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HEADER UNKNOWN FUNCTION 01-DEC-15 5F2H
TITLE 2.75 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF UNCHARACTERIZED PROTEIN
TITLE 2 FROM BACILLUS CEREUS ATCC 10987
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 222523;
SOURCE 4 STRAIN: ATCC 10987 / NRS 248;
SOURCE 5 GENE: BCE_2095;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3) MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS BACILLUS CEREUS ATCC 10987, PSI-BIOLOGY, HUMAN MICROBIOME,
KEYWDS 2 METAGENOMICS DEGRADOME REPRESENTATIVES, STRUCTURAL GENOMICS, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,O.KIRYUKHINA,
AUTHOR 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 16-DEC-15 5F2H 0
JRNL AUTH A.S.HALAVATY,E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,O.KIRYUKHINA,
JRNL AUTH 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL 2.75 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF
JRNL TITL 2 UNCHARACTERIZED PROTEIN FROM BACILLUS CEREUS ATCC 10987
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 15767
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 836
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1103
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5027
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.46000
REMARK 3 B22 (A**2) : 2.73000
REMARK 3 B33 (A**2) : -13.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.32000
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): 0.463
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.391
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.683
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5163 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4825 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6963 ; 1.511 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11166 ; 0.920 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 609 ; 1.267 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;19.412 ;25.839
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 899 ; 7.281 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ; 9.129 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 733 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5805 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1161 ; 0.004 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 5 310 B 5 310 17533 0.12 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 5 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8328 5.2199 95.5826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1025 T22: 0.2973
REMARK 3 T33: 0.5618 T12: -0.0347
REMARK 3 T13: 0.0805 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.6529 L22: 1.2925
REMARK 3 L33: 5.4879 L12: -0.7295
REMARK 3 L13: 0.8208 L23: 0.1349
REMARK 3 S TENSOR
REMARK 3 S11: -0.1773 S12: -0.3361 S13: -0.0304
REMARK 3 S21: 0.2344 S22: 0.2543 S23: 0.1514
REMARK 3 S31: 0.3966 S32: -0.4609 S33: -0.0771
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 : A 128 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6689 11.7385 34.9408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0799 T22: 0.1621
REMARK 3 T33: 0.4898 T12: 0.0741
REMARK 3 T13: 0.0742 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.3216 L22: 4.3567
REMARK 3 L33: 8.3153 L12: 0.2752
REMARK 3 L13: -1.7903 L23: 1.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.2038 S12: -0.1596 S13: 0.2992
REMARK 3 S21: 0.4022 S22: 0.3809 S23: 0.1343
REMARK 3 S31: -0.3250 S32: -0.0984 S33: -0.5846
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 : B 5 B 127
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3103 2.3222 11.4338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0756 T22: 0.2346
REMARK 3 T33: 0.4669 T12: 0.0044
REMARK 3 T13: 0.0496 T23: -0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 1.0472 L22: 1.2237
REMARK 3 L33: 6.9520 L12: 0.4185
REMARK 3 L13: -0.5762 L23: 1.2612
REMARK 3 S TENSOR
REMARK 3 S11: -0.0802 S12: 0.2441 S13: 0.1475
REMARK 3 S21: -0.1193 S22: 0.4699 S23: -0.2639
REMARK 3 S31: 0.4490 S32: 0.8527 S33: -0.3897
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 128 B 312
REMARK 3 ORIGIN FOR THE GROUP (A): 64.2681 15.0727 70.4624
REMARK 3 T TENSOR
REMARK 3 T11: 0.0463 T22: 0.3348
REMARK 3 T33: 0.5317 T12: -0.0866
REMARK 3 T13: 0.0391 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 2.6250 L22: 3.8717
REMARK 3 L33: 5.1938 L12: -0.1761
REMARK 3 L13: -0.7564 L23: -0.3200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: 0.3759 S13: 0.2362
REMARK 3 S21: -0.2658 S22: 0.0756 S23: -0.2829
REMARK 3 S31: -0.2150 S32: 0.1709 S33: -0.0690
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 5F2H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16616
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.63400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (SEMET): 8.9 MG/ML IN 10 MM
REMARK 280 TRIS-HCL PH 8.3 0.25 M NACL, 5 MM BME CRYSTALLIZATION: THE
REMARK 280 CLASSICS II D7(43): 0.1 M BIS-TRIS PH 6.5, 25% (W/V) PEG3350
REMARK 280 CRYO: CRYSTALLIZATION CONDITION SOAK, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
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 21.08800
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 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: 6120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 LYS A 124
REMARK 465 LYS A 125
REMARK 465 LYS A 311
REMARK 465 SER A 312
REMARK 465 ASN A 313
REMARK 465 LYS A 314
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 ASN B 313
REMARK 465 LYS B 314
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 LEU A 241 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 GLU B 309 CB - CA - C ANGL. DEV. = -13.1 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 LYS A 21 -167.56 -108.85
REMARK 500 ASN A 40 100.11 -19.45
REMARK 500 GLU A 127 87.79 70.90
REMARK 500 GLU A 138 -159.75 -122.56
REMARK 500 ASN A 139 -167.89 -172.43
REMARK 500 SER A 149 7.45 -66.70
REMARK 500 ASP A 169 16.55 59.84
REMARK 500 HIS A 194 -22.68 -150.93
REMARK 500 SER A 205 -131.74 51.52
REMARK 500 ASN A 249 73.76 57.34
REMARK 500 GLU A 265 -74.60 -60.87
REMARK 500 ASN A 288 -13.10 64.56
REMARK 500 LYS A 290 -146.51 -96.48
REMARK 500 ASP A 296 40.06 -109.63
REMARK 500 LYS B 21 -167.01 -108.67
REMARK 500 LYS B 125 89.86 64.32
REMARK 500 LYS B 126 84.02 -67.88
REMARK 500 GLU B 138 -162.05 -122.39
REMARK 500 ASN B 139 -170.96 -170.10
REMARK 500 SER B 149 6.59 -67.14
REMARK 500 HIS B 194 -73.00 -157.23
REMARK 500 ARG B 195 70.23 73.31
REMARK 500 GLU B 197 -91.23 -87.72
REMARK 500 SER B 205 -131.52 51.59
REMARK 500 ASN B 249 75.55 51.53
REMARK 500 ASP B 258 5.82 -69.74
REMARK 500 ASN B 288 -13.50 64.69
REMARK 500 LYS B 290 -146.26 -96.83
REMARK 500 ASP B 296 40.28 -109.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC113072 RELATED DB: TARGETTRACK
DBREF 5F2H A 1 314 UNP Q739P5 Q739P5_BACC1 1 314
DBREF 5F2H B 1 314 UNP Q739P5 Q739P5_BACC1 1 314
SEQADV 5F2H SER A -2 UNP Q739P5 EXPRESSION TAG
SEQADV 5F2H ASN A -1 UNP Q739P5 EXPRESSION TAG
SEQADV 5F2H ALA A 0 UNP Q739P5 EXPRESSION TAG
SEQADV 5F2H SER B -2 UNP Q739P5 EXPRESSION TAG
SEQADV 5F2H ASN B -1 UNP Q739P5 EXPRESSION TAG
SEQADV 5F2H ALA B 0 UNP Q739P5 EXPRESSION TAG
SEQRES 1 A 317 SER ASN ALA MSE LYS ASN SER MSE THR TYR ILE GLN LEU
SEQRES 2 A 317 LEU ASN GLU THR LEU HIS CYS TYR ALA SER LYS GLY SER
SEQRES 3 A 317 LEU GLU ALA TYR THR TYR ILE MSE GLU HIS ALA LYS GLY
SEQRES 4 A 317 ILE VAL GLY ASN GLU ALA GLN ILE TYR ASN PHE LYS TYR
SEQRES 5 A 317 ALA LEU ALA SER ALA ALA GLY LEU GLU GLU GLU ALA MSE
SEQRES 6 A 317 HIS VAL MSE LYS GLU ALA ILE ILE GLU LYS GLY PHE TRP
SEQRES 7 A 317 TYR GLY ASN GLU TYR LEU ILE SER ASP ASP ASP LEU LYS
SEQRES 8 A 317 PRO LEU HIS LYS PHE GLU GLU PHE HIS GLN MSE VAL GLN
SEQRES 9 A 317 LEU CYS LYS GLU ARG GLU GLU LEU ALA LYS LYS THR GLU
SEQRES 10 A 317 ARG ALA ASP VAL LYS TYR ILE ASP SER LYS LYS LYS GLU
SEQRES 11 A 317 LYS LEU PHE ILE ALA MSE HIS GLY ASP GLN GLU ASN ILE
SEQRES 12 A 317 ALA ILE VAL GLU PRO TYR TRP LYS SER VAL LEU ASP GLN
SEQRES 13 A 317 ASP TYR THR LEU ALA LEU PRO GLN SER SER GLN ILE GLN
SEQRES 14 A 317 PHE SER ASP GLY PHE VAL TRP ASP ASP ILE GLN ARG GLY
SEQRES 15 A 317 LYS GLU GLU LEU LYS GLU HIS TYR VAL LYS PHE ILE GLU
SEQRES 16 A 317 ASN HIS ARG GLY GLU SER VAL ILE ILE GLY GLY PHE SER
SEQRES 17 A 317 ALA GLY ALA ARG VAL ALA LEU TYR THR ILE LEU HIS LYS
SEQRES 18 A 317 ASP ILE ASP VAL ASP GLY PHE ILE PHE MSE ALA PRO TRP
SEQRES 19 A 317 LEU PRO GLU ILE ASP GLU TRP ASN GLU LEU LEU GLU VAL
SEQRES 20 A 317 LEU GLN ASP LYS ASN ILE LYS GLY TYR VAL VAL CYS GLY
SEQRES 21 A 317 ASP GLN ASP GLU ASP CYS PHE GLU CYS THR GLN GLN PHE
SEQRES 22 A 317 VAL GLN VAL LEU LYS ASP LYS ASN ILE GLU HIS GLU PHE
SEQRES 23 A 317 LYS VAL VAL PRO ASN LEU LYS HIS ASP TYR PRO GLU ASP
SEQRES 24 A 317 PHE ASP GLU LEU LEU LYS GLU ALA ILE LYS TYR ILE GLU
SEQRES 25 A 317 ASP LYS SER ASN LYS
SEQRES 1 B 317 SER ASN ALA MSE LYS ASN SER MSE THR TYR ILE GLN LEU
SEQRES 2 B 317 LEU ASN GLU THR LEU HIS CYS TYR ALA SER LYS GLY SER
SEQRES 3 B 317 LEU GLU ALA TYR THR TYR ILE MSE GLU HIS ALA LYS GLY
SEQRES 4 B 317 ILE VAL GLY ASN GLU ALA GLN ILE TYR ASN PHE LYS TYR
SEQRES 5 B 317 ALA LEU ALA SER ALA ALA GLY LEU GLU GLU GLU ALA MSE
SEQRES 6 B 317 HIS VAL MSE LYS GLU ALA ILE ILE GLU LYS GLY PHE TRP
SEQRES 7 B 317 TYR GLY ASN GLU TYR LEU ILE SER ASP ASP ASP LEU LYS
SEQRES 8 B 317 PRO LEU HIS LYS PHE GLU GLU PHE HIS GLN MSE VAL GLN
SEQRES 9 B 317 LEU CYS LYS GLU ARG GLU GLU LEU ALA LYS LYS THR GLU
SEQRES 10 B 317 ARG ALA ASP VAL LYS TYR ILE ASP SER LYS LYS LYS GLU
SEQRES 11 B 317 LYS LEU PHE ILE ALA MSE HIS GLY ASP GLN GLU ASN ILE
SEQRES 12 B 317 ALA ILE VAL GLU PRO TYR TRP LYS SER VAL LEU ASP GLN
SEQRES 13 B 317 ASP TYR THR LEU ALA LEU PRO GLN SER SER GLN ILE GLN
SEQRES 14 B 317 PHE SER ASP GLY PHE VAL TRP ASP ASP ILE GLN ARG GLY
SEQRES 15 B 317 LYS GLU GLU LEU LYS GLU HIS TYR VAL LYS PHE ILE GLU
SEQRES 16 B 317 ASN HIS ARG GLY GLU SER VAL ILE ILE GLY GLY PHE SER
SEQRES 17 B 317 ALA GLY ALA ARG VAL ALA LEU TYR THR ILE LEU HIS LYS
SEQRES 18 B 317 ASP ILE ASP VAL ASP GLY PHE ILE PHE MSE ALA PRO TRP
SEQRES 19 B 317 LEU PRO GLU ILE ASP GLU TRP ASN GLU LEU LEU GLU VAL
SEQRES 20 B 317 LEU GLN ASP LYS ASN ILE LYS GLY TYR VAL VAL CYS GLY
SEQRES 21 B 317 ASP GLN ASP GLU ASP CYS PHE GLU CYS THR GLN GLN PHE
SEQRES 22 B 317 VAL GLN VAL LEU LYS ASP LYS ASN ILE GLU HIS GLU PHE
SEQRES 23 B 317 LYS VAL VAL PRO ASN LEU LYS HIS ASP TYR PRO GLU ASP
SEQRES 24 B 317 PHE ASP GLU LEU LEU LYS GLU ALA ILE LYS TYR ILE GLU
SEQRES 25 B 317 ASP LYS SER ASN LYS
MODRES 5F2H MSE A 5 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 31 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 62 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 65 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 99 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 133 MET MODIFIED RESIDUE
MODRES 5F2H MSE A 228 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 5 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 31 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 62 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 65 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 99 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 133 MET MODIFIED RESIDUE
MODRES 5F2H MSE B 228 MET MODIFIED RESIDUE
HET MSE A 5 8
HET MSE A 31 8
HET MSE A 62 8
HET MSE A 65 8
HET MSE A 99 8
HET MSE A 133 8
HET MSE A 228 8
HET MSE B 5 8
HET MSE B 31 8
HET MSE B 62 8
HET MSE B 65 8
HET MSE B 99 8
HET MSE B 133 8
HET MSE B 228 8
HET TRS A 401 8
HET TRS B 401 8
HET TRS B 402 8
HETNAM MSE SELENOMETHIONINE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 TRS 3(C4 H12 N O3 1+)
FORMUL 6 HOH *20(H2 O)
HELIX 1 AA1 THR A 6 LYS A 21 1 16
HELIX 2 AA2 GLY A 22 LYS A 35 1 14
HELIX 3 AA3 ASN A 40 GLY A 56 1 17
HELIX 4 AA4 LEU A 57 ILE A 70 1 14
HELIX 5 AA5 GLY A 77 ASP A 84 1 8
HELIX 6 AA6 ASP A 85 HIS A 91 5 7
HELIX 7 AA7 PHE A 93 THR A 113 1 21
HELIX 8 AA8 ASN A 139 LYS A 148 1 10
HELIX 9 AA9 SER A 149 GLN A 153 5 5
HELIX 10 AB1 ASP A 175 ASN A 193 1 19
HELIX 11 AB2 SER A 205 HIS A 217 1 13
HELIX 12 AB3 GLU A 240 LEU A 242 5 3
HELIX 13 AB4 GLU A 243 LYS A 248 1 6
HELIX 14 AB5 CYS A 263 LYS A 277 1 15
HELIX 15 AB6 ASP A 296 ASP A 310 1 15
HELIX 16 AB7 THR B 6 LYS B 21 1 16
HELIX 17 AB8 GLY B 22 LYS B 35 1 14
HELIX 18 AB9 ASN B 40 GLY B 56 1 17
HELIX 19 AC1 LEU B 57 ILE B 70 1 14
HELIX 20 AC2 GLY B 77 ASP B 84 1 8
HELIX 21 AC3 ASP B 85 HIS B 91 5 7
HELIX 22 AC4 PHE B 93 THR B 113 1 21
HELIX 23 AC5 ASN B 139 LYS B 148 1 10
HELIX 24 AC6 SER B 149 GLN B 153 5 5
HELIX 25 AC7 ASP B 175 ASN B 193 1 19
HELIX 26 AC8 SER B 205 HIS B 217 1 13
HELIX 27 AC9 GLU B 240 LEU B 242 5 3
HELIX 28 AD1 GLU B 243 LYS B 248 1 6
HELIX 29 AD2 CYS B 263 LYS B 277 1 15
HELIX 30 AD3 ASP B 296 GLU B 309 1 14
SHEET 1 AA1 7 ASP A 117 ILE A 121 0
SHEET 2 AA1 7 TYR B 155 GLN B 161 -1 O GLN B 161 N ASP A 117
SHEET 3 AA1 7 LYS B 128 MSE B 133 1 N PHE B 130 O ALA B 158
SHEET 4 AA1 7 VAL B 199 PHE B 204 1 O GLY B 202 N ILE B 131
SHEET 5 AA1 7 GLY B 224 MSE B 228 1 O MSE B 228 N GLY B 203
SHEET 6 AA1 7 LYS B 251 GLY B 257 1 O TYR B 253 N PHE B 225
SHEET 7 AA1 7 HIS B 281 VAL B 286 1 O LYS B 284 N VAL B 254
SHEET 1 AA2 7 HIS A 281 VAL A 286 0
SHEET 2 AA2 7 LYS A 251 GLY A 257 1 N VAL A 254 O LYS A 284
SHEET 3 AA2 7 GLY A 224 MSE A 228 1 N PHE A 225 O TYR A 253
SHEET 4 AA2 7 VAL A 199 PHE A 204 1 N GLY A 203 O MSE A 228
SHEET 5 AA2 7 LYS A 128 MSE A 133 1 N ILE A 131 O GLY A 202
SHEET 6 AA2 7 TYR A 155 GLN A 161 1 O ALA A 158 N PHE A 130
SHEET 7 AA2 7 ASP B 117 ILE B 121 -1 O ASP B 117 N GLN A 161
SHEET 1 AA3 2 ILE A 165 PHE A 167 0
SHEET 2 AA3 2 GLY A 170 PHE A 171 -1 O GLY A 170 N PHE A 167
SHEET 1 AA4 2 ILE B 165 PHE B 167 0
SHEET 2 AA4 2 GLY B 170 PHE B 171 -1 O GLY B 170 N PHE B 167
LINK C MSE A 5 N THR A 6 1555 1555 1.33
LINK C ILE A 30 N MSE A 31 1555 1555 1.33
LINK C MSE A 31 N GLU A 32 1555 1555 1.33
LINK C ALA A 61 N MSE A 62 1555 1555 1.33
LINK C MSE A 62 N HIS A 63 1555 1555 1.34
LINK C VAL A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N LYS A 66 1555 1555 1.33
LINK C GLN A 98 N MSE A 99 1555 1555 1.33
LINK C MSE A 99 N VAL A 100 1555 1555 1.33
LINK C ALA A 132 N MSE A 133 1555 1555 1.34
LINK C MSE A 133 N HIS A 134 1555 1555 1.33
LINK C PHE A 227 N MSE A 228 1555 1555 1.33
LINK C MSE A 228 N ALA A 229 1555 1555 1.32
LINK C MSE B 5 N THR B 6 1555 1555 1.34
LINK C ILE B 30 N MSE B 31 1555 1555 1.34
LINK C MSE B 31 N GLU B 32 1555 1555 1.34
LINK C ALA B 61 N MSE B 62 1555 1555 1.33
LINK C MSE B 62 N HIS B 63 1555 1555 1.34
LINK C VAL B 64 N MSE B 65 1555 1555 1.33
LINK C MSE B 65 N LYS B 66 1555 1555 1.33
LINK C GLN B 98 N MSE B 99 1555 1555 1.33
LINK C MSE B 99 N VAL B 100 1555 1555 1.33
LINK C ALA B 132 N MSE B 133 1555 1555 1.34
LINK C MSE B 133 N HIS B 134 1555 1555 1.32
LINK C PHE B 227 N MSE B 228 1555 1555 1.33
LINK C MSE B 228 N ALA B 229 1555 1555 1.33
SITE 1 AC1 4 ASP A 136 TRP A 231 ASP A 262 CYS A 263
SITE 1 AC2 2 TRP B 231 ASP B 262
SITE 1 AC3 3 ASN B 46 TYR B 80 ASP B 84
CRYST1 71.067 42.176 106.032 90.00 92.45 90.00 P 1 21 1 4
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 0.014071 0.000000 0.000601 0.00000
SCALE2 0.000000 0.023710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009440 0.00000
TER 2498 ASP A 310
TER 5029 SER B 312
MASTER 419 0 17 30 18 0 3 6 5071 2 162 50
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