HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 03-MAY-05 1ZKP
TITLE 1.5A RESOLUTION CRYSTAL STRUCTURE OF A METALLO BETA LACTAMASE FAMILY
TITLE 2 PROTEIN, THE ELAC HOMOLGUE OF BACILLUS ANTHRACIS, A PUTATIVE
TITLE 3 RIBONUCLEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN BA1088;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR.;
SOURCE 3 ORGANISM_TAXID: 198094;
SOURCE 4 STRAIN: AMES;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ZINC BINDING PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.BRUNZELLE,G.MINASOV,L.SHUVALOVA,F.R.COLLART,W.F.ANDERSON,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 4 11-OCT-17 1ZKP 1 REMARK
REVDAT 3 13-JUL-11 1ZKP 1 VERSN
REVDAT 2 24-FEB-09 1ZKP 1 VERSN
REVDAT 1 21-JUN-05 1ZKP 0
JRNL AUTH J.S.BRUNZELLE,G.MINASOV,L.SHUVALOVA,F.R.COLLART,
JRNL AUTH 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL 1.5A RESOLUTION CRYSTAL STRUCTURE OF A METALLO BETA
JRNL TITL 2 LACTAMASE FAMILY PROTEIN, THE ELAC HOMOLGUE OF BACILLUS
JRNL TITL 3 ANTHRACIS, A PUTATIVE RIBONUCLEASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 135032
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7103
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8778
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.1690
REMARK 3 BIN FREE R VALUE SET COUNT : 438
REMARK 3 BIN FREE R VALUE : 0.2170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7741
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 1375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : -0.49000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.125
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8280 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11336 ; 1.251 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1061 ; 6.256 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 374 ;35.739 ;24.759
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1261 ;11.820 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;21.182 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1242 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6509 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4082 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5689 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1218 ; 0.112 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 28 ; 0.058 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 93 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 72 ; 0.111 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 3 ; 0.030 ; 0.200
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): 5172 ; 1.229 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8401 ; 1.992 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3191 ; 3.089 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2935 ; 4.697 ; 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 : 1.20
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
REMARK 4
REMARK 4 1ZKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032829.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-05; 26-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 99.8; 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 32-ID; 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792; 1.0
REMARK 200 MONOCHROMATOR : DIAMOND 111; SI 111
REMARK 200 OPTICS : MIRRORS; MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM; MARMOSAIC 225 MM
REMARK 200 CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148486
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.86
REMARK 200 R MERGE FOR SHELL (I) : 0.20700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX, SHARP, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONOUM SULFATE, 0.1M SODIUM
REMARK 280 CITRATE TRIBASIC DIHYDRATE PH 5.6, 30% W/V PEG 4000 0.5M NACL,
REMARK 280 ZNCL, VAPOR DIFFUSION, TEMPERATURE 298K. 0.2M AMMONOUM SULFATE,
REMARK 280 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE PH 5.6, 30% W/V PEG
REMARK 280 40000.5M NACL, ZNCL , VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 45.59500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -189.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 3050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MSE A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 MSE B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -1
REMARK 465 MSE C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 MSE D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 GLY D -14
REMARK 465 VAL D -13
REMARK 465 ASP D -12
REMARK 465 LEU D -11
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 GLU D -8
REMARK 465 ASN D -7
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 ALA B 0 CB
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 PHE A 8 -5.89 -147.86
REMARK 500 GLU A 17 -159.14 -126.19
REMARK 500 ASP A 34 156.72 66.14
REMARK 500 CYS A 35 64.16 -152.46
REMARK 500 ALA A 154 -139.01 48.86
REMARK 500 PHE B 8 -5.09 -153.01
REMARK 500 ASP B 34 156.08 68.29
REMARK 500 ALA B 154 -137.75 48.78
REMARK 500 PHE C 8 -2.29 -150.03
REMARK 500 GLU C 17 -158.47 -124.76
REMARK 500 ASP C 34 157.96 68.95
REMARK 500 CYS C 35 61.54 -152.95
REMARK 500 ALA C 154 -140.83 51.80
REMARK 500 PHE D 8 -3.35 -145.91
REMARK 500 GLU D 17 -159.70 -124.82
REMARK 500 ASP D 34 157.40 65.34
REMARK 500 CYS D 35 61.90 -152.09
REMARK 500 ALA D 154 -140.46 50.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 245 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 59 NE2
REMARK 620 2 ASP A 155 OD2 88.7
REMARK 620 3 HIS A 61 ND1 99.9 169.2
REMARK 620 4 HIS A 134 NE2 107.3 88.4 95.2
REMARK 620 5 HOH A 260 O 114.4 67.7 102.5 130.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 246 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 64 NE2
REMARK 620 2 ASP A 155 OD2 96.6
REMARK 620 3 HOH A 260 O 110.1 79.3
REMARK 620 4 ASP A 63 OD2 89.6 167.0 87.8
REMARK 620 5 HIS A 211 NE2 116.3 99.0 133.4 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 247 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 358 O
REMARK 620 2 HOH A 274 O 83.2
REMARK 620 3 HOH A 295 O 90.6 86.1
REMARK 620 4 HOH A 414 O 86.9 97.8 175.0
REMARK 620 5 HOH A 415 O 95.7 173.3 87.3 88.7
REMARK 620 6 HOH A 319 O 175.3 92.4 90.7 92.2 88.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 245 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 155 OD2
REMARK 620 2 HOH B 275 O 69.5
REMARK 620 3 HIS B 134 NE2 86.8 132.3
REMARK 620 4 HIS B 59 NE2 87.9 114.3 105.2
REMARK 620 5 HIS B 61 ND1 171.6 103.2 95.6 99.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 246 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 211 NE2
REMARK 620 2 ASP B 155 OD2 102.5
REMARK 620 3 HOH B 275 O 134.6 78.1
REMARK 620 4 ASP B 63 OD2 85.6 166.3 88.3
REMARK 620 5 HIS B 64 NE2 115.5 97.0 109.4 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 248 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 346 O
REMARK 620 2 HOH B 274 O 85.0
REMARK 620 3 HOH B 466 O 143.0 99.8
REMARK 620 4 HOH B 469 O 76.5 101.2 136.7
REMARK 620 5 HOH B 314 O 78.6 93.9 64.6 149.5
REMARK 620 6 HOH B 437 O 136.6 78.8 79.8 67.8 141.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 249 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 265 O
REMARK 620 2 HOH B 346 O 84.7
REMARK 620 3 HOH B 469 O 86.7 78.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 245 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 155 OD2
REMARK 620 2 HOH C 254 O 69.3
REMARK 620 3 HIS C 134 NE2 86.0 130.7
REMARK 620 4 HIS C 61 ND1 170.1 102.5 95.9
REMARK 620 5 HIS C 59 NE2 87.8 114.2 106.3 100.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 246 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 211 NE2
REMARK 620 2 ASP C 63 OD2 87.4
REMARK 620 3 HIS C 64 NE2 116.7 89.2
REMARK 620 4 HOH C 254 O 133.6 87.2 109.3
REMARK 620 5 ASP C 155 OD2 100.4 166.0 97.4 79.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 247 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 265 O
REMARK 620 2 HOH C 270 O 81.7
REMARK 620 3 HOH C 439 O 168.7 93.8
REMARK 620 4 HOH C 388 O 95.7 91.5 94.8
REMARK 620 5 HOH C 327 O 96.4 176.9 87.6 91.1
REMARK 620 6 HOH C 315 O 85.0 98.4 85.3 170.0 78.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 245 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 258 O
REMARK 620 2 HIS D 134 NE2 130.9
REMARK 620 3 HIS D 61 ND1 102.7 95.7
REMARK 620 4 HIS D 59 NE2 115.2 104.9 101.1
REMARK 620 5 ASP D 155 OD2 67.4 87.5 168.7 88.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 246 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 258 O
REMARK 620 2 ASP D 63 OD2 88.1
REMARK 620 3 HIS D 211 NE2 133.6 87.1
REMARK 620 4 ASP D 155 OD2 78.8 166.6 100.1
REMARK 620 5 HIS D 64 NE2 109.4 88.7 116.6 97.9
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 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 247
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC28677 RELATED DB: TARGETDB
DBREF 1ZKP A 1 244 UNP Q81U06 Q81U06_BACAN 1 244
DBREF 1ZKP B 1 244 UNP Q81U06 Q81U06_BACAN 1 244
DBREF 1ZKP C 1 244 UNP Q81U06 Q81U06_BACAN 1 244
DBREF 1ZKP D 1 244 UNP Q81U06 Q81U06_BACAN 1 244
SEQADV 1ZKP MSE A -23 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP HIS A -22 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS A -21 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS A -20 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS A -19 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS A -18 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS A -17 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP SER A -16 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER A -15 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY A -14 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP VAL A -13 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASP A -12 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU A -11 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY A -10 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP THR A -9 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLU A -8 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN A -7 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU A -6 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP TYR A -5 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP PHE A -4 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLN A -3 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER A -2 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN A -1 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ALA A 0 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP MSE A 1 UNP Q81U06 MET 1 MODIFIED RESIDUE
SEQADV 1ZKP MSE A 3 UNP Q81U06 MET 3 MODIFIED RESIDUE
SEQADV 1ZKP MSE A 141 UNP Q81U06 MET 141 MODIFIED RESIDUE
SEQADV 1ZKP MSE A 178 UNP Q81U06 MET 178 MODIFIED RESIDUE
SEQADV 1ZKP MSE A 190 UNP Q81U06 MET 190 MODIFIED RESIDUE
SEQADV 1ZKP MSE B -23 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP HIS B -22 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS B -21 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS B -20 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS B -19 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS B -18 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS B -17 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP SER B -16 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER B -15 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY B -14 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP VAL B -13 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASP B -12 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU B -11 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY B -10 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP THR B -9 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLU B -8 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN B -7 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU B -6 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP TYR B -5 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP PHE B -4 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLN B -3 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER B -2 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN B -1 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ALA B 0 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP MSE B 1 UNP Q81U06 MET 1 MODIFIED RESIDUE
SEQADV 1ZKP MSE B 3 UNP Q81U06 MET 3 MODIFIED RESIDUE
SEQADV 1ZKP MSE B 141 UNP Q81U06 MET 141 MODIFIED RESIDUE
SEQADV 1ZKP MSE B 178 UNP Q81U06 MET 178 MODIFIED RESIDUE
SEQADV 1ZKP MSE B 190 UNP Q81U06 MET 190 MODIFIED RESIDUE
SEQADV 1ZKP MSE C -23 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP HIS C -22 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS C -21 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS C -20 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS C -19 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS C -18 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS C -17 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP SER C -16 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER C -15 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY C -14 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP VAL C -13 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASP C -12 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU C -11 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY C -10 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP THR C -9 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLU C -8 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN C -7 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU C -6 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP TYR C -5 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP PHE C -4 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLN C -3 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER C -2 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN C -1 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ALA C 0 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP MSE C 1 UNP Q81U06 MET 1 MODIFIED RESIDUE
SEQADV 1ZKP MSE C 3 UNP Q81U06 MET 3 MODIFIED RESIDUE
SEQADV 1ZKP MSE C 141 UNP Q81U06 MET 141 MODIFIED RESIDUE
SEQADV 1ZKP MSE C 178 UNP Q81U06 MET 178 MODIFIED RESIDUE
SEQADV 1ZKP MSE C 190 UNP Q81U06 MET 190 MODIFIED RESIDUE
SEQADV 1ZKP MSE D -23 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP HIS D -22 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS D -21 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS D -20 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS D -19 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS D -18 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP HIS D -17 UNP Q81U06 EXPRESSION TAG
SEQADV 1ZKP SER D -16 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER D -15 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY D -14 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP VAL D -13 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASP D -12 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU D -11 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLY D -10 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP THR D -9 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLU D -8 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN D -7 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP LEU D -6 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP TYR D -5 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP PHE D -4 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP GLN D -3 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP SER D -2 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ASN D -1 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP ALA D 0 UNP Q81U06 CLONING ARTIFACT
SEQADV 1ZKP MSE D 1 UNP Q81U06 MET 1 MODIFIED RESIDUE
SEQADV 1ZKP MSE D 3 UNP Q81U06 MET 3 MODIFIED RESIDUE
SEQADV 1ZKP MSE D 141 UNP Q81U06 MET 141 MODIFIED RESIDUE
SEQADV 1ZKP MSE D 178 UNP Q81U06 MET 178 MODIFIED RESIDUE
SEQADV 1ZKP MSE D 190 UNP Q81U06 MET 190 MODIFIED RESIDUE
SEQRES 1 A 268 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 268 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE LYS
SEQRES 3 A 268 MSE THR VAL VAL GLY PHE TRP GLY GLY PHE PRO GLU ALA
SEQRES 4 A 268 GLY GLU ALA THR SER GLY TYR LEU PHE GLU HIS ASP GLY
SEQRES 5 A 268 PHE ARG LEU LEU VAL ASP CYS GLY SER GLY VAL LEU ALA
SEQRES 6 A 268 GLN LEU GLN LYS TYR ILE THR PRO SER ASP ILE ASP ALA
SEQRES 7 A 268 VAL VAL LEU SER HIS TYR HIS HIS ASP HIS VAL ALA ASP
SEQRES 8 A 268 ILE GLY VAL LEU GLN TYR ALA ARG LEU ILE THR SER ALA
SEQRES 9 A 268 THR LYS GLY GLN LEU PRO GLU LEU PRO ILE TYR GLY HIS
SEQRES 10 A 268 THR PHE ASP GLU ASN GLY PHE HIS SER LEU THR HIS GLU
SEQRES 11 A 268 PRO HIS THR LYS GLY ILE PRO TYR ASN PRO GLU GLU THR
SEQRES 12 A 268 LEU GLN ILE GLY PRO PHE SER ILE SER PHE LEU LYS THR
SEQRES 13 A 268 VAL HIS PRO VAL THR CYS PHE ALA MSE ARG ILE THR ALA
SEQRES 14 A 268 GLY ASN ASP ILE VAL VAL TYR SER ALA ASP SER SER TYR
SEQRES 15 A 268 ILE PRO GLU PHE ILE PRO PHE THR LYS ASP ALA ASP LEU
SEQRES 16 A 268 PHE ILE CYS GLU CYS ASN MSE TYR ALA HIS GLN GLU ALA
SEQRES 17 A 268 ALA LYS ALA GLY HIS MSE ASN SER THR GLU VAL ALA SER
SEQRES 18 A 268 ILE ALA LYS ASP ALA ASN VAL LYS GLU LEU LEU LEU THR
SEQRES 19 A 268 HIS LEU PRO HIS THR GLY ASN PRO ALA ASP LEU VAL THR
SEQRES 20 A 268 GLU ALA LYS GLN ILE PHE SER GLY HIS ILE THR LEU ALA
SEQRES 21 A 268 HIS SER GLY TYR VAL TRP ASN SER
SEQRES 1 B 268 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 268 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE LYS
SEQRES 3 B 268 MSE THR VAL VAL GLY PHE TRP GLY GLY PHE PRO GLU ALA
SEQRES 4 B 268 GLY GLU ALA THR SER GLY TYR LEU PHE GLU HIS ASP GLY
SEQRES 5 B 268 PHE ARG LEU LEU VAL ASP CYS GLY SER GLY VAL LEU ALA
SEQRES 6 B 268 GLN LEU GLN LYS TYR ILE THR PRO SER ASP ILE ASP ALA
SEQRES 7 B 268 VAL VAL LEU SER HIS TYR HIS HIS ASP HIS VAL ALA ASP
SEQRES 8 B 268 ILE GLY VAL LEU GLN TYR ALA ARG LEU ILE THR SER ALA
SEQRES 9 B 268 THR LYS GLY GLN LEU PRO GLU LEU PRO ILE TYR GLY HIS
SEQRES 10 B 268 THR PHE ASP GLU ASN GLY PHE HIS SER LEU THR HIS GLU
SEQRES 11 B 268 PRO HIS THR LYS GLY ILE PRO TYR ASN PRO GLU GLU THR
SEQRES 12 B 268 LEU GLN ILE GLY PRO PHE SER ILE SER PHE LEU LYS THR
SEQRES 13 B 268 VAL HIS PRO VAL THR CYS PHE ALA MSE ARG ILE THR ALA
SEQRES 14 B 268 GLY ASN ASP ILE VAL VAL TYR SER ALA ASP SER SER TYR
SEQRES 15 B 268 ILE PRO GLU PHE ILE PRO PHE THR LYS ASP ALA ASP LEU
SEQRES 16 B 268 PHE ILE CYS GLU CYS ASN MSE TYR ALA HIS GLN GLU ALA
SEQRES 17 B 268 ALA LYS ALA GLY HIS MSE ASN SER THR GLU VAL ALA SER
SEQRES 18 B 268 ILE ALA LYS ASP ALA ASN VAL LYS GLU LEU LEU LEU THR
SEQRES 19 B 268 HIS LEU PRO HIS THR GLY ASN PRO ALA ASP LEU VAL THR
SEQRES 20 B 268 GLU ALA LYS GLN ILE PHE SER GLY HIS ILE THR LEU ALA
SEQRES 21 B 268 HIS SER GLY TYR VAL TRP ASN SER
SEQRES 1 C 268 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 268 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE LYS
SEQRES 3 C 268 MSE THR VAL VAL GLY PHE TRP GLY GLY PHE PRO GLU ALA
SEQRES 4 C 268 GLY GLU ALA THR SER GLY TYR LEU PHE GLU HIS ASP GLY
SEQRES 5 C 268 PHE ARG LEU LEU VAL ASP CYS GLY SER GLY VAL LEU ALA
SEQRES 6 C 268 GLN LEU GLN LYS TYR ILE THR PRO SER ASP ILE ASP ALA
SEQRES 7 C 268 VAL VAL LEU SER HIS TYR HIS HIS ASP HIS VAL ALA ASP
SEQRES 8 C 268 ILE GLY VAL LEU GLN TYR ALA ARG LEU ILE THR SER ALA
SEQRES 9 C 268 THR LYS GLY GLN LEU PRO GLU LEU PRO ILE TYR GLY HIS
SEQRES 10 C 268 THR PHE ASP GLU ASN GLY PHE HIS SER LEU THR HIS GLU
SEQRES 11 C 268 PRO HIS THR LYS GLY ILE PRO TYR ASN PRO GLU GLU THR
SEQRES 12 C 268 LEU GLN ILE GLY PRO PHE SER ILE SER PHE LEU LYS THR
SEQRES 13 C 268 VAL HIS PRO VAL THR CYS PHE ALA MSE ARG ILE THR ALA
SEQRES 14 C 268 GLY ASN ASP ILE VAL VAL TYR SER ALA ASP SER SER TYR
SEQRES 15 C 268 ILE PRO GLU PHE ILE PRO PHE THR LYS ASP ALA ASP LEU
SEQRES 16 C 268 PHE ILE CYS GLU CYS ASN MSE TYR ALA HIS GLN GLU ALA
SEQRES 17 C 268 ALA LYS ALA GLY HIS MSE ASN SER THR GLU VAL ALA SER
SEQRES 18 C 268 ILE ALA LYS ASP ALA ASN VAL LYS GLU LEU LEU LEU THR
SEQRES 19 C 268 HIS LEU PRO HIS THR GLY ASN PRO ALA ASP LEU VAL THR
SEQRES 20 C 268 GLU ALA LYS GLN ILE PHE SER GLY HIS ILE THR LEU ALA
SEQRES 21 C 268 HIS SER GLY TYR VAL TRP ASN SER
SEQRES 1 D 268 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 268 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE LYS
SEQRES 3 D 268 MSE THR VAL VAL GLY PHE TRP GLY GLY PHE PRO GLU ALA
SEQRES 4 D 268 GLY GLU ALA THR SER GLY TYR LEU PHE GLU HIS ASP GLY
SEQRES 5 D 268 PHE ARG LEU LEU VAL ASP CYS GLY SER GLY VAL LEU ALA
SEQRES 6 D 268 GLN LEU GLN LYS TYR ILE THR PRO SER ASP ILE ASP ALA
SEQRES 7 D 268 VAL VAL LEU SER HIS TYR HIS HIS ASP HIS VAL ALA ASP
SEQRES 8 D 268 ILE GLY VAL LEU GLN TYR ALA ARG LEU ILE THR SER ALA
SEQRES 9 D 268 THR LYS GLY GLN LEU PRO GLU LEU PRO ILE TYR GLY HIS
SEQRES 10 D 268 THR PHE ASP GLU ASN GLY PHE HIS SER LEU THR HIS GLU
SEQRES 11 D 268 PRO HIS THR LYS GLY ILE PRO TYR ASN PRO GLU GLU THR
SEQRES 12 D 268 LEU GLN ILE GLY PRO PHE SER ILE SER PHE LEU LYS THR
SEQRES 13 D 268 VAL HIS PRO VAL THR CYS PHE ALA MSE ARG ILE THR ALA
SEQRES 14 D 268 GLY ASN ASP ILE VAL VAL TYR SER ALA ASP SER SER TYR
SEQRES 15 D 268 ILE PRO GLU PHE ILE PRO PHE THR LYS ASP ALA ASP LEU
SEQRES 16 D 268 PHE ILE CYS GLU CYS ASN MSE TYR ALA HIS GLN GLU ALA
SEQRES 17 D 268 ALA LYS ALA GLY HIS MSE ASN SER THR GLU VAL ALA SER
SEQRES 18 D 268 ILE ALA LYS ASP ALA ASN VAL LYS GLU LEU LEU LEU THR
SEQRES 19 D 268 HIS LEU PRO HIS THR GLY ASN PRO ALA ASP LEU VAL THR
SEQRES 20 D 268 GLU ALA LYS GLN ILE PHE SER GLY HIS ILE THR LEU ALA
SEQRES 21 D 268 HIS SER GLY TYR VAL TRP ASN SER
MODRES 1ZKP MSE A 1 MET SELENOMETHIONINE
MODRES 1ZKP MSE A 3 MET SELENOMETHIONINE
MODRES 1ZKP MSE A 141 MET SELENOMETHIONINE
MODRES 1ZKP MSE A 178 MET SELENOMETHIONINE
MODRES 1ZKP MSE A 190 MET SELENOMETHIONINE
MODRES 1ZKP MSE B 1 MET SELENOMETHIONINE
MODRES 1ZKP MSE B 3 MET SELENOMETHIONINE
MODRES 1ZKP MSE B 141 MET SELENOMETHIONINE
MODRES 1ZKP MSE B 178 MET SELENOMETHIONINE
MODRES 1ZKP MSE B 190 MET SELENOMETHIONINE
MODRES 1ZKP MSE C 1 MET SELENOMETHIONINE
MODRES 1ZKP MSE C 3 MET SELENOMETHIONINE
MODRES 1ZKP MSE C 141 MET SELENOMETHIONINE
MODRES 1ZKP MSE C 178 MET SELENOMETHIONINE
MODRES 1ZKP MSE C 190 MET SELENOMETHIONINE
MODRES 1ZKP MSE D 1 MET SELENOMETHIONINE
MODRES 1ZKP MSE D 3 MET SELENOMETHIONINE
MODRES 1ZKP MSE D 141 MET SELENOMETHIONINE
MODRES 1ZKP MSE D 178 MET SELENOMETHIONINE
MODRES 1ZKP MSE D 190 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 3 8
HET MSE A 141 8
HET MSE A 178 8
HET MSE A 190 8
HET MSE B 1 8
HET MSE B 3 8
HET MSE B 141 8
HET MSE B 178 8
HET MSE B 190 8
HET MSE C 1 8
HET MSE C 3 8
HET MSE C 141 8
HET MSE C 178 8
HET MSE C 190 8
HET MSE D 1 8
HET MSE D 3 8
HET MSE D 141 8
HET MSE D 178 8
HET MSE D 190 8
HET ZN A 245 1
HET ZN A 246 1
HET NA A 247 1
HET ZN B 245 1
HET ZN B 246 1
HET CL B 247 1
HET NA B 248 1
HET NA B 249 1
HET ZN C 245 1
HET ZN C 246 1
HET NA C 247 1
HET ZN D 245 1
HET ZN D 246 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 NA 4(NA 1+)
FORMUL 10 CL CL 1-
FORMUL 18 HOH *1375(H2 O)
HELIX 1 1 GLY A 38 GLN A 44 1 7
HELIX 2 2 THR A 48 ILE A 52 5 5
HELIX 3 3 HIS A 61 ALA A 66 1 6
HELIX 4 4 ASP A 67 GLY A 83 1 17
HELIX 5 5 ASP A 96 SER A 102 1 7
HELIX 6 6 GLU A 161 LYS A 167 1 7
HELIX 7 7 ALA A 184 GLY A 188 5 5
HELIX 8 8 ASN A 191 ALA A 202 1 12
HELIX 9 9 PRO A 218 GLN A 227 1 10
HELIX 10 10 GLY B 38 GLN B 44 1 7
HELIX 11 11 THR B 48 ILE B 52 5 5
HELIX 12 12 HIS B 61 ALA B 66 1 6
HELIX 13 13 ASP B 67 LYS B 82 1 16
HELIX 14 14 ASP B 96 LEU B 103 1 8
HELIX 15 15 GLU B 161 LYS B 167 1 7
HELIX 16 16 ALA B 184 GLY B 188 5 5
HELIX 17 17 ASN B 191 ASN B 203 1 13
HELIX 18 18 ALA B 219 GLN B 227 1 9
HELIX 19 19 GLY C 38 GLN C 44 1 7
HELIX 20 20 THR C 48 ILE C 52 5 5
HELIX 21 21 HIS C 61 ALA C 66 1 6
HELIX 22 22 ASP C 67 GLY C 83 1 17
HELIX 23 23 ASP C 96 LEU C 103 1 8
HELIX 24 24 GLU C 161 LYS C 167 1 7
HELIX 25 25 ALA C 184 GLY C 188 5 5
HELIX 26 26 ASN C 191 ALA C 202 1 12
HELIX 27 27 PRO C 218 GLN C 227 1 10
HELIX 28 28 GLY D 38 GLN D 44 1 7
HELIX 29 29 THR D 48 ILE D 52 5 5
HELIX 30 30 HIS D 61 ALA D 66 1 6
HELIX 31 31 ASP D 67 LYS D 82 1 16
HELIX 32 32 ASP D 96 SER D 102 1 7
HELIX 33 33 GLU D 161 LYS D 167 1 7
HELIX 34 34 ALA D 184 GLY D 188 5 5
HELIX 35 35 ASN D 191 ALA D 202 1 12
HELIX 36 36 PRO D 218 GLN D 227 1 10
SHEET 1 A 7 THR A 109 PRO A 113 0
SHEET 2 A 7 LEU A 88 GLY A 92 1 N ILE A 90 O LYS A 110
SHEET 3 A 7 ALA A 54 VAL A 56 1 N VAL A 55 O TYR A 91
SHEET 4 A 7 PHE A 29 VAL A 33 1 N LEU A 32 O ALA A 54
SHEET 5 A 7 GLY A 21 HIS A 26 -1 N PHE A 24 O LEU A 31
SHEET 6 A 7 MSE A 1 GLY A 7 -1 N THR A 4 O LEU A 23
SHEET 7 A 7 VAL A 241 ASN A 243 -1 O TRP A 242 N MSE A 3
SHEET 1 B 7 LEU A 120 ILE A 122 0
SHEET 2 B 7 PHE A 125 LYS A 131 -1 O ILE A 127 N LEU A 120
SHEET 3 B 7 PHE A 139 ALA A 145 -1 O ALA A 140 N LEU A 130
SHEET 4 B 7 ASP A 148 TYR A 152 -1 O VAL A 150 N ILE A 143
SHEET 5 B 7 LEU A 171 GLU A 175 1 O ILE A 173 N VAL A 151
SHEET 6 B 7 GLU A 206 THR A 210 1 O LEU A 208 N PHE A 172
SHEET 7 B 7 HIS A 232 LEU A 235 1 O HIS A 232 N LEU A 207
SHEET 1 C 7 THR B 109 PRO B 113 0
SHEET 2 C 7 LEU B 88 GLY B 92 1 N ILE B 90 O LYS B 110
SHEET 3 C 7 ALA B 54 VAL B 56 1 N VAL B 55 O TYR B 91
SHEET 4 C 7 PHE B 29 VAL B 33 1 N LEU B 32 O VAL B 56
SHEET 5 C 7 GLY B 21 HIS B 26 -1 N PHE B 24 O LEU B 31
SHEET 6 C 7 LYS B 2 GLY B 7 -1 N THR B 4 O LEU B 23
SHEET 7 C 7 VAL B 241 ASN B 243 -1 O TRP B 242 N MSE B 3
SHEET 1 D 7 LEU B 120 ILE B 122 0
SHEET 2 D 7 PHE B 125 LYS B 131 -1 O ILE B 127 N LEU B 120
SHEET 3 D 7 PHE B 139 ALA B 145 -1 O ALA B 140 N LEU B 130
SHEET 4 D 7 ASP B 148 TYR B 152 -1 O VAL B 150 N ILE B 143
SHEET 5 D 7 LEU B 171 GLU B 175 1 O ILE B 173 N VAL B 151
SHEET 6 D 7 GLU B 206 THR B 210 1 O LEU B 208 N PHE B 172
SHEET 7 D 7 HIS B 232 LEU B 235 1 O THR B 234 N LEU B 209
SHEET 1 E 7 THR C 109 PRO C 113 0
SHEET 2 E 7 LEU C 88 GLY C 92 1 N ILE C 90 O LYS C 110
SHEET 3 E 7 ALA C 54 VAL C 56 1 N VAL C 55 O TYR C 91
SHEET 4 E 7 PHE C 29 VAL C 33 1 N LEU C 32 O ALA C 54
SHEET 5 E 7 GLY C 21 HIS C 26 -1 N PHE C 24 O LEU C 31
SHEET 6 E 7 LYS C 2 GLY C 7 -1 N THR C 4 O LEU C 23
SHEET 7 E 7 VAL C 241 ASN C 243 -1 O TRP C 242 N MSE C 3
SHEET 1 F 7 LEU C 120 ILE C 122 0
SHEET 2 F 7 PHE C 125 LYS C 131 -1 O ILE C 127 N LEU C 120
SHEET 3 F 7 PHE C 139 ALA C 145 -1 O ARG C 142 N SER C 128
SHEET 4 F 7 ASP C 148 TYR C 152 -1 O VAL C 150 N ILE C 143
SHEET 5 F 7 LEU C 171 GLU C 175 1 O ILE C 173 N VAL C 151
SHEET 6 F 7 GLU C 206 THR C 210 1 O LEU C 208 N PHE C 172
SHEET 7 F 7 HIS C 232 LEU C 235 1 O THR C 234 N LEU C 209
SHEET 1 G 7 THR D 109 PRO D 113 0
SHEET 2 G 7 LEU D 88 GLY D 92 1 N ILE D 90 O LYS D 110
SHEET 3 G 7 ALA D 54 VAL D 56 1 N VAL D 55 O TYR D 91
SHEET 4 G 7 PHE D 29 VAL D 33 1 N LEU D 32 O ALA D 54
SHEET 5 G 7 GLY D 21 HIS D 26 -1 N PHE D 24 O LEU D 31
SHEET 6 G 7 LYS D 2 GLY D 7 -1 N THR D 4 O LEU D 23
SHEET 7 G 7 VAL D 241 ASN D 243 -1 O TRP D 242 N MSE D 3
SHEET 1 H 7 LEU D 120 ILE D 122 0
SHEET 2 H 7 PHE D 125 LYS D 131 -1 O ILE D 127 N LEU D 120
SHEET 3 H 7 PHE D 139 ALA D 145 -1 O ALA D 140 N LEU D 130
SHEET 4 H 7 ASP D 148 TYR D 152 -1 O VAL D 150 N ILE D 143
SHEET 5 H 7 LEU D 171 GLU D 175 1 O ILE D 173 N VAL D 151
SHEET 6 H 7 GLU D 206 THR D 210 1 O LEU D 208 N PHE D 172
SHEET 7 H 7 HIS D 232 LEU D 235 1 O HIS D 232 N LEU D 207
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C LYS A 2 N MSE A 3 1555 1555 1.32
LINK C MSE A 3 N THR A 4 1555 1555 1.34
LINK C ALA A 140 N MSE A 141 1555 1555 1.33
LINK C MSE A 141 N ARG A 142 1555 1555 1.33
LINK C ASN A 177 N MSE A 178 1555 1555 1.33
LINK C MSE A 178 N TYR A 179 1555 1555 1.33
LINK C HIS A 189 N MSE A 190 1555 1555 1.33
LINK C MSE A 190 N ASN A 191 1555 1555 1.33
LINK ZN ZN A 245 NE2 HIS A 59 1555 1555 2.15
LINK ZN ZN A 245 OD2 ASP A 155 1555 1555 2.54
LINK ZN ZN A 245 ND1 HIS A 61 1555 1555 2.09
LINK ZN ZN A 245 NE2 HIS A 134 1555 1555 2.12
LINK ZN ZN A 245 O HOH A 260 1555 1555 1.98
LINK ZN ZN A 246 NE2 HIS A 64 1555 1555 2.05
LINK ZN ZN A 246 OD2 ASP A 155 1555 1555 2.08
LINK ZN ZN A 246 O HOH A 260 1555 1555 1.94
LINK ZN ZN A 246 OD2 ASP A 63 1555 1555 2.40
LINK ZN ZN A 246 NE2 HIS A 211 1555 1555 2.03
LINK NA NA A 247 O HOH A 358 1555 1555 2.41
LINK NA NA A 247 O HOH A 274 1555 1555 2.39
LINK NA NA A 247 O HOH A 295 1555 1555 2.52
LINK NA NA A 247 O HOH A 414 1555 1555 2.30
LINK NA NA A 247 O HOH A 415 1555 1555 2.32
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C LYS B 2 N MSE B 3 1555 1555 1.33
LINK C MSE B 3 N THR B 4 1555 1555 1.33
LINK C ALA B 140 N MSE B 141 1555 1555 1.34
LINK C MSE B 141 N ARG B 142 1555 1555 1.33
LINK C ASN B 177 N MSE B 178 1555 1555 1.33
LINK C MSE B 178 N TYR B 179 1555 1555 1.33
LINK C HIS B 189 N MSE B 190 1555 1555 1.33
LINK C MSE B 190 N ASN B 191 1555 1555 1.33
LINK ZN ZN B 245 OD2 ASP B 155 1555 1555 2.48
LINK ZN ZN B 245 O HOH B 275 1555 1555 1.97
LINK ZN ZN B 245 NE2 HIS B 134 1555 1555 2.14
LINK ZN ZN B 245 NE2 HIS B 59 1555 1555 2.13
LINK ZN ZN B 245 ND1 HIS B 61 1555 1555 2.08
LINK ZN ZN B 246 NE2 HIS B 211 1555 1555 2.02
LINK ZN ZN B 246 OD2 ASP B 155 1555 1555 2.13
LINK ZN ZN B 246 O HOH B 275 1555 1555 1.95
LINK ZN ZN B 246 OD2 ASP B 63 1555 1555 2.39
LINK ZN ZN B 246 NE2 HIS B 64 1555 1555 2.07
LINK NA NA B 248 O HOH B 346 1555 1555 2.45
LINK NA NA B 248 O HOH B 274 1555 1555 2.25
LINK NA NA B 248 O HOH B 466 1555 1555 2.38
LINK NA NA B 248 O HOH B 469 1555 1555 2.40
LINK NA NA B 249 O HOH B 265 1555 1555 2.40
LINK NA NA B 249 O HOH B 346 1555 1555 2.41
LINK NA NA B 249 O HOH B 469 1555 1555 2.34
LINK C ALA C 0 N MSE C 1 1555 1555 1.33
LINK C MSE C 1 N LYS C 2 1555 1555 1.34
LINK C LYS C 2 N MSE C 3 1555 1555 1.33
LINK C MSE C 3 N THR C 4 1555 1555 1.34
LINK C ALA C 140 N MSE C 141 1555 1555 1.33
LINK C MSE C 141 N ARG C 142 1555 1555 1.33
LINK C ASN C 177 N MSE C 178 1555 1555 1.33
LINK C MSE C 178 N TYR C 179 1555 1555 1.33
LINK C HIS C 189 N MSE C 190 1555 1555 1.33
LINK C MSE C 190 N ASN C 191 1555 1555 1.34
LINK ZN ZN C 245 OD2 ASP C 155 1555 1555 2.51
LINK ZN ZN C 245 O HOH C 254 1555 1555 1.99
LINK ZN ZN C 245 NE2 HIS C 134 1555 1555 2.11
LINK ZN ZN C 245 ND1 HIS C 61 1555 1555 2.11
LINK ZN ZN C 245 NE2 HIS C 59 1555 1555 2.13
LINK ZN ZN C 246 NE2 HIS C 211 1555 1555 2.03
LINK ZN ZN C 246 OD2 ASP C 63 1555 1555 2.36
LINK ZN ZN C 246 NE2 HIS C 64 1555 1555 2.05
LINK ZN ZN C 246 O HOH C 254 1555 1555 1.94
LINK ZN ZN C 246 OD2 ASP C 155 1555 1555 2.13
LINK NA NA C 247 O HOH C 265 1555 1555 2.41
LINK NA NA C 247 O HOH C 270 1555 1555 2.45
LINK NA NA C 247 O HOH C 439 1555 1555 2.39
LINK NA NA C 247 O HOH C 388 1555 1555 2.36
LINK NA NA C 247 O HOH C 327 1555 1555 2.43
LINK NA NA C 247 O HOH C 315 1555 1555 2.41
LINK C ALA D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N LYS D 2 1555 1555 1.33
LINK C LYS D 2 N MSE D 3 1555 1555 1.33
LINK C MSE D 3 N THR D 4 1555 1555 1.34
LINK C ALA D 140 N MSE D 141 1555 1555 1.33
LINK C MSE D 141 N ARG D 142 1555 1555 1.33
LINK C ASN D 177 N MSE D 178 1555 1555 1.34
LINK C MSE D 178 N TYR D 179 1555 1555 1.33
LINK C HIS D 189 N MSE D 190 1555 1555 1.33
LINK C MSE D 190 N ASN D 191 1555 1555 1.34
LINK ZN ZN D 245 O HOH D 258 1555 1555 1.98
LINK ZN ZN D 245 NE2 HIS D 134 1555 1555 2.10
LINK ZN ZN D 245 ND1 HIS D 61 1555 1555 2.11
LINK ZN ZN D 245 NE2 HIS D 59 1555 1555 2.17
LINK ZN ZN D 245 OD2 ASP D 155 1555 1555 2.56
LINK ZN ZN D 246 O HOH D 258 1555 1555 1.92
LINK ZN ZN D 246 OD2 ASP D 63 1555 1555 2.41
LINK ZN ZN D 246 NE2 HIS D 211 1555 1555 2.05
LINK ZN ZN D 246 OD2 ASP D 155 1555 1555 2.11
LINK ZN ZN D 246 NE2 HIS D 64 1555 1555 2.04
LINK NA NA B 248 O HOH B 314 1555 1555 2.93
LINK NA NA B 248 O HOH B 437 1555 1555 2.87
LINK NA NA A 247 O HOH A 319 1555 1555 2.62
CISPEP 1 GLU A 106 PRO A 107 0 -0.43
CISPEP 2 GLU B 106 PRO B 107 0 -3.28
CISPEP 3 GLU C 106 PRO C 107 0 -5.95
CISPEP 4 GLU D 106 PRO D 107 0 -3.57
CISPEP 5 GLU D 106 PRO D 107 0 -8.02
SITE 1 AC1 6 HIS A 59 HIS A 61 HIS A 134 ASP A 155
SITE 2 AC1 6 ZN A 246 HOH A 260
SITE 1 AC2 6 ASP A 63 HIS A 64 ASP A 155 HIS A 211
SITE 2 AC2 6 ZN A 245 HOH A 260
SITE 1 AC3 6 HIS B 59 HIS B 61 HIS B 134 ASP B 155
SITE 2 AC3 6 ZN B 246 HOH B 275
SITE 1 AC4 6 ASP B 63 HIS B 64 ASP B 155 HIS B 211
SITE 2 AC4 6 ZN B 245 HOH B 275
SITE 1 AC5 6 HIS C 59 HIS C 61 HIS C 134 ASP C 155
SITE 2 AC5 6 ZN C 246 HOH C 254
SITE 1 AC6 6 ASP C 63 HIS C 64 ASP C 155 HIS C 211
SITE 2 AC6 6 ZN C 245 HOH C 254
SITE 1 AC7 6 HIS D 59 HIS D 61 HIS D 134 ASP D 155
SITE 2 AC7 6 ZN D 246 HOH D 258
SITE 1 AC8 6 ASP D 63 HIS D 64 ASP D 155 HIS D 211
SITE 2 AC8 6 ZN D 245 HOH D 258
SITE 1 AC9 4 ASN B 217 PRO B 218 ALA B 219 HOH B 357
SITE 1 BC1 6 HOH C 265 HOH C 270 HOH C 315 HOH C 327
SITE 2 BC1 6 HOH C 388 HOH C 439
SITE 1 BC2 7 NA B 249 HOH B 274 HOH B 314 HOH B 346
SITE 2 BC2 7 HOH B 437 HOH B 466 HOH B 469
SITE 1 BC3 4 NA B 248 HOH B 265 HOH B 346 HOH B 469
SITE 1 BC4 6 HOH A 274 HOH A 295 HOH A 319 HOH A 358
SITE 2 BC4 6 HOH A 414 HOH A 415
CRYST1 73.375 91.190 78.466 90.00 115.31 90.00 P 1 21 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 0.013629 0.000000 0.006444 0.00000
SCALE2 0.000000 0.010966 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014097 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
