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HEADER HYDROLASE 16-MAY-06 2H1I
TITLE CRYSTAL STRUCTURE OF THE BACILLUS CEREUS CARBOXYLESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS ATCC 14579;
SOURCE 3 ORGANISM_TAXID: 226900;
SOURCE 4 STRAIN: ATCC 14579;
SOURCE 5 GENE: AAP10572;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS CRYSTAL STRUCTURE, STRUCTURAL GENOMICS, CARBOXYLESTERASE, ,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,L.SHUVALOVA,F.R.COLLART,W.F.ANDERSON,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 2 24-FEB-09 2H1I 1 VERSN
REVDAT 1 30-MAY-06 2H1I 0
JRNL AUTH G.MINASOV,L.SHUVALOVA,F.R.COLLART,W.F.ANDERSON
JRNL TITL CRYSTAL STRUCTURE OF THE BACILLUS CEREUS
JRNL TITL 2 CARBOXYLESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 20089
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1094
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1096
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.09000
REMARK 3 B22 (A**2) : 1.09000
REMARK 3 B33 (A**2) : -1.64000
REMARK 3 B12 (A**2) : 0.55000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.334
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.225
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.191
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4961 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6692 ; 1.196 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 618 ; 5.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;33.742 ;24.877
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 877 ;16.547 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;14.425 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 731 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3782 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2253 ; 0.236 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3346 ; 0.329 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 410 ; 0.215 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.137 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 65 ; 0.197 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.213 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 3 ; 0.211 ; 0.500
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): 3132 ; 1.116 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4902 ; 1.546 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2001 ; 2.219 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1790 ; 3.522 ; 4.500
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2H1I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037812.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97874
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21218
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 10.200
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM CHLORIDE, 0.25M SODIUM
REMARK 280 CHLORIDE,0.1M HEPES, 14% V/V PEG 400, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 53.41133
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 106.82267
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.11700
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 133.52833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.70567
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 0.500000 -0.866025 0.000000 99.60700
REMARK 350 BIOMT2 1 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 26.70567
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 99.60700
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 26.70567
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 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 -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
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 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 ASP A 38 87.72 -164.43
REMARK 500 SER A 103 -116.18 45.73
REMARK 500 GLU A 117 -54.62 -16.32
REMARK 500 ALA A 141 -80.45 -18.70
REMARK 500 ASN A 152 60.11 -109.68
REMARK 500 ASP B 38 98.19 -165.39
REMARK 500 SER B 103 -119.85 55.82
REMARK 500 ASN B 152 58.58 -112.74
REMARK 500 ASN B 172 6.46 84.78
REMARK 500 ARG B 182 47.86 -86.93
REMARK 500 PRO C 15 -177.31 -58.07
REMARK 500 ASN C 96 55.93 -143.83
REMARK 500 SER C 103 -118.40 57.71
REMARK 500 ASN C 172 9.17 96.87
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 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 153 OD2
REMARK 620 2 CYS A 156 SG 87.5
REMARK 620 3 HIS A 127 ND1 101.0 125.8
REMARK 620 4 HIS A 184 ND1 117.9 102.3 118.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 153 OD2
REMARK 620 2 HIS B 184 ND1 110.1
REMARK 620 3 HIS B 127 ND1 102.7 123.1
REMARK 620 4 CYS B 156 SG 106.4 93.9 119.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 153 OD2
REMARK 620 2 HIS C 127 ND1 99.9
REMARK 620 3 HIS C 184 ND1 111.8 117.2
REMARK 620 4 CYS C 156 SG 99.1 107.0 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 53 OD1
REMARK 620 2 ASN A 53 ND2 46.4
REMARK 620 3 GLU B 89 OE1 113.9 74.2
REMARK 620 4 GLU B 89 OE2 85.3 72.5 45.7
REMARK 620 5 HOH B 329 O 157.2 133.1 58.9 74.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 384 O
REMARK 620 2 ASP B 84 OD2 91.7
REMARK 620 3 GLU B 81 OE1 85.8 112.7
REMARK 620 4 GLU B 81 OE2 110.5 72.6 46.9
REMARK 620 5 GLU C 85 OE2 92.0 83.8 163.3 147.5
REMARK 620 6 HOH C 351 O 101.5 149.4 95.8 125.9 68.4
REMARK 620 7 GLU C 81 OE2 169.1 99.2 89.8 73.1 89.3 69.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 85 OE2
REMARK 620 2 GLU B 81 OE2 96.9
REMARK 620 3 GLU C 81 OE1 173.9 85.5
REMARK 620 4 ASP C 84 OD2 92.0 97.7 93.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 156 O
REMARK 620 2 HOH C 340 O 83.3
REMARK 620 3 ASP C 153 O 87.6 93.6
REMARK 620 N 1 2
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 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 300
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 302
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 301
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 303
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC26065 RELATED DB: TARGETDB
DBREF 2H1I A 1 202 UNP Q81AD5 Q81AD5_BACCR 1 202
DBREF 2H1I B 1 202 UNP Q81AD5 Q81AD5_BACCR 1 202
DBREF 2H1I C 1 202 UNP Q81AD5 Q81AD5_BACCR 1 202
SEQADV 2H1I MSE A -23 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I HIS A -22 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS A -21 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS A -20 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS A -19 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS A -18 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS A -17 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I SER A -16 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER A -15 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY A -14 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I VAL A -13 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASP A -12 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU A -11 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY A -10 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I THR A -9 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLU A -8 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN A -7 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU A -6 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I TYR A -5 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I PHE A -4 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLN A -3 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER A -2 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN A -1 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ALA A 0 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I MSE A 1 UNP Q81AD5 MET 1 MODIFIED RESIDUE
SEQADV 2H1I MSE A 2 UNP Q81AD5 MET 2 MODIFIED RESIDUE
SEQADV 2H1I MSE A 55 UNP Q81AD5 MET 55 MODIFIED RESIDUE
SEQADV 2H1I MSE A 129 UNP Q81AD5 MET 129 MODIFIED RESIDUE
SEQADV 2H1I MSE A 135 UNP Q81AD5 MET 135 MODIFIED RESIDUE
SEQADV 2H1I MSE A 177 UNP Q81AD5 MET 177 MODIFIED RESIDUE
SEQADV 2H1I MSE A 188 UNP Q81AD5 MET 188 MODIFIED RESIDUE
SEQADV 2H1I MSE B -23 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I HIS B -22 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS B -21 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS B -20 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS B -19 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS B -18 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS B -17 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I SER B -16 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER B -15 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY B -14 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I VAL B -13 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASP B -12 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU B -11 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY B -10 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I THR B -9 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLU B -8 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN B -7 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU B -6 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I TYR B -5 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I PHE B -4 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLN B -3 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER B -2 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN B -1 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ALA B 0 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I MSE B 1 UNP Q81AD5 MET 1 MODIFIED RESIDUE
SEQADV 2H1I MSE B 2 UNP Q81AD5 MET 2 MODIFIED RESIDUE
SEQADV 2H1I MSE B 55 UNP Q81AD5 MET 55 MODIFIED RESIDUE
SEQADV 2H1I MSE B 129 UNP Q81AD5 MET 129 MODIFIED RESIDUE
SEQADV 2H1I MSE B 135 UNP Q81AD5 MET 135 MODIFIED RESIDUE
SEQADV 2H1I MSE B 177 UNP Q81AD5 MET 177 MODIFIED RESIDUE
SEQADV 2H1I MSE B 188 UNP Q81AD5 MET 188 MODIFIED RESIDUE
SEQADV 2H1I MSE C -23 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I HIS C -22 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS C -21 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS C -20 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS C -19 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS C -18 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I HIS C -17 UNP Q81AD5 EXPRESSION TAG
SEQADV 2H1I SER C -16 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER C -15 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY C -14 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I VAL C -13 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASP C -12 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU C -11 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLY C -10 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I THR C -9 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLU C -8 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN C -7 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I LEU C -6 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I TYR C -5 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I PHE C -4 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I GLN C -3 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I SER C -2 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ASN C -1 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I ALA C 0 UNP Q81AD5 CLONING ARTIFACT
SEQADV 2H1I MSE C 1 UNP Q81AD5 MET 1 MODIFIED RESIDUE
SEQADV 2H1I MSE C 2 UNP Q81AD5 MET 2 MODIFIED RESIDUE
SEQADV 2H1I MSE C 55 UNP Q81AD5 MET 55 MODIFIED RESIDUE
SEQADV 2H1I MSE C 129 UNP Q81AD5 MET 129 MODIFIED RESIDUE
SEQADV 2H1I MSE C 135 UNP Q81AD5 MET 135 MODIFIED RESIDUE
SEQADV 2H1I MSE C 177 UNP Q81AD5 MET 177 MODIFIED RESIDUE
SEQADV 2H1I MSE C 188 UNP Q81AD5 MET 188 MODIFIED RESIDUE
SEQRES 1 A 226 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 226 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE MSE
SEQRES 3 A 226 LYS HIS VAL PHE GLN LYS GLY LYS ASP THR SER LYS PRO
SEQRES 4 A 226 VAL LEU LEU LEU LEU HIS GLY THR GLY GLY ASN GLU LEU
SEQRES 5 A 226 ASP LEU LEU PRO LEU ALA GLU ILE VAL ASP SER GLU ALA
SEQRES 6 A 226 SER VAL LEU SER VAL ARG GLY ASN VAL LEU GLU ASN GLY
SEQRES 7 A 226 MSE PRO ARG PHE PHE ARG ARG LEU ALA GLU GLY ILE PHE
SEQRES 8 A 226 ASP GLU GLU ASP LEU ILE PHE ARG THR LYS GLU LEU ASN
SEQRES 9 A 226 GLU PHE LEU ASP GLU ALA ALA LYS GLU TYR LYS PHE ASP
SEQRES 10 A 226 ARG ASN ASN ILE VAL ALA ILE GLY TYR SER ASN GLY ALA
SEQRES 11 A 226 ASN ILE ALA ALA SER LEU LEU PHE HIS TYR GLU ASN ALA
SEQRES 12 A 226 LEU LYS GLY ALA VAL LEU HIS HIS PRO MSE VAL PRO ARG
SEQRES 13 A 226 ARG GLY MSE GLN LEU ALA ASN LEU ALA GLY LYS SER VAL
SEQRES 14 A 226 PHE ILE ALA ALA GLY THR ASN ASP PRO ILE CYS SER SER
SEQRES 15 A 226 ALA GLU SER GLU GLU LEU LYS VAL LEU LEU GLU ASN ALA
SEQRES 16 A 226 ASN ALA ASN VAL THR MSE HIS TRP GLU ASN ARG GLY HIS
SEQRES 17 A 226 GLN LEU THR MSE GLY GLU VAL GLU LYS ALA LYS GLU TRP
SEQRES 18 A 226 TYR ASP LYS ALA PHE
SEQRES 1 B 226 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 226 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE MSE
SEQRES 3 B 226 LYS HIS VAL PHE GLN LYS GLY LYS ASP THR SER LYS PRO
SEQRES 4 B 226 VAL LEU LEU LEU LEU HIS GLY THR GLY GLY ASN GLU LEU
SEQRES 5 B 226 ASP LEU LEU PRO LEU ALA GLU ILE VAL ASP SER GLU ALA
SEQRES 6 B 226 SER VAL LEU SER VAL ARG GLY ASN VAL LEU GLU ASN GLY
SEQRES 7 B 226 MSE PRO ARG PHE PHE ARG ARG LEU ALA GLU GLY ILE PHE
SEQRES 8 B 226 ASP GLU GLU ASP LEU ILE PHE ARG THR LYS GLU LEU ASN
SEQRES 9 B 226 GLU PHE LEU ASP GLU ALA ALA LYS GLU TYR LYS PHE ASP
SEQRES 10 B 226 ARG ASN ASN ILE VAL ALA ILE GLY TYR SER ASN GLY ALA
SEQRES 11 B 226 ASN ILE ALA ALA SER LEU LEU PHE HIS TYR GLU ASN ALA
SEQRES 12 B 226 LEU LYS GLY ALA VAL LEU HIS HIS PRO MSE VAL PRO ARG
SEQRES 13 B 226 ARG GLY MSE GLN LEU ALA ASN LEU ALA GLY LYS SER VAL
SEQRES 14 B 226 PHE ILE ALA ALA GLY THR ASN ASP PRO ILE CYS SER SER
SEQRES 15 B 226 ALA GLU SER GLU GLU LEU LYS VAL LEU LEU GLU ASN ALA
SEQRES 16 B 226 ASN ALA ASN VAL THR MSE HIS TRP GLU ASN ARG GLY HIS
SEQRES 17 B 226 GLN LEU THR MSE GLY GLU VAL GLU LYS ALA LYS GLU TRP
SEQRES 18 B 226 TYR ASP LYS ALA PHE
SEQRES 1 C 226 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 226 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE MSE
SEQRES 3 C 226 LYS HIS VAL PHE GLN LYS GLY LYS ASP THR SER LYS PRO
SEQRES 4 C 226 VAL LEU LEU LEU LEU HIS GLY THR GLY GLY ASN GLU LEU
SEQRES 5 C 226 ASP LEU LEU PRO LEU ALA GLU ILE VAL ASP SER GLU ALA
SEQRES 6 C 226 SER VAL LEU SER VAL ARG GLY ASN VAL LEU GLU ASN GLY
SEQRES 7 C 226 MSE PRO ARG PHE PHE ARG ARG LEU ALA GLU GLY ILE PHE
SEQRES 8 C 226 ASP GLU GLU ASP LEU ILE PHE ARG THR LYS GLU LEU ASN
SEQRES 9 C 226 GLU PHE LEU ASP GLU ALA ALA LYS GLU TYR LYS PHE ASP
SEQRES 10 C 226 ARG ASN ASN ILE VAL ALA ILE GLY TYR SER ASN GLY ALA
SEQRES 11 C 226 ASN ILE ALA ALA SER LEU LEU PHE HIS TYR GLU ASN ALA
SEQRES 12 C 226 LEU LYS GLY ALA VAL LEU HIS HIS PRO MSE VAL PRO ARG
SEQRES 13 C 226 ARG GLY MSE GLN LEU ALA ASN LEU ALA GLY LYS SER VAL
SEQRES 14 C 226 PHE ILE ALA ALA GLY THR ASN ASP PRO ILE CYS SER SER
SEQRES 15 C 226 ALA GLU SER GLU GLU LEU LYS VAL LEU LEU GLU ASN ALA
SEQRES 16 C 226 ASN ALA ASN VAL THR MSE HIS TRP GLU ASN ARG GLY HIS
SEQRES 17 C 226 GLN LEU THR MSE GLY GLU VAL GLU LYS ALA LYS GLU TRP
SEQRES 18 C 226 TYR ASP LYS ALA PHE
MODRES 2H1I MSE A 1 MET SELENOMETHIONINE
MODRES 2H1I MSE A 2 MET SELENOMETHIONINE
MODRES 2H1I MSE A 55 MET SELENOMETHIONINE
MODRES 2H1I MSE A 129 MET SELENOMETHIONINE
MODRES 2H1I MSE A 135 MET SELENOMETHIONINE
MODRES 2H1I MSE A 177 MET SELENOMETHIONINE
MODRES 2H1I MSE A 188 MET SELENOMETHIONINE
MODRES 2H1I MSE B 1 MET SELENOMETHIONINE
MODRES 2H1I MSE B 2 MET SELENOMETHIONINE
MODRES 2H1I MSE B 55 MET SELENOMETHIONINE
MODRES 2H1I MSE B 129 MET SELENOMETHIONINE
MODRES 2H1I MSE B 135 MET SELENOMETHIONINE
MODRES 2H1I MSE B 177 MET SELENOMETHIONINE
MODRES 2H1I MSE B 188 MET SELENOMETHIONINE
MODRES 2H1I MSE C 1 MET SELENOMETHIONINE
MODRES 2H1I MSE C 2 MET SELENOMETHIONINE
MODRES 2H1I MSE C 55 MET SELENOMETHIONINE
MODRES 2H1I MSE C 129 MET SELENOMETHIONINE
MODRES 2H1I MSE C 135 MET SELENOMETHIONINE
MODRES 2H1I MSE C 177 MET SELENOMETHIONINE
MODRES 2H1I MSE C 188 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 2 8
HET MSE A 55 8
HET MSE A 129 8
HET MSE A 135 8
HET MSE A 177 8
HET MSE A 188 8
HET MSE B 1 8
HET MSE B 2 8
HET MSE B 55 8
HET MSE B 129 8
HET MSE B 135 8
HET MSE B 177 8
HET MSE B 188 8
HET MSE C 1 16
HET MSE C 2 8
HET MSE C 55 8
HET MSE C 129 8
HET MSE C 135 8
HET MSE C 177 8
HET MSE C 188 8
HET ZN A 300 1
HET ZN B 300 1
HET ZN C 300 1
HET CA A 301 1
HET CA B 301 1
HET CA B 302 1
HET CA C 301 1
HET CL A 302 1
HET CL B 303 1
HET CL C 302 1
HET CL B 304 1
HET CL C 303 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 21(C5 H11 N O2 SE)
FORMUL 4 ZN 3(ZN 2+)
FORMUL 7 CA 4(CA 2+)
FORMUL 11 CL 5(CL 1-)
FORMUL 16 HOH *193(H2 O)
HELIX 1 1 ASN A -7 ALA A 0 1 8
HELIX 2 2 LEU A 30 SER A 39 1 10
HELIX 3 3 ASP A 68 TYR A 90 1 23
HELIX 4 4 SER A 103 TYR A 116 1 14
HELIX 5 5 SER A 157 ASN A 170 1 14
HELIX 6 6 THR A 187 PHE A 202 1 16
HELIX 7 7 LEU B 30 ASP B 38 1 9
HELIX 8 8 ASP B 68 LYS B 91 1 24
HELIX 9 9 SER B 103 TYR B 116 1 14
HELIX 10 10 SER B 157 ALA B 171 1 15
HELIX 11 11 THR B 187 PHE B 202 1 16
HELIX 12 12 LEU C 30 SER C 39 1 10
HELIX 13 13 ASP C 68 LYS C 91 1 24
HELIX 14 14 SER C 103 TYR C 116 1 14
HELIX 15 15 SER C 157 ALA C 171 1 15
HELIX 16 16 THR C 187 PHE C 202 1 16
SHEET 1 A 7 HIS A 4 GLN A 7 0
SHEET 2 A 7 VAL A 43 VAL A 46 -1 O SER A 45 N VAL A 5
SHEET 3 A 7 VAL A 16 LEU A 20 1 N LEU A 19 O LEU A 44
SHEET 4 A 7 ILE A 97 TYR A 102 1 O ILE A 100 N LEU A 18
SHEET 5 A 7 GLY A 122 HIS A 126 1 O VAL A 124 N ALA A 99
SHEET 6 A 7 SER A 144 GLY A 150 1 O PHE A 146 N LEU A 125
SHEET 7 A 7 ASN A 174 GLU A 180 1 O ASN A 174 N VAL A 145
SHEET 1 B 2 VAL A 50 GLU A 52 0
SHEET 2 B 2 MSE A 55 ARG A 57 -1 O ARG A 57 N VAL A 50
SHEET 1 C 2 ARG A 61 ALA A 63 0
SHEET 2 C 2 ILE A 66 PHE A 67 -1 O ILE A 66 N ALA A 63
SHEET 1 D 7 HIS B 4 GLN B 7 0
SHEET 2 D 7 VAL B 43 VAL B 46 -1 O VAL B 43 N GLN B 7
SHEET 3 D 7 VAL B 16 LEU B 20 1 N LEU B 19 O LEU B 44
SHEET 4 D 7 ILE B 97 TYR B 102 1 O ILE B 100 N LEU B 18
SHEET 5 D 7 GLY B 122 HIS B 126 1 O VAL B 124 N ALA B 99
SHEET 6 D 7 SER B 144 GLY B 150 1 O PHE B 146 N LEU B 125
SHEET 7 D 7 ASN B 174 GLU B 180 1 O ASN B 174 N VAL B 145
SHEET 1 E 2 VAL B 50 GLU B 52 0
SHEET 2 E 2 MSE B 55 ARG B 57 -1 O ARG B 57 N VAL B 50
SHEET 1 F 2 ARG B 61 ALA B 63 0
SHEET 2 F 2 ILE B 66 PHE B 67 -1 O ILE B 66 N ALA B 63
SHEET 1 G 7 HIS C 4 GLN C 7 0
SHEET 2 G 7 SER C 42 VAL C 46 -1 O VAL C 43 N GLN C 7
SHEET 3 G 7 VAL C 16 LEU C 20 1 N LEU C 17 O LEU C 44
SHEET 4 G 7 ILE C 97 TYR C 102 1 O ILE C 100 N LEU C 18
SHEET 5 G 7 GLY C 122 HIS C 126 1 O VAL C 124 N ALA C 99
SHEET 6 G 7 SER C 144 GLY C 150 1 O PHE C 146 N LEU C 125
SHEET 7 G 7 ASN C 174 GLU C 180 1 O THR C 176 N ILE C 147
SHEET 1 H 2 VAL C 50 LEU C 51 0
SHEET 2 H 2 PRO C 56 ARG C 57 -1 O ARG C 57 N VAL C 50
SHEET 1 I 2 ARG C 61 ALA C 63 0
SHEET 2 I 2 ILE C 66 PHE C 67 -1 O ILE C 66 N LEU C 62
LINK ZN ZN A 300 OD2 ASP A 153 1555 1555 1.83
LINK ZN ZN B 300 OD2 ASP B 153 1555 1555 2.23
LINK ZN ZN C 300 OD2 ASP C 153 1555 1555 2.08
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N MSE A 2 1555 1555 1.33
LINK C MSE A 2 N LYS A 3 1555 1555 1.33
LINK C GLY A 54 N MSE A 55 1555 1555 1.33
LINK C MSE A 55 N PRO A 56 1555 1555 1.33
LINK C PRO A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N VAL A 130 1555 1555 1.32
LINK C GLY A 134 N MSE A 135 1555 1555 1.32
LINK C MSE A 135 N GLN A 136 1555 1555 1.33
LINK C THR A 176 N MSE A 177 1555 1555 1.32
LINK C MSE A 177 N HIS A 178 1555 1555 1.33
LINK C THR A 187 N MSE A 188 1555 1555 1.33
LINK C MSE A 188 N GLY A 189 1555 1555 1.33
LINK ZN ZN A 300 SG CYS A 156 1555 1555 2.58
LINK ZN ZN A 300 ND1 HIS A 127 1555 1555 2.63
LINK ZN ZN A 300 ND1 HIS A 184 1555 1555 2.12
LINK CA CA A 301 OD1 ASN A 53 1555 1555 2.56
LINK CA CA A 301 ND2 ASN A 53 1555 1555 3.06
LINK CA CA A 301 OE1 GLU B 89 1555 1555 2.66
LINK CA CA A 301 OE2 GLU B 89 1555 1555 2.89
LINK CA CA A 301 O HOH B 329 1555 1555 3.31
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N MSE B 2 1555 1555 1.33
LINK C MSE B 2 N LYS B 3 1555 1555 1.32
LINK C GLY B 54 N MSE B 55 1555 1555 1.32
LINK C MSE B 55 N PRO B 56 1555 1555 1.34
LINK C PRO B 128 N MSE B 129 1555 1555 1.33
LINK C MSE B 129 N VAL B 130 1555 1555 1.33
LINK C GLY B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N GLN B 136 1555 1555 1.33
LINK C THR B 176 N MSE B 177 1555 1555 1.33
LINK C MSE B 177 N HIS B 178 1555 1555 1.32
LINK C THR B 187 N MSE B 188 1555 1555 1.33
LINK C MSE B 188 N GLY B 189 1555 1555 1.33
LINK ZN ZN B 300 ND1 HIS B 184 1555 1555 2.19
LINK ZN ZN B 300 ND1 HIS B 127 1555 1555 2.73
LINK CA CA B 301 O HOH B 384 1555 1555 2.75
LINK CA CA B 301 OD2 ASP B 84 1555 1555 2.40
LINK CA CA B 301 OE1 GLU B 81 1555 1555 2.28
LINK CA CA B 301 OE2 GLU B 81 1555 1555 3.02
LINK CA CA B 302 OE2 GLU B 85 1555 1555 2.31
LINK CA CA B 302 OE2 GLU B 81 1555 1555 2.46
LINK C BALA C 0 N BMSE C 1 1555 1555 1.33
LINK C AALA C 0 N AMSE C 1 1555 1555 1.33
LINK C BMSE C 1 N MSE C 2 1555 1555 1.33
LINK C AMSE C 1 N MSE C 2 1555 1555 1.33
LINK C MSE C 2 N LYS C 3 1555 1555 1.32
LINK C GLY C 54 N MSE C 55 1555 1555 1.33
LINK C MSE C 55 N PRO C 56 1555 1555 1.34
LINK C PRO C 128 N MSE C 129 1555 1555 1.33
LINK C MSE C 129 N VAL C 130 1555 1555 1.32
LINK C GLY C 134 N MSE C 135 1555 1555 1.32
LINK C MSE C 135 N GLN C 136 1555 1555 1.33
LINK C THR C 176 N MSE C 177 1555 1555 1.33
LINK C MSE C 177 N HIS C 178 1555 1555 1.32
LINK C THR C 187 N MSE C 188 1555 1555 1.32
LINK C MSE C 188 N GLY C 189 1555 1555 1.33
LINK ZN ZN C 300 ND1 HIS C 127 1555 1555 2.21
LINK ZN ZN C 300 ND1 HIS C 184 1555 1555 2.17
LINK ZN ZN C 300 SG CYS C 156 1555 1555 2.37
LINK CA CA C 301 O CYS C 156 1555 1555 2.39
LINK CA CA C 301 O HOH C 340 1555 1555 2.95
LINK CA CA C 301 O ASP C 153 1555 1555 2.21
LINK CA CA B 301 OE2 GLU C 85 1555 6655 2.64
LINK CA CA B 301 O HOH C 351 1555 6655 2.57
LINK CA CA B 301 OE2 GLU C 81 1555 6655 2.17
LINK CA CA B 302 OE1 GLU C 81 1555 6655 2.17
LINK CA CA B 302 OD2 ASP C 84 1555 6655 2.33
LINK SG CYS B 156 ZN ZN B 300 1555 1555 2.99
SITE 1 AC1 4 HIS A 127 ASP A 153 CYS A 156 HIS A 184
SITE 1 AC2 4 HIS B 127 ASP B 153 CYS B 156 HIS B 184
SITE 1 AC3 4 HIS C 127 ASP C 153 CYS C 156 HIS C 184
SITE 1 AC4 3 ASN A 53 GLU B 89 GLU C 117
SITE 1 AC5 6 GLU B 81 ASP B 84 HOH B 384 GLU C 81
SITE 2 AC5 6 GLU C 85 HOH C 351
SITE 1 AC6 4 GLU B 81 GLU B 85 GLU C 81 ASP C 84
SITE 1 AC7 3 ASP C 153 CYS C 156 HOH C 340
SITE 1 AC8 3 ARG A 57 ASN A 104 ASN A 107
SITE 1 AC9 4 ARG B 57 PHE B 67 ASN B 104 ASN B 107
SITE 1 BC1 4 ARG C 57 PHE C 67 ASN C 104 ASN C 107
SITE 1 BC2 5 ASN B 80 ALA B 119 HOH B 305 HOH B 375
SITE 2 BC2 5 LYS C 88
SITE 1 BC3 5 LYS B 88 ASN C 80 ASN C 118 ALA C 119
SITE 2 BC3 5 HOH C 334
CRYST1 99.607 99.607 160.234 90.00 90.00 120.00 P 61 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 0.010039 0.005796 0.000000 0.00000
SCALE2 0.000000 0.011593 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006241 0.00000
TER 1669 PHE A 202
TER 3268 PHE B 202
TER 4872 PHE C 202
MASTER 492 0 33 16 33 0 15 6 5074 3 246 54
END |