HEADER UNKNOWN FUNCTION 15-JUL-14 4QVS
TITLE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF S-LAYER DOMAIN-CONTAINING
TITLE 2 PROTEIN (RESIDUES 221-444) FROM CLOSTRIDIUM THERMOCELLUM ATCC 27405
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-LAYER DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 221-444;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RUMINICLOSTRIDIUM THERMOCELLUM ATCC 27405;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 STRAIN: ATCC 27405 / DSM 1237;
SOURCE 5 GENE: CTHE_2506;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS HUMAN MICROBIOME, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, PSI-
KEYWDS 2 BIOLOGY, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,Z.WAWRZAK,E.V.FILIPPOVA,G.MINASOV,O.KIRYUKHINA,
AUTHOR 2 L.SHUVALOVA,R.JEDRZEJCZAK,A.JOACHIMIAK,W.F.ANDERSON,MIDWEST CENTER
AUTHOR 3 FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 2 22-NOV-17 4QVS 1 REMARK
REVDAT 1 30-JUL-14 4QVS 0
JRNL AUTH A.S.HALAVATY,Z.WAWRZAK,E.V.FILIPPOVA,G.MINASOV,O.KIRYUKHINA,
JRNL AUTH 2 L.SHUVALOVA,R.JEDRZEJCZAK,A.JOACHIMIAK,W.F.ANDERSON
JRNL TITL 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF S-LAYER
JRNL TITL 2 DOMAIN-CONTAINING PROTEIN (RESIDUES 221-444) FROM
JRNL TITL 3 CLOSTRIDIUM THERMOCELLUM ATCC 27405
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 13697
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 721
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 968
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1673
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.60000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : 6.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1725 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1525 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2340 ; 1.814 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3518 ; 0.833 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 217 ; 4.326 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;30.246 ;25.119
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 251 ;10.693 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;14.100 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 250 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2015 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 413 ; 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): 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 221 A 285
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9955 22.9051 81.8999
REMARK 3 T TENSOR
REMARK 3 T11: 0.3095 T22: 0.1329
REMARK 3 T33: 0.0229 T12: -0.0069
REMARK 3 T13: 0.0194 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.8644 L22: 1.3275
REMARK 3 L33: 1.0777 L12: 0.4747
REMARK 3 L13: 0.4266 L23: -0.8905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: -0.2951 S13: 0.1972
REMARK 3 S21: 0.2173 S22: -0.1149 S23: 0.0245
REMARK 3 S31: -0.2017 S32: -0.0384 S33: 0.0684
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 286 A 345
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2886 5.7955 82.4876
REMARK 3 T TENSOR
REMARK 3 T11: 0.2992 T22: 0.1571
REMARK 3 T33: 0.0655 T12: 0.0068
REMARK 3 T13: -0.0227 T23: 0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 2.0203 L22: 2.4097
REMARK 3 L33: 1.1234 L12: 0.0013
REMARK 3 L13: -0.0972 L23: 0.2707
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: -0.1943 S13: -0.3079
REMARK 3 S21: 0.1350 S22: -0.0215 S23: -0.2011
REMARK 3 S31: 0.1067 S32: 0.0404 S33: 0.0071
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 : A 346 A 389
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8405 -8.4474 107.7386
REMARK 3 T TENSOR
REMARK 3 T11: 0.3161 T22: 0.2027
REMARK 3 T33: 0.0994 T12: -0.0106
REMARK 3 T13: 0.1073 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 4.8550 L22: 1.7001
REMARK 3 L33: 2.9475 L12: -1.1403
REMARK 3 L13: 2.7436 L23: -0.5518
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.3654 S13: 0.1665
REMARK 3 S21: -0.4554 S22: 0.0424 S23: -0.3695
REMARK 3 S31: -0.2866 S32: -0.1293 S33: -0.0496
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 : A 390 A 438
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8677 -12.2684 113.5942
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.1647
REMARK 3 T33: 0.0312 T12: 0.0098
REMARK 3 T13: 0.0113 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.8757 L22: 2.4651
REMARK 3 L33: 0.7886 L12: -0.2453
REMARK 3 L13: -0.5487 L23: 0.2837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.2066 S13: 0.1318
REMARK 3 S21: -0.1182 S22: -0.0640 S23: -0.0115
REMARK 3 S31: 0.0798 S32: -0.0438 S33: 0.0787
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2, MOSFLM
REMARK 200 DATA SCALING SOFTWARE : POINTLESS, AIMLESS, XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14480
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 9.35 MG/ML IN 10 MM TRIS-HCL
REMARK 280 PH 8.3, 500 MM NACL, 5 MM BME, CRYSTALLIZATION: THE PEGS II
REMARK 280 SUITE G11 (83): 0.5 M LITHIUM CHLORIDE, 0.1 M TRIS PH 8.5. 28%
REMARK 280 (W/V) PEG 6000, CYO: WELL SOLUTION, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.19900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.19900
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.97900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.40650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.97900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.40650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.19900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.97900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.40650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.19900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.97900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 37.40650
REMARK 290 SMTRY3 8 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: 16780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 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 196.79600
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 603 LIES ON A SPECIAL POSITION.
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 218
REMARK 465 ASN A 219
REMARK 465 ALA A 220
REMARK 465 ARG A 383
REMARK 465 VAL A 439
REMARK 465 ALA A 440
REMARK 465 THR A 441
REMARK 465 ARG A 442
REMARK 465 VAL A 443
REMARK 465 ASN A 444
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 MSE A 317 CG - SE - CE ANGL. DEV. = -15.2 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 237 15.64 -141.24
REMARK 500 ASP A 272 12.43 -149.32
REMARK 500 ALA A 437 5.28 -68.16
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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 644 O
REMARK 620 2 ASN A 264 O 169.5
REMARK 620 3 MSE A 227 O 88.6 98.3
REMARK 620 4 ASN A 262 O 76.8 93.2 145.6
REMARK 620 5 ASP A 229 OD1 95.6 78.1 78.3 72.5
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 CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC113088 RELATED DB: TARGETTRACK
DBREF 4QVS A 221 444 UNP A3DIC9 A3DIC9_CLOTH 221 444
SEQADV 4QVS SER A 218 UNP A3DIC9 EXPRESSION TAG
SEQADV 4QVS ASN A 219 UNP A3DIC9 EXPRESSION TAG
SEQADV 4QVS ALA A 220 UNP A3DIC9 EXPRESSION TAG
SEQRES 1 A 227 SER ASN ALA GLU THR GLY ALA TRP TYR MSE PHE ASP GLU
SEQRES 2 A 227 ALA VAL GLU GLY SER THR ASN GLU PHE LYS ASP TYR LYS
SEQRES 3 A 227 GLY ASN HIS GLY ASN ALA VAL LEU TYR SER ALA ASN GLY
SEQRES 4 A 227 VAL VAL PRO GLY LEU ASN GLY ASN SER VAL SER LEU ASP
SEQRES 5 A 227 GLY VAL ASP ASP TYR VAL ALA LEU PRO ASP GLY ILE ALA
SEQRES 6 A 227 GLY THR PHE TYR ASN PHE THR ILE ALA PHE TRP VAL ARG
SEQRES 7 A 227 LEU ASP THR ILE GLY GLU GLN PRO ILE PHE ASP PHE PHE
SEQRES 8 A 227 ASP SER GLY SER ASN ASN LYS TYR MSE ARG LEU THR ALA
SEQRES 9 A 227 GLU SER ASP GLY LYS ILE LYS PHE ALA MSE THR GLN SER
SEQRES 10 A 227 GLY TYR TYR GLY GLU LYS THR ILE THR SER GLY SER ALA
SEQRES 11 A 227 LEU THR GLU GLY VAL TRP LYS HIS VAL ALA VAL THR LEU
SEQRES 12 A 227 SER GLY ASP THR GLY THR LEU TYR ILE ASN GLY GLU ASN
SEQRES 13 A 227 VAL GLY GLU ASN ASN THR LEU SER LEU ARG PRO LEU THR
SEQRES 14 A 227 PHE LEU GLY GLU THR SER LYS GLY TYR ILE GLY LYS SER
SEQRES 15 A 227 HIS GLN THR ASP SER SER GLU ASP PRO TYR TYR ASN SER
SEQRES 16 A 227 TYR LEU HIS GLY MSE ILE ASP ASP PHE ARG ILE PHE ASP
SEQRES 17 A 227 ARG ALA LEU SER ALA ASP GLU ILE LYS THR LEU ALA SER
SEQRES 18 A 227 VAL ALA THR ARG VAL ASN
MODRES 4QVS MSE A 227 MET SELENOMETHIONINE
MODRES 4QVS MSE A 317 MET SELENOMETHIONINE
MODRES 4QVS MSE A 331 MET SELENOMETHIONINE
MODRES 4QVS MSE A 417 MET SELENOMETHIONINE
HET MSE A 227 8
HET MSE A 317 8
HET MSE A 331 8
HET MSE A 417 8
HET CL A 501 1
HET NA A 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 CL CL 1-
FORMUL 3 NA NA 1+
FORMUL 4 HOH *44(H2 O)
HELIX 1 1 GLY A 335 GLU A 339 5 5
HELIX 2 2 LEU A 388 SER A 392 5 5
HELIX 3 3 SER A 429 ALA A 437 1 9
SHEET 1 A 3 GLU A 238 PHE A 239 0
SHEET 2 A 3 ALA A 249 TYR A 252 -1 O ALA A 249 N PHE A 239
SHEET 3 A 3 TYR A 274 ALA A 276 -1 O ALA A 276 N VAL A 250
SHEET 1 B 2 VAL A 257 PRO A 259 0
SHEET 2 B 2 ASN A 264 VAL A 266 -1 O SER A 265 N VAL A 258
SHEET 1 C 4 GLN A 302 PHE A 308 0
SHEET 2 C 4 TYR A 316 ALA A 321 -1 O LEU A 319 N ILE A 304
SHEET 3 C 4 ILE A 327 THR A 332 -1 O LYS A 328 N THR A 320
SHEET 4 C 4 LYS A 340 THR A 343 -1 O LYS A 340 N MSE A 331
SHEET 1 D 3 VAL A 356 SER A 361 0
SHEET 2 D 3 THR A 364 ILE A 369 -1 O THR A 364 N SER A 361
SHEET 3 D 3 GLU A 372 ASN A 377 -1 O VAL A 374 N LEU A 367
LINK C TYR A 226 N MSE A 227 1555 1555 1.33
LINK C MSE A 227 N PHE A 228 1555 1555 1.34
LINK C TYR A 316 N MSE A 317 1555 1555 1.34
LINK C MSE A 317 N ARG A 318 1555 1555 1.33
LINK C ALA A 330 N MSE A 331 1555 1555 1.33
LINK C MSE A 331 N THR A 332 1555 1555 1.34
LINK C GLY A 416 N MSE A 417 1555 1555 1.34
LINK C MSE A 417 N ILE A 418 1555 1555 1.34
LINK NA NA A 502 O HOH A 644 1555 1555 2.02
LINK O ASN A 264 NA NA A 502 1555 1555 2.15
LINK O MSE A 227 NA NA A 502 1555 1555 2.30
LINK O ASN A 262 NA NA A 502 1555 1555 2.38
LINK OD1 ASP A 229 NA NA A 502 1555 1555 2.50
CISPEP 1 THR A 386 PHE A 387 0 -1.77
SITE 1 AC1 3 ASP A 229 GLU A 230 TYR A 242
SITE 1 AC2 6 MSE A 227 ASP A 229 ASN A 262 ASN A 264
SITE 2 AC2 6 ASP A 419 HOH A 644
CRYST1 65.958 74.813 98.398 90.00 90.00 90.00 C 2 2 21 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 0.015161 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
