HEADER HYDROLASE 18-MAR-03 1OS2
TITLE TERNARY ENZYME-PRODUCT-INHIBITOR COMPLEXES OF HUMAN MMP12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE METALLOELASTASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
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 OR HME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MATRIX METALLOPROTEINASE, HYDROXAMIC ACID, MMP12, ELASTASE, COMPLEX
KEYWDS 2 (ELASTASE-INHIBITOR), METALLO ELASTASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BERTINI,V.CALDERONE,M.FRAGAI,C.LUCHINAT,S.MANGANI,B.TERNI
REVDAT 6 16-AUG-23 1OS2 1 REMARK
REVDAT 5 27-OCT-21 1OS2 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1OS2 1 VERSN
REVDAT 3 15-FEB-05 1OS2 1 JRNL
REVDAT 2 10-FEB-04 1OS2 1 LINK
REVDAT 1 05-AUG-03 1OS2 0
JRNL AUTH I.BERTINI,V.CALDERONE,M.FRAGAI,C.LUCHINAT,S.MANGANI,B.TERNI
JRNL TITL X-RAY STRUCTURES OF BINARY AND TERNARY
JRNL TITL 2 ENZYME-PRODUCT-INHIBITOR COMPLEXES OF MATRIX
JRNL TITL 3 METALLOPROTEINASES
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 42 2673 2003
JRNL REFN ESSN 0570-0833
JRNL PMID 12813751
JRNL DOI 10.1002/ANIE.200350957
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.LANG,A.KOCOUREK,M.BRAUN,H.TSCHESCHE,R.HUBER,W.BODE,
REMARK 1 AUTH 2 K.MASKOS
REMARK 1 TITL SUBSTRATE SPECIFICITY DETERMINANTS OF HUMAN MACROPHAGE
REMARK 1 TITL 2 ELASTASE (MMP-12) BASED ON THE 1.1 A CRYSTAL STRUCTURE
REMARK 1 REF J.MOL.BIOL. V. 312 731 2001
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2001.4954
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.80
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 61741
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3296
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4512
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.871
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8016 ; 0.035 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10852 ; 2.763 ; 1.916
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 984 ; 9.963 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1110 ; 0.233 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6334 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3395 ; 0.312 ; 0.200
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): 156 ; 0.482 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 116 ; 0.452 ; 0.200
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): 4884 ; 1.667 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7804 ; 2.718 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3132 ; 4.425 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3048 ; 6.140 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9322
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : SI (111) MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64964
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 107.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.07800
REMARK 200 R SYM FOR SHELL (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1JK3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG6000, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.24333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.48667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
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 300 REMARK: THE PROTEIN IS MONOMERIC IN VIVO, WHILE THERE ARE SIX
REMARK 300 MOLECULES IN THE CRYSTAL ASYMMETRIC UNIT.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -200.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -197.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 61.91950
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 107.24772
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 46.48667
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 ASN E 246 N PHE E 248 1.78
REMARK 500 OH TYR B 121 O HOH B 437 1.88
REMARK 500 O HOH D 577 O HOH D 612 1.90
REMARK 500 ND2 ASN A 246 O HOH A 918 1.93
REMARK 500 NH2 ARG E 127 O HOH E 731 1.97
REMARK 500 OXT ASN A 268 O HOH A 905 2.07
REMARK 500 CE LYS C 136 CD1 ILE C 245 2.08
REMARK 500 CE LYS F 136 CD1 ILE F 245 2.14
REMARK 500 O HOH A 904 O HOH B 387 2.14
REMARK 500 OD2 ASP C 231 N LYS C 233 2.16
REMARK 500 CD PRO E 107 O HOH E 705 2.19
REMARK 500 NH1 ARG B 117 O GLY B 155 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS B 233 NH1 ARG E 249 1554 2.07
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 ALA A 137 CA ALA A 137 CB 0.153
REMARK 500 MET A 156 C MET A 156 O 0.165
REMARK 500 PHE B 138 CZ PHE B 138 CE2 0.117
REMARK 500 SER B 142 CB SER B 142 OG -0.081
REMARK 500 TYR C 116 CD1 TYR C 116 CE1 0.091
REMARK 500 ARG D 117 CG ARG D 117 CD 0.152
REMARK 500 ALA D 137 CA ALA D 137 CB 0.130
REMARK 500 GLN D 139 CG GLN D 139 CD 0.180
REMARK 500 ASN D 246 CB ASN D 246 CG 0.171
REMARK 500 TYR E 113 CD1 TYR E 113 CE1 0.098
REMARK 500 TYR E 132 CE2 TYR E 132 CD2 0.091
REMARK 500 GLU E 199 CD GLU E 199 OE1 -0.084
REMARK 500 ARG F 135 CG ARG F 135 CD 0.156
REMARK 500 ALA F 252 CA ALA F 252 CB 0.153
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 ASP A 124 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 MET A 156 C - N - CA ANGL. DEV. = -15.4 DEGREES
REMARK 500 ASP A 170 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 194 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 231 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 253 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 LYS A 266 CB - CA - C ANGL. DEV. = 14.2 DEGREES
REMARK 500 ASN B 119 CB - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 ASP B 129 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 160 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 LEU B 160 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ASP B 194 CB - CG - OD2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP B 254 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU B 261 CB - CG - CD1 ANGL. DEV. = -15.4 DEGREES
REMARK 500 ASP C 124 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP C 131 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG C 135 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 171 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP C 175 CB - CG - OD2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU C 181 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP C 198 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP C 200 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP C 231 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP C 253 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP C 254 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP C 264 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 MET D 105 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP D 124 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU D 160 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP D 170 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP D 194 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP D 198 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 231 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASN E 119 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASP E 158 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU E 160 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ALA E 167 C - N - CA ANGL. DEV. = -31.8 DEGREES
REMARK 500 ALA E 167 CA - C - N ANGL. DEV. = -18.2 DEGREES
REMARK 500 ASP E 175 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP E 194 CB - CG - OD2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 ASP E 198 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 VAL E 243 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASP E 244 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASN E 246 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 ASP E 254 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG F 117 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP F 124 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP F 131 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP F 175 CB - CG - OD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 LEU F 181 CB - CG - CD1 ANGL. DEV. = -13.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 ARG A 110 43.42 -106.64
REMARK 500 HIS A 206 -159.54 -142.13
REMARK 500 LYS A 266 80.47 123.18
REMARK 500 ARG B 110 48.70 -103.37
REMARK 500 HIS B 168 34.93 -146.38
REMARK 500 ASP B 170 -169.60 -114.26
REMARK 500 SER B 189 151.70 -49.71
REMARK 500 ASP B 264 132.60 104.30
REMARK 500 LYS B 266 76.77 162.49
REMARK 500 GLU B 267 157.82 156.35
REMARK 500 PRO C 146 0.17 -67.81
REMARK 500 HIS C 168 21.90 -142.01
REMARK 500 ASP C 170 -163.29 -118.87
REMARK 500 ALA C 182 148.66 179.97
REMARK 500 HIS C 206 -143.58 -141.80
REMARK 500 ILE C 245 27.93 -48.88
REMARK 500 ASN C 246 -50.11 -123.71
REMARK 500 THR C 247 -39.01 -28.18
REMARK 500 LYS C 266 -9.08 143.15
REMARK 500 GLU C 267 -162.42 -18.37
REMARK 500 ARG D 110 34.18 -94.80
REMARK 500 LYS D 266 78.64 98.73
REMARK 500 ARG E 110 51.21 -100.12
REMARK 500 LYS E 111 155.48 176.52
REMARK 500 ASP E 170 -167.94 -110.28
REMARK 500 ASP E 171 31.26 -99.20
REMARK 500 ASN E 246 -103.68 -73.09
REMARK 500 THR E 247 -23.19 -4.17
REMARK 500 LYS E 266 18.64 147.55
REMARK 500 PHE F 174 -169.15 -74.65
REMARK 500 ASP F 175 26.74 -146.24
REMARK 500 HIS F 206 -149.03 -143.38
REMARK 500 ILE F 245 -19.31 -37.35
REMARK 500 LYS F 266 107.04 168.43
REMARK 500 GLU F 267 -162.94 161.94
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 PRO A 265 LYS A 266 -41.12
REMARK 500 PRO B 265 LYS B 266 -33.06
REMARK 500 LYS B 266 GLU B 267 -135.56
REMARK 500 ILE C 245 ASN C 246 133.56
REMARK 500 LYS C 266 GLU C 267 136.82
REMARK 500 ALA E 167 HIS E 168 -141.69
REMARK 500 LYS E 266 GLU E 267 145.41
REMARK 500 MET F 104 MET F 105 123.50
REMARK 500 ILE F 245 ASN F 246 149.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET A 156 21.04
REMARK 500 MET E 125 -11.57
REMARK 500 ALA E 167 15.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HET GROUP TRIVIAL NAME: HAE IS ALSO KNOWN AS ACETOHYDROXAMIC ACID
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 873 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD1
REMARK 620 2 ASP A 124 OD2 50.3
REMARK 620 3 GLU A 199 O 130.6 167.3
REMARK 620 4 GLU A 199 OE2 84.6 84.6 82.9
REMARK 620 5 GLU A 201 O 76.7 120.7 68.2 118.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 872 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 158 O
REMARK 620 2 GLY A 190 O 168.6
REMARK 620 3 GLY A 192 O 99.9 90.8
REMARK 620 4 ASP A 194 OD2 86.4 90.5 86.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 870 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 168 NE2
REMARK 620 2 ASP A 170 OD1 90.5
REMARK 620 3 HIS A 183 NE2 116.3 131.8
REMARK 620 4 HIS A 196 ND1 117.1 87.2 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 871 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 175 OD2
REMARK 620 2 GLY A 176 O 84.8
REMARK 620 3 GLY A 178 O 87.9 82.5
REMARK 620 4 ILE A 180 O 89.3 174.1 97.8
REMARK 620 5 ASP A 198 OD1 97.3 89.4 170.0 90.8
REMARK 620 6 GLU A 201 OE2 175.8 99.0 90.9 86.9 84.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 869 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 218 NE2
REMARK 620 2 HIS A 222 NE2 98.6
REMARK 620 3 HIS A 228 NE2 96.2 92.2
REMARK 620 4 HAE A 874 O2 153.1 106.9 91.4
REMARK 620 5 HAE A 874 O 96.5 105.5 156.3 68.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 373 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 124 OD1
REMARK 620 2 ASP B 124 OD2 52.0
REMARK 620 3 GLU B 199 O 135.8 155.6
REMARK 620 4 GLU B 199 OE2 91.0 80.8 76.3
REMARK 620 5 GLU B 201 O 72.8 122.8 76.1 117.3
REMARK 620 6 HOH B 393 O 139.7 87.7 80.9 81.7 144.8
REMARK 620 7 HOH B 430 O 99.9 92.4 106.3 159.8 82.4 79.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 372 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 158 O
REMARK 620 2 GLY B 190 O 165.7
REMARK 620 3 GLY B 192 O 90.3 98.9
REMARK 620 4 ASP B 194 OD2 95.2 95.0 94.7
REMARK 620 5 HOH B 397 O 90.7 80.7 177.1 82.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 370 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 168 NE2
REMARK 620 2 ASP B 170 OD1 110.7
REMARK 620 3 HIS B 183 NE2 117.0 120.2
REMARK 620 4 HIS B 196 ND1 113.4 91.4 100.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 371 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 175 OD2
REMARK 620 2 GLY B 176 O 87.7
REMARK 620 3 GLY B 178 O 93.5 93.4
REMARK 620 4 ILE B 180 O 84.9 172.5 87.6
REMARK 620 5 ASP B 198 OD1 81.3 86.6 174.9 91.6
REMARK 620 6 GLU B 201 OE2 173.3 94.6 92.6 92.7 92.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 369 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 218 NE2
REMARK 620 2 HIS B 222 NE2 107.1
REMARK 620 3 HIS B 228 NE2 96.5 99.2
REMARK 620 4 ACT B 374 OXT 111.2 127.2 110.8
REMARK 620 5 ACT B 374 O 146.8 103.3 91.4 36.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 473 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 124 OD1
REMARK 620 2 ASP C 124 OD2 47.4
REMARK 620 3 GLU C 199 O 151.7 154.0
REMARK 620 4 GLU C 199 OE2 89.5 82.9 80.9
REMARK 620 5 GLU C 201 O 81.0 124.2 81.7 122.0
REMARK 620 6 HOH C 506 O 122.3 75.1 81.6 77.5 151.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 472 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 158 O
REMARK 620 2 GLY C 190 O 169.6
REMARK 620 3 GLY C 192 O 99.6 89.2
REMARK 620 4 ASP C 194 OD2 83.6 102.7 86.6
REMARK 620 5 HOH C 494 O 86.8 88.2 85.3 166.3
REMARK 620 6 HOH C 520 O 84.0 86.4 168.5 104.7 84.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 470 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 168 NE2
REMARK 620 2 ASP C 170 OD1 104.5
REMARK 620 3 HIS C 183 NE2 127.4 114.1
REMARK 620 4 HIS C 196 ND1 99.7 101.5 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 471 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 175 OD2
REMARK 620 2 GLY C 176 O 85.2
REMARK 620 3 GLY C 178 O 86.6 85.4
REMARK 620 4 ILE C 180 O 91.6 176.2 92.4
REMARK 620 5 ASP C 198 OD1 88.7 86.3 170.7 95.7
REMARK 620 6 GLU C 201 OE2 175.0 91.8 89.1 91.2 95.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 469 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 218 NE2
REMARK 620 2 HIS C 222 NE2 98.7
REMARK 620 3 HIS C 228 NE2 80.4 92.8
REMARK 620 4 AZI C 474 N3 111.3 105.9 155.6
REMARK 620 5 AZI C 474 N2 135.6 111.3 127.8 30.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 573 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 124 OD1
REMARK 620 2 ASP D 124 OD2 51.1
REMARK 620 3 GLU D 199 O 130.1 168.3
REMARK 620 4 GLU D 199 OE2 86.2 83.3 85.1
REMARK 620 5 GLU D 201 O 73.3 119.3 68.5 118.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 572 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 158 O
REMARK 620 2 GLY D 190 O 167.7
REMARK 620 3 GLY D 192 O 100.6 87.6
REMARK 620 4 ASP D 194 OD2 94.3 95.4 86.5
REMARK 620 5 HOH D 598 O 82.8 88.8 176.3 94.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 570 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 168 NE2
REMARK 620 2 ASP D 170 OD1 102.1
REMARK 620 3 HIS D 183 NE2 122.5 119.8
REMARK 620 4 HIS D 196 ND1 120.8 88.9 98.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 571 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 175 OD2
REMARK 620 2 GLY D 176 O 81.9
REMARK 620 3 GLY D 178 O 82.0 81.3
REMARK 620 4 ILE D 180 O 86.3 167.5 93.1
REMARK 620 5 ASP D 198 OD1 101.0 89.8 170.2 96.4
REMARK 620 6 GLU D 201 OE2 167.5 104.5 88.2 86.4 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 569 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 218 NE2
REMARK 620 2 HIS D 222 NE2 99.6
REMARK 620 3 HIS D 228 NE2 97.8 92.7
REMARK 620 4 HAE D 574 O2 155.6 101.0 94.3
REMARK 620 5 HAE D 574 O 94.4 103.5 157.9 68.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 673 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 124 OD1
REMARK 620 2 ASP E 124 OD2 52.1
REMARK 620 3 GLU E 199 O 137.6 162.6
REMARK 620 4 GLU E 199 OE2 86.7 84.1 82.5
REMARK 620 5 GLU E 201 O 78.5 124.5 72.3 120.6
REMARK 620 6 HOH E 708 O 136.1 84.5 82.7 81.9 142.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 672 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 158 O
REMARK 620 2 GLY E 190 O 166.3
REMARK 620 3 GLY E 192 O 97.5 94.6
REMARK 620 4 ASP E 194 OD2 89.0 97.1 91.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 670 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 168 NE2
REMARK 620 2 ASP E 170 OD1 112.2
REMARK 620 3 HIS E 183 NE2 115.6 115.7
REMARK 620 4 HIS E 196 ND1 111.6 87.5 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 671 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 175 OD2
REMARK 620 2 GLY E 176 O 88.5
REMARK 620 3 GLY E 178 O 92.3 87.8
REMARK 620 4 ILE E 180 O 89.7 172.3 84.8
REMARK 620 5 ASP E 198 OD1 86.3 90.5 177.9 96.8
REMARK 620 6 GLU E 201 OE2 175.8 95.7 88.0 86.1 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 669 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 218 NE2
REMARK 620 2 HIS E 222 NE2 103.1
REMARK 620 3 HIS E 228 NE2 99.2 101.9
REMARK 620 4 ACT E 674 OXT 121.0 133.4 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 773 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 124 OD1
REMARK 620 2 ASP F 124 OD2 49.8
REMARK 620 3 GLU F 199 O 151.3 155.7
REMARK 620 4 GLU F 199 OE2 95.5 81.2 83.6
REMARK 620 5 GLU F 201 O 82.4 129.7 74.5 123.6
REMARK 620 6 HOH F 802 O 143.4 94.4 65.2 84.4 127.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 772 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 158 O
REMARK 620 2 GLY F 190 O 170.4
REMARK 620 3 GLY F 192 O 98.3 81.9
REMARK 620 4 ASP F 194 OD2 85.8 103.8 88.7
REMARK 620 5 HOH F 786 O 86.2 84.3 84.8 168.9
REMARK 620 6 HOH F 812 O 89.8 87.7 163.3 106.5 81.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 770 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 168 NE2
REMARK 620 2 ASP F 170 OD1 106.2
REMARK 620 3 HIS F 183 NE2 124.8 112.8
REMARK 620 4 HIS F 196 ND1 102.0 102.6 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 771 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 175 OD2
REMARK 620 2 GLY F 176 O 81.7
REMARK 620 3 GLY F 178 O 84.2 81.0
REMARK 620 4 ILE F 180 O 93.4 175.1 97.8
REMARK 620 5 ASP F 198 OD1 91.0 87.5 168.0 93.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 769 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 218 NE2
REMARK 620 2 HIS F 222 NE2 102.4
REMARK 620 3 HIS F 228 NE2 80.8 91.1
REMARK 620 4 AZI F 774 N3 127.8 101.0 144.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 869
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 870
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 871
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 872
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 873
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI C 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 569
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 570
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 571
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 572
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 573
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 669
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 769
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 770
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 771
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 772
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 773
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI F 774
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAE A 874
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAE D 574
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MMP-12 (MACROPHAGE ELASTASE) AT TRUE
REMARK 900 ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1OS9 RELATED DB: PDB
REMARK 900 BINARY ENZYME-PRODUCT COMPLEXES OF HUMAN MMP12
DBREF 1OS2 A 106 268 UNP P39900 MMP12_HUMAN 106 268
DBREF 1OS2 B 106 268 UNP P39900 MMP12_HUMAN 106 268
DBREF 1OS2 C 106 268 UNP P39900 MMP12_HUMAN 106 268
DBREF 1OS2 D 106 268 UNP P39900 MMP12_HUMAN 106 268
DBREF 1OS2 E 106 268 UNP P39900 MMP12_HUMAN 106 268
DBREF 1OS2 F 106 268 UNP P39900 MMP12_HUMAN 106 268
SEQADV 1OS2 MET A 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET A 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP A 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQADV 1OS2 MET B 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET B 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP B 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQADV 1OS2 MET C 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET C 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP C 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQADV 1OS2 MET D 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET D 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP D 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQADV 1OS2 MET E 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET E 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP E 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQADV 1OS2 MET F 104 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 MET F 105 UNP P39900 CLONING ARTIFACT
SEQADV 1OS2 ASP F 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQRES 1 A 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 A 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 A 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 A 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 A 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 A 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 A 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 A 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 A 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 A 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 A 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 A 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 A 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
SEQRES 1 B 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 B 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 B 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 B 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 B 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 B 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 B 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 B 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 B 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 B 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 B 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 B 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 B 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
SEQRES 1 C 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 C 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 C 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 C 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 C 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 C 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 C 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 C 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 C 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 C 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 C 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 C 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 C 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
SEQRES 1 D 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 D 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 D 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 D 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 D 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 D 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 D 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 D 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 D 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 D 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 D 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 D 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 D 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
SEQRES 1 E 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 E 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 E 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 E 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 E 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 E 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 E 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 E 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 E 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 E 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 E 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 E 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 E 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
SEQRES 1 F 165 MET MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR
SEQRES 2 F 165 ARG ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP
SEQRES 3 F 165 VAL ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER
SEQRES 4 F 165 ASN VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY
SEQRES 5 F 165 MET ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS
SEQRES 6 F 165 GLY ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU
SEQRES 7 F 165 ALA HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP
SEQRES 8 F 165 ALA HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER
SEQRES 9 F 165 GLY GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE
SEQRES 10 F 165 GLY HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS
SEQRES 11 F 165 ALA VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN
SEQRES 12 F 165 THR PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN
SEQRES 13 F 165 SER LEU TYR GLY ASP PRO LYS GLU ASN
HET ZN A 869 1
HET ZN A 870 1
HET CA A 871 1
HET CA A 872 1
HET CA A 873 1
HET HAE A 874 5
HET ZN B 369 1
HET ZN B 370 1
HET CA B 371 1
HET CA B 372 1
HET CA B 373 1
HET ACT B 374 4
HET ZN C 469 1
HET ZN C 470 1
HET CA C 471 1
HET CA C 472 1
HET CA C 473 1
HET AZI C 474 3
HET ZN D 569 1
HET ZN D 570 1
HET CA D 571 1
HET CA D 572 1
HET CA D 573 1
HET HAE D 574 5
HET ZN E 669 1
HET ZN E 670 1
HET CA E 671 1
HET CA E 672 1
HET CA E 673 1
HET ACT E 674 4
HET ZN F 769 1
HET ZN F 770 1
HET CA F 771 1
HET CA F 772 1
HET CA F 773 1
HET AZI F 774 3
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM HAE ACETOHYDROXAMIC ACID
HETNAM ACT ACETATE ION
HETNAM AZI AZIDE ION
FORMUL 7 ZN 12(ZN 2+)
FORMUL 9 CA 18(CA 2+)
FORMUL 12 HAE 2(C2 H5 N O2)
FORMUL 18 ACT 2(C2 H3 O2 1-)
FORMUL 24 AZI 2(N3 1-)
FORMUL 43 HOH *308(H2 O)
HELIX 1 1 ASN A 126 ASN A 143 1 18
HELIX 2 2 LEU A 212 LEU A 224 1 13
HELIX 3 3 SER A 251 GLY A 263 1 13
HELIX 4 4 ASN B 126 ASN B 143 1 18
HELIX 5 5 LEU B 212 LEU B 224 1 13
HELIX 6 6 ASP B 244 PHE B 248 5 5
HELIX 7 7 SER B 251 GLY B 263 1 13
HELIX 8 8 ASN C 126 VAL C 144 1 19
HELIX 9 9 LEU C 212 LEU C 224 1 13
HELIX 10 10 SER C 251 GLY C 263 1 13
HELIX 11 11 ASN D 126 ASN D 143 1 18
HELIX 12 12 LEU D 212 LEU D 224 1 13
HELIX 13 13 SER D 251 GLY D 263 1 13
HELIX 14 14 ASN E 126 ASN E 143 1 18
HELIX 15 15 LEU E 212 LEU E 224 1 13
HELIX 16 16 SER E 251 GLY E 263 1 13
HELIX 17 17 ASN F 126 ASN F 143 1 18
HELIX 18 18 LEU F 212 LEU F 224 1 13
HELIX 19 19 SER F 251 GLY F 263 1 13
SHEET 1 A 5 LYS A 148 LYS A 151 0
SHEET 2 A 5 TYR A 113 ILE A 118 1 N ILE A 114 O LYS A 148
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
SHEET 1 C 5 LYS B 148 LYS B 151 0
SHEET 2 C 5 TYR B 113 ILE B 118 1 N ILE B 114 O LYS B 148
SHEET 3 C 5 ILE B 159 ALA B 164 1 O VAL B 161 N ARG B 117
SHEET 4 C 5 ALA B 195 ASP B 198 1 O PHE B 197 N VAL B 162
SHEET 5 C 5 ALA B 182 ALA B 184 -1 N HIS B 183 O HIS B 196
SHEET 1 D 2 TRP B 203 THR B 204 0
SHEET 2 D 2 THR B 210 ASN B 211 1 O THR B 210 N THR B 204
SHEET 1 E 5 LYS C 148 LYS C 151 0
SHEET 2 E 5 TYR C 113 ILE C 118 1 N ILE C 114 O SER C 150
SHEET 3 E 5 ILE C 159 ALA C 164 1 O VAL C 161 N ARG C 117
SHEET 4 E 5 ALA C 195 ASP C 198 1 O PHE C 197 N VAL C 162
SHEET 5 E 5 ALA C 182 ALA C 184 -1 N HIS C 183 O HIS C 196
SHEET 1 F 2 TRP C 203 THR C 204 0
SHEET 2 F 2 THR C 210 ASN C 211 1 O THR C 210 N THR C 204
SHEET 1 G 5 LYS D 148 LYS D 151 0
SHEET 2 G 5 TYR D 113 ILE D 118 1 N ILE D 114 O LYS D 148
SHEET 3 G 5 ILE D 159 ALA D 164 1 O VAL D 161 N ARG D 117
SHEET 4 G 5 ALA D 195 ASP D 198 1 O PHE D 197 N VAL D 162
SHEET 5 G 5 ALA D 182 ALA D 184 -1 N HIS D 183 O HIS D 196
SHEET 1 H 2 TRP D 203 THR D 204 0
SHEET 2 H 2 THR D 210 ASN D 211 1 O THR D 210 N THR D 204
SHEET 1 I 2 MET E 105 PRO E 107 0
SHEET 2 I 2 THR F 239 TYR F 240 1 O TYR F 240 N MET E 105
SHEET 1 J 5 LYS E 148 LYS E 151 0
SHEET 2 J 5 TYR E 113 ILE E 118 1 N ILE E 114 O LYS E 148
SHEET 3 J 5 ILE E 159 ALA E 164 1 O VAL E 161 N ARG E 117
SHEET 4 J 5 ALA E 195 ASP E 198 1 O PHE E 197 N VAL E 162
SHEET 5 J 5 ALA E 182 ALA E 184 -1 N HIS E 183 O HIS E 196
SHEET 1 K 2 TRP E 203 THR E 204 0
SHEET 2 K 2 THR E 210 ASN E 211 1 O THR E 210 N THR E 204
SHEET 1 L 5 LYS F 148 LYS F 151 0
SHEET 2 L 5 TYR F 113 ILE F 118 1 N ILE F 114 O SER F 150
SHEET 3 L 5 ILE F 159 ALA F 164 1 O VAL F 161 N ARG F 117
SHEET 4 L 5 ALA F 195 ASP F 198 1 O PHE F 197 N VAL F 162
SHEET 5 L 5 ALA F 182 ALA F 184 -1 N HIS F 183 O HIS F 196
SHEET 1 M 2 TRP F 203 THR F 204 0
SHEET 2 M 2 THR F 210 ASN F 211 1 O THR F 210 N THR F 204
LINK OD1 ASP A 124 CA CA A 873 1555 1555 2.64
LINK OD2 ASP A 124 CA CA A 873 1555 1555 2.27
LINK O ASP A 158 CA CA A 872 1555 1555 2.25
LINK NE2 HIS A 168 ZN ZN A 870 1555 1555 1.87
LINK OD1 ASP A 170 ZN ZN A 870 1555 1555 2.32
LINK OD2 ASP A 175 CA CA A 871 1555 1555 2.38
LINK O GLY A 176 CA CA A 871 1555 1555 2.17
LINK O GLY A 178 CA CA A 871 1555 1555 2.10
LINK O ILE A 180 CA CA A 871 1555 1555 2.27
LINK NE2AHIS A 183 ZN ZN A 870 1555 1555 2.00
LINK O GLY A 190 CA CA A 872 1555 1555 2.40
LINK O GLY A 192 CA CA A 872 1555 1555 2.29
LINK OD2 ASP A 194 CA CA A 872 1555 1555 2.55
LINK ND1 HIS A 196 ZN ZN A 870 1555 1555 2.01
LINK OD1 ASP A 198 CA CA A 871 1555 1555 2.31
LINK O GLU A 199 CA CA A 873 1555 1555 2.50
LINK OE2 GLU A 199 CA CA A 873 1555 1555 2.33
LINK OE2 GLU A 201 CA CA A 871 1555 1555 2.43
LINK O GLU A 201 CA CA A 873 1555 1555 2.45
LINK NE2 HIS A 218 ZN ZN A 869 1555 1555 2.34
LINK NE2 HIS A 222 ZN ZN A 869 1555 1555 2.07
LINK NE2 HIS A 228 ZN ZN A 869 1555 1555 2.03
LINK ZN ZN A 869 O2 HAE A 874 1555 1555 2.23
LINK ZN ZN A 869 O HAE A 874 1555 1555 1.91
LINK OD1 ASP B 124 CA CA B 373 1555 1555 2.60
LINK OD2 ASP B 124 CA CA B 373 1555 1555 2.43
LINK O ASP B 158 CA CA B 372 1555 1555 2.44
LINK NE2 HIS B 168 ZN ZN B 370 1555 1555 2.00
LINK OD1 ASP B 170 ZN ZN B 370 1555 1555 1.94
LINK OD2 ASP B 175 CA CA B 371 1555 1555 2.44
LINK O GLY B 176 CA CA B 371 1555 1555 2.15
LINK O GLY B 178 CA CA B 371 1555 1555 2.13
LINK O ILE B 180 CA CA B 371 1555 1555 2.11
LINK NE2AHIS B 183 ZN ZN B 370 1555 1555 2.01
LINK O GLY B 190 CA CA B 372 1555 1555 2.34
LINK O GLY B 192 CA CA B 372 1555 1555 2.39
LINK OD2 ASP B 194 CA CA B 372 1555 1555 2.38
LINK ND1 HIS B 196 ZN ZN B 370 1555 1555 2.15
LINK OD1 ASP B 198 CA CA B 371 1555 1555 2.54
LINK O GLU B 199 CA CA B 373 1555 1555 2.43
LINK OE2 GLU B 199 CA CA B 373 1555 1555 2.04
LINK OE2 GLU B 201 CA CA B 371 1555 1555 2.23
LINK O GLU B 201 CA CA B 373 1555 1555 2.34
LINK NE2 HIS B 218 ZN ZN B 369 1555 1555 2.10
LINK NE2 HIS B 222 ZN ZN B 369 1555 1555 2.01
LINK NE2 HIS B 228 ZN ZN B 369 1555 1555 2.17
LINK ZN ZN B 369 OXT ACT B 374 1555 1555 2.82
LINK ZN ZN B 369 O ACT B 374 1555 1555 1.99
LINK CA CA B 372 O HOH B 397 1555 1555 2.46
LINK CA CA B 373 O HOH B 393 1555 1555 2.53
LINK CA CA B 373 O HOH B 430 1555 1555 2.10
LINK OD1 ASP C 124 CA CA C 473 1555 1555 2.21
LINK OD2 ASP C 124 CA CA C 473 1555 1555 2.94
LINK O ASP C 158 CA CA C 472 1555 1555 2.22
LINK NE2 HIS C 168 ZN ZN C 470 1555 1555 1.85
LINK OD1 ASP C 170 ZN ZN C 470 1555 1555 2.04
LINK OD2 ASP C 175 CA CA C 471 1555 1555 2.04
LINK O GLY C 176 CA CA C 471 1555 1555 2.37
LINK O GLY C 178 CA CA C 471 1555 1555 2.30
LINK O ILE C 180 CA CA C 471 1555 1555 2.35
LINK NE2AHIS C 183 ZN ZN C 470 1555 1555 1.86
LINK O GLY C 190 CA CA C 472 1555 1555 2.38
LINK O GLY C 192 CA CA C 472 1555 1555 2.20
LINK OD2 ASP C 194 CA CA C 472 1555 1555 2.54
LINK ND1 HIS C 196 ZN ZN C 470 1555 1555 2.24
LINK OD1 ASP C 198 CA CA C 471 1555 1555 2.57
LINK O GLU C 199 CA CA C 473 1555 1555 2.07
LINK OE2 GLU C 199 CA CA C 473 1555 1555 2.51
LINK OE2 GLU C 201 CA CA C 471 1555 1555 2.04
LINK O GLU C 201 CA CA C 473 1555 1555 2.24
LINK NE2 HIS C 218 ZN ZN C 469 1555 1555 1.80
LINK NE2 HIS C 222 ZN ZN C 469 1555 1555 2.25
LINK NE2 HIS C 228 ZN ZN C 469 1555 1555 1.85
LINK ZN ZN C 469 N3 AZI C 474 1555 1555 1.69
LINK ZN ZN C 469 N2 AZI C 474 1555 1555 2.28
LINK CA CA C 472 O HOH C 494 1555 1555 2.42
LINK CA CA C 472 O HOH C 520 1555 1555 2.16
LINK CA CA C 473 O HOH C 506 1555 1555 2.33
LINK OD1 ASP D 124 CA CA D 573 1555 1555 2.61
LINK OD2 ASP D 124 CA CA D 573 1555 1555 2.34
LINK O ASP D 158 CA CA D 572 1555 1555 2.21
LINK NE2 HIS D 168 ZN ZN D 570 1555 1555 1.85
LINK OD1 ASP D 170 ZN ZN D 570 1555 1555 2.17
LINK OD2 ASP D 175 CA CA D 571 1555 1555 2.47
LINK O GLY D 176 CA CA D 571 1555 1555 2.22
LINK O GLY D 178 CA CA D 571 1555 1555 2.16
LINK O ILE D 180 CA CA D 571 1555 1555 2.26
LINK NE2AHIS D 183 ZN ZN D 570 1555 1555 1.97
LINK O GLY D 190 CA CA D 572 1555 1555 2.37
LINK O GLY D 192 CA CA D 572 1555 1555 2.21
LINK OD2 ASP D 194 CA CA D 572 1555 1555 2.36
LINK ND1 HIS D 196 ZN ZN D 570 1555 1555 1.92
LINK OD1 ASP D 198 CA CA D 571 1555 1555 2.31
LINK O GLU D 199 CA CA D 573 1555 1555 2.63
LINK OE2 GLU D 199 CA CA D 573 1555 1555 2.48
LINK OE2 GLU D 201 CA CA D 571 1555 1555 2.49
LINK O GLU D 201 CA CA D 573 1555 1555 2.59
LINK NE2 HIS D 218 ZN ZN D 569 1555 1555 2.23
LINK NE2 HIS D 222 ZN ZN D 569 1555 1555 2.00
LINK NE2 HIS D 228 ZN ZN D 569 1555 1555 2.04
LINK ZN ZN D 569 O2 HAE D 574 1555 1555 2.20
LINK ZN ZN D 569 O HAE D 574 1555 1555 2.02
LINK CA CA D 572 O HOH D 598 1555 1555 2.39
LINK OD1 ASP E 124 CA CA E 673 1555 1555 2.38
LINK OD2 ASP E 124 CA CA E 673 1555 1555 2.59
LINK O ASP E 158 CA CA E 672 1555 1555 2.46
LINK NE2 HIS E 168 ZN ZN E 670 1555 1555 1.94
LINK OD1 ASP E 170 ZN ZN E 670 1555 1555 1.91
LINK OD2 ASP E 175 CA CA E 671 1555 1555 2.41
LINK O GLY E 176 CA CA E 671 1555 1555 2.18
LINK O GLY E 178 CA CA E 671 1555 1555 2.29
LINK O ILE E 180 CA CA E 671 1555 1555 2.10
LINK NE2AHIS E 183 ZN ZN E 670 1555 1555 1.97
LINK O GLY E 190 CA CA E 672 1555 1555 2.29
LINK O GLY E 192 CA CA E 672 1555 1555 2.31
LINK OD2 ASP E 194 CA CA E 672 1555 1555 2.35
LINK ND1 HIS E 196 ZN ZN E 670 1555 1555 2.15
LINK OD1 ASP E 198 CA CA E 671 1555 1555 2.48
LINK O GLU E 199 CA CA E 673 1555 1555 2.43
LINK OE2 GLU E 199 CA CA E 673 1555 1555 2.11
LINK OE2 GLU E 201 CA CA E 671 1555 1555 2.26
LINK O GLU E 201 CA CA E 673 1555 1555 2.37
LINK NE2 HIS E 218 ZN ZN E 669 1555 1555 2.07
LINK NE2 HIS E 222 ZN ZN E 669 1555 1555 1.99
LINK NE2 HIS E 228 ZN ZN E 669 1555 1555 2.17
LINK ZN ZN E 669 OXT ACT E 674 1555 1555 1.75
LINK CA CA E 673 O HOH E 708 1555 1555 2.64
LINK OD1 ASP F 124 CA CA F 773 1555 1555 2.06
LINK OD2 ASP F 124 CA CA F 773 1555 1555 2.84
LINK O ASP F 158 CA CA F 772 1555 1555 2.24
LINK NE2 HIS F 168 ZN ZN F 770 1555 1555 1.89
LINK OD1 ASP F 170 ZN ZN F 770 1555 1555 2.01
LINK OD2 ASP F 175 CA CA F 771 1555 1555 2.00
LINK O GLY F 176 CA CA F 771 1555 1555 2.35
LINK O GLY F 178 CA CA F 771 1555 1555 2.39
LINK O ILE F 180 CA CA F 771 1555 1555 2.40
LINK NE2AHIS F 183 ZN ZN F 770 1555 1555 1.94
LINK O GLY F 190 CA CA F 772 1555 1555 2.31
LINK O GLY F 192 CA CA F 772 1555 1555 2.19
LINK OD2 ASP F 194 CA CA F 772 1555 1555 2.46
LINK ND1 HIS F 196 ZN ZN F 770 1555 1555 2.18
LINK OD1 ASP F 198 CA CA F 771 1555 1555 2.55
LINK O GLU F 199 CA CA F 773 1555 1555 2.13
LINK OE2 GLU F 199 CA CA F 773 1555 1555 2.40
LINK O GLU F 201 CA CA F 773 1555 1555 2.30
LINK NE2 HIS F 218 ZN ZN F 769 1555 1555 1.89
LINK NE2 HIS F 222 ZN ZN F 769 1555 1555 2.16
LINK NE2 HIS F 228 ZN ZN F 769 1555 1555 1.90
LINK ZN ZN F 769 N3 AZI F 774 1555 1555 1.93
LINK CA CA F 772 O HOH F 786 1555 1555 2.43
LINK CA CA F 772 O HOH F 812 1555 1555 2.11
LINK CA CA F 773 O HOH F 802 1555 1555 2.37
CISPEP 1 GLU A 267 ASN A 268 0 2.37
CISPEP 2 GLU B 267 ASN B 268 0 -6.32
CISPEP 3 PRO C 265 LYS C 266 0 -29.31
CISPEP 4 GLU C 267 ASN C 268 0 -14.97
CISPEP 5 PRO D 265 LYS D 266 0 -4.38
CISPEP 6 GLU D 267 ASN D 268 0 -3.00
CISPEP 7 PRO E 265 LYS E 266 0 -14.59
CISPEP 8 GLU E 267 ASN E 268 0 12.58
CISPEP 9 PRO F 265 LYS F 266 0 -25.43
CISPEP 10 GLU F 267 ASN F 268 0 8.28
SITE 1 AC1 4 HIS A 218 HIS A 222 HIS A 228 HAE A 874
SITE 1 AC2 4 HIS A 168 ASP A 170 HIS A 183 HIS A 196
SITE 1 AC3 6 ASP A 175 GLY A 176 GLY A 178 ILE A 180
SITE 2 AC3 6 ASP A 198 GLU A 201
SITE 1 AC4 4 ASP A 158 GLY A 190 GLY A 192 ASP A 194
SITE 1 AC5 3 ASP A 124 GLU A 199 GLU A 201
SITE 1 AC6 4 HIS B 218 HIS B 222 HIS B 228 ACT B 374
SITE 1 AC7 4 HIS B 168 ASP B 170 HIS B 183 HIS B 196
SITE 1 AC8 6 ASP B 175 GLY B 176 GLY B 178 ILE B 180
SITE 2 AC8 6 ASP B 198 GLU B 201
SITE 1 AC9 5 ASP B 158 GLY B 190 GLY B 192 ASP B 194
SITE 2 AC9 5 HOH B 397
SITE 1 BC1 5 ASP B 124 GLU B 199 GLU B 201 HOH B 393
SITE 2 BC1 5 HOH B 430
SITE 1 BC2 5 MET A 104 HIS B 222 HIS B 228 ZN B 369
SITE 2 BC2 5 HOH B 434
SITE 1 BC3 5 MET B 104 HIS C 218 HIS C 222 HIS C 228
SITE 2 BC3 5 AZI C 474
SITE 1 BC4 4 HIS C 168 ASP C 170 HIS C 183 HIS C 196
SITE 1 BC5 6 ASP C 175 GLY C 176 GLY C 178 ILE C 180
SITE 2 BC5 6 ASP C 198 GLU C 201
SITE 1 BC6 6 ASP C 158 GLY C 190 GLY C 192 ASP C 194
SITE 2 BC6 6 HOH C 494 HOH C 520
SITE 1 BC7 5 HOH A 905 ASP C 124 GLU C 199 GLU C 201
SITE 2 BC7 5 HOH C 506
SITE 1 BC8 6 MET B 104 HIS C 218 GLU C 219 HIS C 222
SITE 2 BC8 6 HIS C 228 ZN C 469
SITE 1 BC9 4 HIS D 218 HIS D 222 HIS D 228 HAE D 574
SITE 1 CC1 4 HIS D 168 ASP D 170 HIS D 183 HIS D 196
SITE 1 CC2 6 ASP D 175 GLY D 176 GLY D 178 ILE D 180
SITE 2 CC2 6 ASP D 198 GLU D 201
SITE 1 CC3 5 ASP D 158 GLY D 190 GLY D 192 ASP D 194
SITE 2 CC3 5 HOH D 598
SITE 1 CC4 3 ASP D 124 GLU D 199 GLU D 201
SITE 1 CC5 4 HIS E 218 HIS E 222 HIS E 228 ACT E 674
SITE 1 CC6 4 HIS E 168 ASP E 170 HIS E 183 HIS E 196
SITE 1 CC7 6 ASP E 175 GLY E 176 GLY E 178 ILE E 180
SITE 2 CC7 6 ASP E 198 GLU E 201
SITE 1 CC8 4 ASP E 158 GLY E 190 GLY E 192 ASP E 194
SITE 1 CC9 4 ASP E 124 GLU E 199 GLU E 201 HOH E 708
SITE 1 DC1 8 MET D 104 ALA E 182 HIS E 218 GLU E 219
SITE 2 DC1 8 HIS E 222 HIS E 228 ZN E 669 HOH E 722
SITE 1 DC2 5 MET E 104 HIS F 218 HIS F 222 HIS F 228
SITE 2 DC2 5 AZI F 774
SITE 1 DC3 4 HIS F 168 ASP F 170 HIS F 183 HIS F 196
SITE 1 DC4 6 ASP F 175 GLY F 176 GLY F 178 ILE F 180
SITE 2 DC4 6 ASP F 198 GLU F 201
SITE 1 DC5 6 ASP F 158 GLY F 190 GLY F 192 ASP F 194
SITE 2 DC5 6 HOH F 786 HOH F 812
SITE 1 DC6 4 ASP F 124 GLU F 199 GLU F 201 HOH F 802
SITE 1 DC7 5 MET E 104 HIS F 218 HIS F 222 HIS F 228
SITE 2 DC7 5 ZN F 769
SITE 1 DC8 10 ALA A 182 HIS A 183 HIS A 218 GLU A 219
SITE 2 DC8 10 HIS A 222 HIS A 228 ZN A 869 HOH A 894
SITE 3 DC8 10 HOH A 919 MET C 104
SITE 1 DC9 10 ALA D 182 HIS D 183 HIS D 218 GLU D 219
SITE 2 DC9 10 HIS D 222 HIS D 228 ZN D 569 HOH D 586
SITE 3 DC9 10 HOH D 607 MET F 104
CRYST1 123.839 123.839 69.730 90.00 90.00 120.00 P 31 18
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 0.008075 0.004662 0.000000 0.00000
SCALE2 0.000000 0.009324 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
