 5 ASN B 152 ARG B 155 0
SHEET 2 BA 5 ASN B 117 ILE B 122 1 O LEU B 118 N THR B 154
SHEET 3 BA 5 ILE B 163 GLY B 168 1 O ILE B 163 N ARG B 121
SHEET 4 BA 5 ALA B 199 ASP B 202 1 O ALA B 199 N SER B 166
SHEET 5 BA 5 ALA B 186 ALA B 188 -1 O HIS B 187 N HIS B 200
SHEET 1 BB 2 TRP B 207 THR B 208 0
SHEET 2 BB 2 TYR B 214 ASN B 215 1 O TYR B 214 N THR B 208
LINK OD2 ASP A 128 NA NA A 306 1555 1555 2.50
LINK O ASP A 162 CA CA A 303 1555 1555 2.25
LINK NE2 HIS A 172 ZN ZN A 304 1555 1555 2.01
LINK OD2 ASP A 174 ZN ZN A 304 1555 1555 2.01
LINK OD1 ASP A 179 CA CA A 305 1555 1555 2.38
LINK O GLY A 180 CA CA A 305 1555 1555 2.27
LINK O SER A 182 CA CA A 305 1555 1555 2.34
LINK O LEU A 184 CA CA A 305 1555 1555 2.29
LINK NE2 HIS A 187 ZN ZN A 304 1555 1555 2.13
LINK O ASN A 194 CA CA A 303 1555 1555 2.29
LINK O GLY A 196 CA CA A 303 1555 1555 2.32
LINK OD1 ASP A 198 CA CA A 303 1555 1555 2.39
LINK ND1 HIS A 200 ZN ZN A 304 1555 1555 2.05
LINK OD2 ASP A 202 CA CA A 305 1555 1555 2.26
LINK O ASP A 203 NA NA A 306 1555 1555 2.87
LINK OD1 ASP A 203 NA NA A 306 1555 1555 2.93
LINK O GLU A 205 NA NA A 306 1555 1555 2.43
LINK OE2 GLU A 205 CA CA A 305 1555 1555 2.22
LINK NE2 HIS A 222 ZN ZN A 302 1555 1555 2.08
LINK NE2 HIS A 226 ZN ZN A 302 1555 1555 2.14
LINK NE2 HIS A 232 ZN ZN A 302 1555 1555 2.17
LINK OD2 ASP B 128 NA NA B 306 1555 1555 2.51
LINK O ASP B 162 CA CA B 304 1555 1555 2.32
LINK NE2 HIS B 172 ZN ZN B 303 1555 1555 2.13
LINK OD2 ASP B 174 ZN ZN B 303 1555 1555 2.03
LINK OD1 ASP B 179 CA CA B 305 1555 1555 2.36
LINK O GLY B 180 CA CA B 305 1555 1555 2.34
LINK O SER B 182 CA CA B 305 1555 1555 2.27
LINK O LEU B 184 CA CA B 305 1555 1555 2.24
LINK NE2 HIS B 187 ZN ZN B 303 1555 1555 2.04
LINK O ASN B 194 CA CA B 304 1555 1555 2.35
LINK O GLY B 196 CA CA B 304 1555 1555 2.28
LINK OD1 ASP B 198 CA CA B 304 1555 1555 2.45
LINK ND1 HIS B 200 ZN ZN B 303 1555 1555 2.13
LINK OD2 ASP B 202 CA CA B 305 1555 1555 2.34
LINK O ASP B 203 NA NA B 306 1555 1555 2.98
LINK OD1 ASP B 203 NA NA B 306 1555 1555 2.74
LINK O GLU B 205 NA NA B 306 1555 1555 2.57
LINK OE2 GLU B 205 CA CA B 305 1555 1555 2.18
LINK NE2 HIS B 222 ZN ZN B 302 1555 1555 2.10
LINK NE2 HIS B 226 ZN ZN B 302 1555 1555 2.11
LINK NE2 HIS B 232 ZN ZN B 302 1555 1555 2.08
LINK ZN ZN A 302 O HOH A 480 1555 1555 2.26
LINK CA CA A 303 O HOH A 464 1555 1555 2.43
LINK CA CA A 303 O HOH A 431 1555 1555 2.38
LINK NA NA A 307 O HOH A 504 1555 1555 2.40
LINK NA NA A 307 O HOH A 543 1555 1555 2.08
LINK NA NA A 307 O HOH A 481 1555 1555 2.44
LINK NA NA A 307 O HOH A 551 1555 1555 1.95
LINK ZN ZN B 302 O HOH B 500 1555 1555 2.18
LINK CA CA B 304 O HOH B 414 1555 1555 2.41
LINK CA CA B 304 O HOH B 416 1555 1555 2.39
LINK NA NA A 306 O HOH B 476 1555 2656 3.12
LINK NA NA B 306 O HOH A 533 1555 2656 2.87
SITE 1 AC1 15 GLY A 183 LEU A 185 LEU A 218 HIS A 222
SITE 2 AC1 15 GLU A 223 GLY A 237 LEU A 239 PHE A 241
SITE 3 AC1 15 PRO A 242 ILE A 243 TYR A 244 THR A 245
SITE 4 AC1 15 THR A 247 HOH A 418 HOH A 427
SITE 1 AC2 16 GLY B 183 LEU B 184 LEU B 185 HIS B 222
SITE 2 AC2 16 GLU B 223 GLY B 237 LEU B 239 PHE B 241
SITE 3 AC2 16 PRO B 242 ILE B 243 TYR B 244 THR B 245
SITE 4 AC2 16 THR B 247 PHE B 252 HOH B 406 HOH B 434
SITE 1 AC3 4 HIS B 222 HIS B 226 HIS B 232 HOH B 500
SITE 1 AC4 4 HIS B 172 ASP B 174 HIS B 187 HIS B 200
SITE 1 AC5 6 ASP B 162 ASN B 194 GLY B 196 ASP B 198
SITE 2 AC5 6 HOH B 416 HOH B 414
SITE 1 AC6 6 ASP B 179 GLY B 180 SER B 182 LEU B 184
SITE 2 AC6 6 ASP B 202 GLU B 205
SITE 1 AC7 4 HIS A 222 HIS A 226 HIS A 232 HOH A 480
SITE 1 AC8 6 ASP A 162 ASN A 194 GLY A 196 ASP A 198
SITE 2 AC8 6 HOH A 431 HOH A 464
SITE 1 AC9 4 HIS A 172 ASP A 174 HIS A 187 HIS A 200
SITE 1 BC1 6 ASP A 179 GLY A 180 SER A 182 LEU A 184
SITE 2 BC1 6 ASP A 202 GLU A 205
SITE 1 BC2 3 ASP A 128 ASP A 203 GLU A 205
SITE 1 BC3 5 THR B 126 ASP B 128 ASP B 203 GLU B 205
SITE 2 BC3 5 HOH A 533
SITE 1 BC4 5 ALA A 188 HOH A 504 HOH A 481 HOH A 543
SITE 2 BC4 5 HOH A 551
CRYST1 134.417 36.074 95.206 90.00 131.49 90.00 C 1 2 1 8
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 0.007440 0.000000 0.006580 0.00000
SCALE2 0.000000 0.027721 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014022 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
