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HEADER OXIDOREDUCTASE 29-DEC-08 3FOB
TITLE CRYSTAL STRUCTURE OF BROMOPEROXIDASE FROM BACILLUS ANTHRACIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMOPEROXIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. AMES;
SOURCE 3 ORGANISM_COMMON: ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 198094;
SOURCE 5 STRAIN: AMES;
SOURCE 6 GENE: BAS2941, BA_3165, GBAA3165;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, IDP00046, BROMOPEROXIDASE, BACILLUS
KEYWDS 2 ANTHRACIS, PEROXIDASE, OXIDOREDUCTASE, CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,M.GU,J.STAM,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 1 06-JAN-09 3FOB 0
JRNL AUTH J.OSIPIUK,M.GU,J.STAM,W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF BROMOPEROXIDASE FROM
JRNL TITL 2 BACILLUS ANTHRACIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 75908
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3809
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) : 1.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4977
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 728
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.303
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6885 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4629 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9393 ; 1.680 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11309 ; 0.977 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 883 ; 5.888 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 334 ;37.053 ;24.401
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1115 ;15.673 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;14.598 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1012 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7845 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1451 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4207 ; 0.965 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1727 ; 0.338 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6797 ; 1.607 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2678 ; 2.710 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2570 ; 4.192 ; 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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 278
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2951 -24.0709 100.2243
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0070
REMARK 3 T33: 0.0034 T12: 0.0085
REMARK 3 T13: -0.0047 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.6510 L22: 0.4899
REMARK 3 L33: 0.8466 L12: 0.0989
REMARK 3 L13: 0.0380 L23: -0.0585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: 0.0097 S13: -0.0084
REMARK 3 S21: 0.0313 S22: -0.0122 S23: 0.0220
REMARK 3 S31: 0.0619 S32: 0.0325 S33: -0.0036
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 278
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1528 -12.8519 66.7350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0138 T22: 0.0235
REMARK 3 T33: 0.0147 T12: -0.0002
REMARK 3 T13: -0.0062 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.0020 L22: 0.3730
REMARK 3 L33: 0.9364 L12: 0.1500
REMARK 3 L13: -0.0991 L23: 0.1349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: 0.0644 S13: 0.0701
REMARK 3 S21: 0.0157 S22: -0.0045 S23: 0.0165
REMARK 3 S31: 0.0129 S32: 0.0973 S33: -0.0227
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 278
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4916 -24.9977 69.4002
REMARK 3 T TENSOR
REMARK 3 T11: 0.0211 T22: 0.0264
REMARK 3 T33: 0.0496 T12: -0.0039
REMARK 3 T13: -0.0135 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4489 L22: 0.5339
REMARK 3 L33: 0.8451 L12: 0.1310
REMARK 3 L13: -0.0918 L23: 0.0458
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: 0.0430 S13: 0.0723
REMARK 3 S21: 0.0248 S22: 0.0176 S23: 0.1182
REMARK 3 S31: -0.0007 S32: -0.1398 S33: 0.0165
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 3FOB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050837.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-08
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) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 28.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.4050
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.560
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, HKL-3000
REMARK 200 STARTING MODEL: PDB ENTRY 1BRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M
REMARK 280 HEPES BUFFER, 25% PEG 3350, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
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 24.16300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: ACCORDING TO AUTHORS, THE BIOLOGICAL UNIT ASSEMBLY THAT
REMARK 300 IS SHOWN IN REMARK 350 IS PUTATIVE AT THE TIME OF DEPOSITION.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.3 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 THR B 5
REMARK 465 VAL B 6
REMARK 465 GLY B 7
REMARK 465 THR B 8
REMARK 465 GLU B 9
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MSE C 1
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 ND2 ASN B 218 O HOH B 474 1.94
REMARK 500 OE1 GLU A 267 O HOH A 638 2.04
REMARK 500 O HOH C 515 O HOH C 699 2.04
REMARK 500 O HOH B 295 O HOH B 685 2.05
REMARK 500 OE2 GLU B 70 O HOH B 357 2.09
REMARK 500 OE1 GLU A 267 O HOH A 502 2.10
REMARK 500 ND1 HIS B 21 O HOH B 720 2.15
REMARK 500 O HOH A 354 O HOH A 542 2.16
REMARK 500 OD1 ASN B 10 O HOH B 643 2.16
REMARK 500 OE1 GLU C 180 NH1 ARG C 183 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 38 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 10 41.65 39.29
REMARK 500 PRO A 34 54.56 -103.44
REMARK 500 LEU A 35 -136.11 -98.50
REMARK 500 GLN A 67 74.65 -118.18
REMARK 500 TYR A 129 104.73 -175.30
REMARK 500 ASP A 156 83.75 -161.16
REMARK 500 SER A 237 -92.67 -150.74
REMARK 500 PRO B 34 52.31 -104.96
REMARK 500 LEU B 35 -133.24 -98.26
REMARK 500 TYR B 129 105.03 -175.31
REMARK 500 ASP B 156 84.17 -153.84
REMARK 500 SER B 237 -94.43 -149.19
REMARK 500 ASN B 247 -3.34 75.08
REMARK 500 GLN C 11 -1.13 68.42
REMARK 500 PRO C 34 59.26 -110.48
REMARK 500 LEU C 35 -139.30 -103.38
REMARK 500 TYR C 129 104.23 179.80
REMARK 500 ASP C 156 87.22 -155.18
REMARK 500 ASN C 218 43.61 -141.98
REMARK 500 SER C 237 -87.37 -142.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 652 DISTANCE = 5.00 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 117 O
REMARK 620 2 HOH A 682 O 71.5
REMARK 620 3 HOH A 603 O 170.8 100.0
REMARK 620 4 HOH A 706 O 84.3 73.3 90.1
REMARK 620 5 HOH A 531 O 95.5 141.6 89.3 69.5
REMARK 620 6 HOH A 424 O 95.5 109.8 90.5 176.7 107.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 328 O
REMARK 620 2 HOH C 308 O 92.7
REMARK 620 3 HOH A 281 O 92.2 93.2
REMARK 620 4 HOH B 365 O 86.0 89.4 176.9
REMARK 620 5 HOH C 289 O 176.4 88.7 91.0 90.7
REMARK 620 6 HOH A 284 O 88.9 176.3 90.1 87.3 89.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 404
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BRO RELATED DB: PDB
REMARK 900 BROMOPEROXIDASE A2
REMARK 900 RELATED ID: IDP00046 RELATED DB: TARGETDB
DBREF 3FOB A 1 278 UNP Q81NM3 Q81NM3_BACAN 1 278
DBREF 3FOB B 1 278 UNP Q81NM3 Q81NM3_BACAN 1 278
DBREF 3FOB C 1 278 UNP Q81NM3 Q81NM3_BACAN 1 278
SEQADV 3FOB SER A -2 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ASN A -1 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ALA A 0 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB SER B -2 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ASN B -1 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ALA B 0 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB SER C -2 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ASN C -1 UNP Q81NM3 EXPRESSION TAG
SEQADV 3FOB ALA C 0 UNP Q81NM3 EXPRESSION TAG
SEQRES 1 A 281 SER ASN ALA MSE ALA LYS ILE THR VAL GLY THR GLU ASN
SEQRES 2 A 281 GLN ALA PRO ILE GLU ILE TYR TYR GLU ASP HIS GLY THR
SEQRES 3 A 281 GLY LYS PRO VAL VAL LEU ILE HIS GLY TRP PRO LEU SER
SEQRES 4 A 281 GLY ARG SER TRP GLU TYR GLN VAL PRO ALA LEU VAL GLU
SEQRES 5 A 281 ALA GLY TYR ARG VAL ILE THR TYR ASP ARG ARG GLY PHE
SEQRES 6 A 281 GLY LYS SER SER GLN PRO TRP GLU GLY TYR GLU TYR ASP
SEQRES 7 A 281 THR PHE THR SER ASP LEU HIS GLN LEU LEU GLU GLN LEU
SEQRES 8 A 281 GLU LEU GLN ASN VAL THR LEU VAL GLY PHE SER MSE GLY
SEQRES 9 A 281 GLY GLY GLU VAL ALA ARG TYR ILE SER THR TYR GLY THR
SEQRES 10 A 281 ASP ARG ILE GLU LYS VAL VAL PHE ALA GLY ALA VAL PRO
SEQRES 11 A 281 PRO TYR LEU TYR LYS SER GLU ASP HIS PRO GLU GLY ALA
SEQRES 12 A 281 LEU ASP ASP ALA THR ILE GLU THR PHE LYS SER GLY VAL
SEQRES 13 A 281 ILE ASN ASP ARG LEU ALA PHE LEU ASP GLU PHE THR LYS
SEQRES 14 A 281 GLY PHE PHE ALA ALA GLY ASP ARG THR ASP LEU VAL SER
SEQRES 15 A 281 GLU SER PHE ARG LEU TYR ASN TRP ASP ILE ALA ALA GLY
SEQRES 16 A 281 ALA SER PRO LYS GLY THR LEU ASP CYS ILE THR ALA PHE
SEQRES 17 A 281 SER LYS THR ASP PHE ARG LYS ASP LEU GLU LYS PHE ASN
SEQRES 18 A 281 ILE PRO THR LEU ILE ILE HIS GLY ASP SER ASP ALA THR
SEQRES 19 A 281 VAL PRO PHE GLU TYR SER GLY LYS LEU THR HIS GLU ALA
SEQRES 20 A 281 ILE PRO ASN SER LYS VAL ALA LEU ILE LYS GLY GLY PRO
SEQRES 21 A 281 HIS GLY LEU ASN ALA THR HIS ALA LYS GLU PHE ASN GLU
SEQRES 22 A 281 ALA LEU LEU LEU PHE LEU LYS ASP
SEQRES 1 B 281 SER ASN ALA MSE ALA LYS ILE THR VAL GLY THR GLU ASN
SEQRES 2 B 281 GLN ALA PRO ILE GLU ILE TYR TYR GLU ASP HIS GLY THR
SEQRES 3 B 281 GLY LYS PRO VAL VAL LEU ILE HIS GLY TRP PRO LEU SER
SEQRES 4 B 281 GLY ARG SER TRP GLU TYR GLN VAL PRO ALA LEU VAL GLU
SEQRES 5 B 281 ALA GLY TYR ARG VAL ILE THR TYR ASP ARG ARG GLY PHE
SEQRES 6 B 281 GLY LYS SER SER GLN PRO TRP GLU GLY TYR GLU TYR ASP
SEQRES 7 B 281 THR PHE THR SER ASP LEU HIS GLN LEU LEU GLU GLN LEU
SEQRES 8 B 281 GLU LEU GLN ASN VAL THR LEU VAL GLY PHE SER MSE GLY
SEQRES 9 B 281 GLY GLY GLU VAL ALA ARG TYR ILE SER THR TYR GLY THR
SEQRES 10 B 281 ASP ARG ILE GLU LYS VAL VAL PHE ALA GLY ALA VAL PRO
SEQRES 11 B 281 PRO TYR LEU TYR LYS SER GLU ASP HIS PRO GLU GLY ALA
SEQRES 12 B 281 LEU ASP ASP ALA THR ILE GLU THR PHE LYS SER GLY VAL
SEQRES 13 B 281 ILE ASN ASP ARG LEU ALA PHE LEU ASP GLU PHE THR LYS
SEQRES 14 B 281 GLY PHE PHE ALA ALA GLY ASP ARG THR ASP LEU VAL SER
SEQRES 15 B 281 GLU SER PHE ARG LEU TYR ASN TRP ASP ILE ALA ALA GLY
SEQRES 16 B 281 ALA SER PRO LYS GLY THR LEU ASP CYS ILE THR ALA PHE
SEQRES 17 B 281 SER LYS THR ASP PHE ARG LYS ASP LEU GLU LYS PHE ASN
SEQRES 18 B 281 ILE PRO THR LEU ILE ILE HIS GLY ASP SER ASP ALA THR
SEQRES 19 B 281 VAL PRO PHE GLU TYR SER GLY LYS LEU THR HIS GLU ALA
SEQRES 20 B 281 ILE PRO ASN SER LYS VAL ALA LEU ILE LYS GLY GLY PRO
SEQRES 21 B 281 HIS GLY LEU ASN ALA THR HIS ALA LYS GLU PHE ASN GLU
SEQRES 22 B 281 ALA LEU LEU LEU PHE LEU LYS ASP
SEQRES 1 C 281 SER ASN ALA MSE ALA LYS ILE THR VAL GLY THR GLU ASN
SEQRES 2 C 281 GLN ALA PRO ILE GLU ILE TYR TYR GLU ASP HIS GLY THR
SEQRES 3 C 281 GLY LYS PRO VAL VAL LEU ILE HIS GLY TRP PRO LEU SER
SEQRES 4 C 281 GLY ARG SER TRP GLU TYR GLN VAL PRO ALA LEU VAL GLU
SEQRES 5 C 281 ALA GLY TYR ARG VAL ILE THR TYR ASP ARG ARG GLY PHE
SEQRES 6 C 281 GLY LYS SER SER GLN PRO TRP GLU GLY TYR GLU TYR ASP
SEQRES 7 C 281 THR PHE THR SER ASP LEU HIS GLN LEU LEU GLU GLN LEU
SEQRES 8 C 281 GLU LEU GLN ASN VAL THR LEU VAL GLY PHE SER MSE GLY
SEQRES 9 C 281 GLY GLY GLU VAL ALA ARG TYR ILE SER THR TYR GLY THR
SEQRES 10 C 281 ASP ARG ILE GLU LYS VAL VAL PHE ALA GLY ALA VAL PRO
SEQRES 11 C 281 PRO TYR LEU TYR LYS SER GLU ASP HIS PRO GLU GLY ALA
SEQRES 12 C 281 LEU ASP ASP ALA THR ILE GLU THR PHE LYS SER GLY VAL
SEQRES 13 C 281 ILE ASN ASP ARG LEU ALA PHE LEU ASP GLU PHE THR LYS
SEQRES 14 C 281 GLY PHE PHE ALA ALA GLY ASP ARG THR ASP LEU VAL SER
SEQRES 15 C 281 GLU SER PHE ARG LEU TYR ASN TRP ASP ILE ALA ALA GLY
SEQRES 16 C 281 ALA SER PRO LYS GLY THR LEU ASP CYS ILE THR ALA PHE
SEQRES 17 C 281 SER LYS THR ASP PHE ARG LYS ASP LEU GLU LYS PHE ASN
SEQRES 18 C 281 ILE PRO THR LEU ILE ILE HIS GLY ASP SER ASP ALA THR
SEQRES 19 C 281 VAL PRO PHE GLU TYR SER GLY LYS LEU THR HIS GLU ALA
SEQRES 20 C 281 ILE PRO ASN SER LYS VAL ALA LEU ILE LYS GLY GLY PRO
SEQRES 21 C 281 HIS GLY LEU ASN ALA THR HIS ALA LYS GLU PHE ASN GLU
SEQRES 22 C 281 ALA LEU LEU LEU PHE LEU LYS ASP
MODRES 3FOB MSE A 100 MET SELENOMETHIONINE
MODRES 3FOB MSE B 1 MET SELENOMETHIONINE
MODRES 3FOB MSE B 100 MET SELENOMETHIONINE
MODRES 3FOB MSE C 100 MET SELENOMETHIONINE
HET MSE A 100 8
HET MSE B 1 8
HET MSE B 100 8
HET MSE C 100 8
HET CL A 401 1
HET NA A 404 1
HET NA A 405 1
HET CL B 402 1
HET CL C 403 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 4 CL 3(CL 1-)
FORMUL 5 NA 2(NA 1+)
FORMUL 9 HOH *723(H2 O)
HELIX 1 1 SER A 36 GLU A 41 5 6
HELIX 2 2 GLN A 43 ALA A 50 1 8
HELIX 3 3 GLU A 73 LEU A 88 1 16
HELIX 4 4 MSE A 100 GLY A 113 1 14
HELIX 5 5 ASP A 142 PHE A 169 1 28
HELIX 6 6 SER A 179 GLY A 192 1 14
HELIX 7 7 SER A 194 THR A 208 1 15
HELIX 8 8 PHE A 210 GLU A 215 1 6
HELIX 9 9 PRO A 233 TYR A 236 5 4
HELIX 10 10 SER A 237 ILE A 245 1 9
HELIX 11 11 GLY A 259 HIS A 264 1 6
HELIX 12 12 HIS A 264 LYS A 277 1 14
HELIX 13 13 SER B 36 GLU B 41 5 6
HELIX 14 14 GLN B 43 ALA B 50 1 8
HELIX 15 15 GLU B 73 LEU B 88 1 16
HELIX 16 16 MSE B 100 GLY B 113 1 14
HELIX 17 17 ASP B 142 PHE B 169 1 28
HELIX 18 18 SER B 179 GLY B 192 1 14
HELIX 19 19 SER B 194 THR B 208 1 15
HELIX 20 20 PHE B 210 GLU B 215 1 6
HELIX 21 21 PRO B 233 TYR B 236 5 4
HELIX 22 22 SER B 237 ILE B 245 1 9
HELIX 23 23 GLY B 259 HIS B 264 1 6
HELIX 24 24 HIS B 264 ASP B 278 1 15
HELIX 25 25 SER C 36 GLU C 41 5 6
HELIX 26 26 GLN C 43 ALA C 50 1 8
HELIX 27 27 GLU C 73 LEU C 88 1 16
HELIX 28 28 MSE C 100 GLY C 113 1 14
HELIX 29 29 ASP C 142 PHE C 169 1 28
HELIX 30 30 SER C 179 GLY C 192 1 14
HELIX 31 31 SER C 194 THR C 208 1 15
HELIX 32 32 PHE C 210 GLU C 215 1 6
HELIX 33 33 PRO C 233 TYR C 236 5 4
HELIX 34 34 SER C 237 ILE C 245 1 9
HELIX 35 35 GLY C 259 HIS C 264 1 6
HELIX 36 36 HIS C 264 ASP C 278 1 15
SHEET 1 A 8 LYS A 3 GLU A 9 0
SHEET 2 A 8 ALA A 12 HIS A 21 -1 O ILE A 16 N ILE A 4
SHEET 3 A 8 TYR A 52 TYR A 57 -1 O VAL A 54 N HIS A 21
SHEET 4 A 8 LYS A 25 ILE A 30 1 N VAL A 27 O ARG A 53
SHEET 5 A 8 VAL A 93 PHE A 98 1 O VAL A 96 N VAL A 28
SHEET 6 A 8 ILE A 117 ALA A 123 1 O GLU A 118 N VAL A 93
SHEET 7 A 8 THR A 221 GLY A 226 1 O LEU A 222 N PHE A 122
SHEET 8 A 8 LYS A 249 ILE A 253 1 O ALA A 251 N ILE A 223
SHEET 1 B 8 ASN B -1 LYS B 3 0
SHEET 2 B 8 GLU B 15 HIS B 21 -1 O ILE B 16 N ALA B 2
SHEET 3 B 8 TYR B 52 TYR B 57 -1 O VAL B 54 N HIS B 21
SHEET 4 B 8 LYS B 25 ILE B 30 1 N LEU B 29 O ILE B 55
SHEET 5 B 8 VAL B 93 PHE B 98 1 O VAL B 96 N ILE B 30
SHEET 6 B 8 ILE B 117 ALA B 123 1 O VAL B 121 N GLY B 97
SHEET 7 B 8 THR B 221 GLY B 226 1 O LEU B 222 N PHE B 122
SHEET 8 B 8 LYS B 249 ILE B 253 1 O LYS B 249 N ILE B 223
SHEET 1 C 8 LYS C 3 GLU C 9 0
SHEET 2 C 8 ALA C 12 HIS C 21 -1 O ILE C 16 N ILE C 4
SHEET 3 C 8 TYR C 52 TYR C 57 -1 O VAL C 54 N HIS C 21
SHEET 4 C 8 LYS C 25 ILE C 30 1 N VAL C 27 O ARG C 53
SHEET 5 C 8 VAL C 93 PHE C 98 1 O VAL C 96 N VAL C 28
SHEET 6 C 8 ILE C 117 ALA C 123 1 O ALA C 123 N GLY C 97
SHEET 7 C 8 THR C 221 GLY C 226 1 O LEU C 222 N PHE C 122
SHEET 8 C 8 LYS C 249 ILE C 253 1 O ALA C 251 N ILE C 223
LINK C SER A 99 N MSE A 100 1555 1555 1.35
LINK C MSE A 100 N GLY A 101 1555 1555 1.34
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ALA B 2 1555 1555 1.33
LINK C SER B 99 N MSE B 100 1555 1555 1.34
LINK C MSE B 100 N GLY B 101 1555 1555 1.33
LINK C SER C 99 N MSE C 100 1555 1555 1.33
LINK C MSE C 100 N GLY C 101 1555 1555 1.32
LINK O ILE A 117 NA NA A 405 1555 1555 2.42
LINK NA NA A 404 O HOH A 328 1555 1555 2.06
LINK NA NA A 404 O HOH C 308 1555 1555 2.14
LINK NA NA A 404 O HOH A 281 1555 1555 2.09
LINK NA NA A 404 O HOH B 365 1555 1555 2.24
LINK NA NA A 404 O HOH C 289 1555 1555 2.13
LINK NA NA A 404 O HOH A 284 1555 1555 2.13
LINK NA NA A 405 O HOH A 682 1555 1555 2.05
LINK NA NA A 405 O HOH A 603 1555 1555 2.14
LINK NA NA A 405 O HOH A 706 1555 1555 2.20
LINK NA NA A 405 O HOH A 531 1555 1555 2.43
LINK NA NA A 405 O HOH A 424 1555 1555 2.46
CISPEP 1 TRP A 33 PRO A 34 0 -13.26
CISPEP 2 PRO A 127 PRO A 128 0 7.22
CISPEP 3 TRP B 33 PRO B 34 0 -11.69
CISPEP 4 PRO B 127 PRO B 128 0 6.90
CISPEP 5 TRP C 33 PRO C 34 0 -8.52
CISPEP 6 PRO C 127 PRO C 128 0 5.72
SITE 1 AC1 4 TRP A 33 SER A 99 MSE A 100 HOH A 326
SITE 1 AC2 6 HOH A 281 HOH A 284 HOH A 328 HOH B 365
SITE 2 AC2 6 HOH C 289 HOH C 308
SITE 1 AC3 7 ILE A 117 GLU A 118 HOH A 424 HOH A 531
SITE 2 AC3 7 HOH A 603 HOH A 682 HOH A 706
SITE 1 AC4 3 TRP B 33 SER B 99 MSE B 100
SITE 1 AC5 4 TRP C 33 SER C 99 MSE C 100 HOH C 343
CRYST1 77.037 48.326 101.932 90.00 94.05 90.00 P 1 21 1 6
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 0.012981 0.000000 0.000919 0.00000
SCALE2 0.000000 0.020693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009835 0.00000
TER 2220 ASP A 278
TER 4437 ASP B 278
TER 6689 ASP C 278
MASTER 439 0 9 36 24 0 7 6 7419 3 56 66
END |