HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 31-MAR-05 1Z94
TITLE X-RAY CRYSTAL STRUCTURE OF PROTEIN CV1439 FROM CHROMOBACTERIUM
TITLE 2 VIOLACEUM. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET CVR12.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHROMOBACTERIUM VIOLACEUM;
SOURCE 3 ORGANISM_TAXID: 243365;
SOURCE 4 STRAIN: ATCC 12472;
SOURCE 5 GENE: CV1439;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21
KEYWDS HYPOTHETICAL PROTEIN, NESG, CV1439, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUZIN,S.M.VOROBIEV,W.YONG,F.FOROUHAR,R.XIO,L.-C.MA,T.ACTON,
AUTHOR 2 G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (NESG)
REVDAT 3 13-JUL-11 1Z94 1 VERSN
REVDAT 2 24-FEB-09 1Z94 1 VERSN
REVDAT 1 10-MAY-05 1Z94 0
JRNL AUTH A.KUZIN,S.M.VOROBIEV,W.YONG,F.FOROUHAR,R.XIO,L.-C.MA,
JRNL AUTH 2 T.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT
JRNL TITL CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN CV1439 FROM
JRNL TITL 2 CHROMOBACTERIUM VIOLACEUM. NORTHEAST STRUCTURAL GENOMICS
JRNL TITL 3 CONSORTIUM TARGET CVR12.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 322286.600
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 121816
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 SET) : 0.245
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 11979
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16699
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1776
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6623
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 408
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.60000
REMARK 3 B22 (A**2) : 1.32000
REMARK 3 B33 (A**2) : 5.28000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.92
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 55.47
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129114
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M SODIUM CHLORIDE, 0.1 M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 64.06300
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 64.06300
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 52.54750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.12350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.54750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.12350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.06300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.54750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 85.12350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.06300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.54750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 85.12350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 105.09500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 192.18900
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 1
REMARK 465 GLY A 90
REMARK 465 LEU A 91
REMARK 465 PRO A 92
REMARK 465 MET A 145
REMARK 465 PRO A 146
REMARK 465 GLY A 147
REMARK 465 MET B 145
REMARK 465 PRO B 146
REMARK 465 GLY B 147
REMARK 465 MSE C 1
REMARK 465 MET C 145
REMARK 465 PRO C 146
REMARK 465 GLY C 147
REMARK 465 MSE D 1
REMARK 465 MET D 145
REMARK 465 PRO D 146
REMARK 465 GLY D 147
REMARK 465 MSE E 1
REMARK 465 ASP E 88
REMARK 465 ALA E 89
REMARK 465 GLY E 90
REMARK 465 LEU E 91
REMARK 465 PRO E 92
REMARK 465 MET E 145
REMARK 465 PRO E 146
REMARK 465 GLY E 147
REMARK 465 MSE F 1
REMARK 465 MET F 145
REMARK 465 PRO F 146
REMARK 465 GLY F 147
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 ASP F 88 N - CA - C ANGL. DEV. = 22.5 DEGREES
REMARK 500 GLY F 90 N - CA - C ANGL. DEV. = -21.8 DEGREES
REMARK 500 LEU F 91 N - CA - CB ANGL. DEV. = -22.3 DEGREES
REMARK 500 LEU F 91 N - CA - C ANGL. DEV. = 33.7 DEGREES
REMARK 500 PRO F 92 N - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 PRO F 92 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLY F 93 N - CA - C ANGL. DEV. = 15.9 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 SER A 12 59.02 -90.19
REMARK 500 HIS A 44 55.99 -151.44
REMARK 500 GLU A 78 -40.85 -136.35
REMARK 500 ASP A 87 45.35 -80.34
REMARK 500 ASN B 3 20.90 47.59
REMARK 500 HIS B 44 75.63 -151.49
REMARK 500 PRO B 76 119.49 -37.75
REMARK 500 GLU B 78 -51.35 -129.46
REMARK 500 HIS C 44 55.51 -145.38
REMARK 500 PRO C 76 120.88 -37.37
REMARK 500 GLU C 78 -38.51 -141.02
REMARK 500 LEU C 91 54.49 -142.06
REMARK 500 PRO D 76 124.50 -37.05
REMARK 500 GLU D 78 -38.67 -139.48
REMARK 500 PRO E 34 178.67 -58.40
REMARK 500 HIS E 44 64.24 -150.65
REMARK 500 PRO E 76 123.39 -38.61
REMARK 500 GLU E 78 -43.70 -138.52
REMARK 500 PRO F 34 -178.44 -66.23
REMARK 500 HIS F 44 62.64 -151.28
REMARK 500 PRO F 76 112.76 -36.82
REMARK 500 GLU F 78 -42.84 -138.44
REMARK 500 ASP F 87 17.05 -141.64
REMARK 500 ASP F 88 -88.31 -119.03
REMARK 500 LEU F 91 -93.13 -103.03
REMARK 500 PRO F 92 115.51 -9.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY F 90 -12.63
REMARK 500 LEU F 91 11.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP F 87 23.1 L L OUTSIDE RANGE
REMARK 500 ASP F 88 22.8 L L OUTSIDE RANGE
REMARK 500 LEU F 91 19.4 L L OUTSIDE RANGE
REMARK 500 PRO F 92 21.4 L L OUTSIDE RANGE
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 A 148 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 232 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 237 DISTANCE = 17.48 ANGSTROMS
REMARK 525 HOH C 207 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 215 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH C 218 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH E 204 DISTANCE = 10.86 ANGSTROMS
REMARK 525 HOH E 205 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH F 207 DISTANCE = 9.08 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CVR12 RELATED DB: TARGETDB
DBREF 1Z94 A 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
DBREF 1Z94 B 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
DBREF 1Z94 C 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
DBREF 1Z94 D 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
DBREF 1Z94 E 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
DBREF 1Z94 F 1 147 UNP Q7NY36 Q7NY36_CHRVO 1 147
SEQADV 1Z94 MSE A 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE A 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE A 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQADV 1Z94 MSE B 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE B 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE B 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQADV 1Z94 MSE C 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE C 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE C 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQADV 1Z94 MSE D 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE D 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE D 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQADV 1Z94 MSE E 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE E 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE E 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQADV 1Z94 MSE F 1 UNP Q7NY36 MET 1 MODIFIED RESIDUE
SEQADV 1Z94 MSE F 54 UNP Q7NY36 MET 54 MODIFIED RESIDUE
SEQADV 1Z94 MSE F 95 UNP Q7NY36 MET 95 MODIFIED RESIDUE
SEQRES 1 A 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 A 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 A 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 A 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 A 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 A 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 A 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 A 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 A 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 A 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 A 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 A 147 ASP MET PRO GLY
SEQRES 1 B 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 B 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 B 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 B 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 B 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 B 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 B 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 B 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 B 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 B 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 B 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 B 147 ASP MET PRO GLY
SEQRES 1 C 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 C 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 C 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 C 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 C 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 C 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 C 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 C 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 C 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 C 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 C 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 C 147 ASP MET PRO GLY
SEQRES 1 D 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 D 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 D 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 D 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 D 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 D 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 D 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 D 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 D 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 D 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 D 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 D 147 ASP MET PRO GLY
SEQRES 1 E 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 E 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 E 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 E 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 E 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 E 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 E 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 E 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 E 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 E 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 E 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 E 147 ASP MET PRO GLY
SEQRES 1 F 147 MSE PRO ASN THR ILE ARG LEU HIS ARG VAL LEU SER ALA
SEQRES 2 F 147 PRO PRO GLU ARG VAL TYR ARG ALA PHE LEU ASP PRO LEU
SEQRES 3 F 147 ALA LEU ALA LYS TRP LEU PRO PRO GLU GLY PHE VAL CYS
SEQRES 4 F 147 LYS VAL LEU GLU HIS ASP ALA ARG VAL GLY GLY ALA TYR
SEQRES 5 F 147 LYS MSE GLU PHE LEU ALA PHE ALA SER GLY GLN LYS HIS
SEQRES 6 F 147 ALA PHE GLY GLY ARG TYR LEU GLU LEU VAL PRO GLY GLU
SEQRES 7 F 147 ARG ILE ARG TYR THR ASP ARG PHE ASP ASP ALA GLY LEU
SEQRES 8 F 147 PRO GLY ASP MSE ILE THR THR ILE THR LEU ALA PRO LEU
SEQRES 9 F 147 SER CYS GLY ALA ASP LEU SER ILE VAL GLN GLU GLY ILE
SEQRES 10 F 147 PRO ASP ALA ILE PRO PRO GLU ASN CYS TYR LEU GLY TRP
SEQRES 11 F 147 GLN GLN SER LEU LYS GLN LEU ALA ALA LEU VAL GLU PRO
SEQRES 12 F 147 ASP MET PRO GLY
MODRES 1Z94 MSE A 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE A 95 MET SELENOMETHIONINE
MODRES 1Z94 MSE B 1 MET SELENOMETHIONINE
MODRES 1Z94 MSE B 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE B 95 MET SELENOMETHIONINE
MODRES 1Z94 MSE C 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE C 95 MET SELENOMETHIONINE
MODRES 1Z94 MSE D 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE D 95 MET SELENOMETHIONINE
MODRES 1Z94 MSE E 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE E 95 MET SELENOMETHIONINE
MODRES 1Z94 MSE F 54 MET SELENOMETHIONINE
MODRES 1Z94 MSE F 95 MET SELENOMETHIONINE
HET MSE A 54 8
HET MSE A 95 8
HET MSE B 1 8
HET MSE B 54 8
HET MSE B 95 8
HET MSE C 54 8
HET MSE C 95 8
HET MSE D 54 8
HET MSE D 95 8
HET MSE E 54 8
HET MSE E 95 8
HET MSE F 54 8
HET MSE F 95 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 13(C5 H11 N O2 SE)
FORMUL 7 HOH *408(H2 O)
HELIX 1 1 PRO A 14 PHE A 22 1 9
HELIX 2 2 ASP A 24 LEU A 32 1 9
HELIX 3 3 PRO A 122 GLU A 142 1 21
HELIX 4 4 PRO B 14 ASP B 24 1 11
HELIX 5 5 ASP B 24 LEU B 32 1 9
HELIX 6 6 PRO B 122 GLU B 142 1 21
HELIX 7 7 PRO C 14 ASP C 24 1 11
HELIX 8 8 ASP C 24 LEU C 32 1 9
HELIX 9 9 PRO C 122 GLU C 142 1 21
HELIX 10 10 PRO D 14 PHE D 22 1 9
HELIX 11 11 ASP D 24 LEU D 32 1 9
HELIX 12 12 PRO D 122 GLU D 142 1 21
HELIX 13 13 PRO E 14 ASP E 24 1 11
HELIX 14 14 ASP E 24 LEU E 32 1 9
HELIX 15 15 PRO E 122 GLU E 142 1 21
HELIX 16 16 PRO F 14 ASP F 24 1 11
HELIX 17 17 ASP F 24 LEU F 32 1 9
HELIX 18 18 PRO F 122 GLU F 142 1 21
SHEET 1 A 7 ILE A 5 LEU A 11 0
SHEET 2 A 7 GLY A 107 GLU A 115 -1 O LEU A 110 N ARG A 9
SHEET 3 A 7 MSE A 95 LEU A 104 -1 N ILE A 96 O GLU A 115
SHEET 4 A 7 ARG A 79 PHE A 86 -1 N ILE A 80 O ILE A 99
SHEET 5 A 7 LYS A 64 VAL A 75 -1 N VAL A 75 O ARG A 79
SHEET 6 A 7 ALA A 51 ALA A 58 -1 N MSE A 54 O PHE A 67
SHEET 7 A 7 PHE A 37 HIS A 44 -1 N GLU A 43 O LYS A 53
SHEET 1 B 7 THR B 4 LEU B 11 0
SHEET 2 B 7 ALA B 108 GLU B 115 -1 O ILE B 112 N LEU B 7
SHEET 3 B 7 MSE B 95 PRO B 103 -1 N ILE B 96 O GLU B 115
SHEET 4 B 7 ARG B 79 PHE B 86 -1 N ILE B 80 O ILE B 99
SHEET 5 B 7 LYS B 64 VAL B 75 -1 N LEU B 72 O ARG B 81
SHEET 6 B 7 ALA B 51 ALA B 58 -1 N PHE B 56 O HIS B 65
SHEET 7 B 7 PHE B 37 HIS B 44 -1 N VAL B 38 O LEU B 57
SHEET 1 C 7 ASN C 3 LEU C 11 0
SHEET 2 C 7 GLY C 107 ILE C 117 -1 O ALA C 108 N LEU C 11
SHEET 3 C 7 MSE C 95 LEU C 104 -1 N ILE C 96 O GLU C 115
SHEET 4 C 7 ARG C 79 PHE C 86 -1 N ILE C 80 O ILE C 99
SHEET 5 C 7 LYS C 64 VAL C 75 -1 N LEU C 72 O ARG C 81
SHEET 6 C 7 ALA C 51 ALA C 58 -1 N TYR C 52 O GLY C 69
SHEET 7 C 7 PHE C 37 HIS C 44 -1 N GLU C 43 O LYS C 53
SHEET 1 D 7 ASN D 3 LEU D 11 0
SHEET 2 D 7 GLY D 107 ILE D 117 -1 O GLN D 114 N ILE D 5
SHEET 3 D 7 MSE D 95 LEU D 104 -1 N ALA D 102 O ASP D 109
SHEET 4 D 7 ARG D 79 PHE D 86 -1 N ASP D 84 O MSE D 95
SHEET 5 D 7 LYS D 64 VAL D 75 -1 N LEU D 72 O ARG D 81
SHEET 6 D 7 ALA D 51 ALA D 58 -1 N MSE D 54 O PHE D 67
SHEET 7 D 7 PHE D 37 HIS D 44 -1 N GLU D 43 O LYS D 53
SHEET 1 E 7 ASN E 3 LEU E 11 0
SHEET 2 E 7 GLY E 107 ILE E 117 -1 O ALA E 108 N LEU E 11
SHEET 3 E 7 ILE E 96 LEU E 104 -1 N ILE E 96 O GLU E 115
SHEET 4 E 7 ARG E 79 TYR E 82 -1 N ILE E 80 O ILE E 99
SHEET 5 E 7 LYS E 64 VAL E 75 -1 N LEU E 72 O ARG E 81
SHEET 6 E 7 ALA E 51 ALA E 58 -1 N PHE E 56 O HIS E 65
SHEET 7 E 7 PHE E 37 HIS E 44 -1 N GLU E 43 O LYS E 53
SHEET 1 F 7 ASN F 3 LEU F 11 0
SHEET 2 F 7 GLY F 107 ILE F 117 -1 O LEU F 110 N ARG F 9
SHEET 3 F 7 MSE F 95 LEU F 104 -1 N THR F 98 O VAL F 113
SHEET 4 F 7 ARG F 79 PHE F 86 -1 N ILE F 80 O ILE F 99
SHEET 5 F 7 LYS F 64 VAL F 75 -1 N LEU F 72 O ARG F 81
SHEET 6 F 7 ALA F 51 ALA F 58 -1 N PHE F 56 O HIS F 65
SHEET 7 F 7 PHE F 37 HIS F 44 -1 N GLU F 43 O LYS F 53
LINK C LYS A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N GLU A 55 1555 1555 1.33
LINK C ASP A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N ILE A 96 1555 1555 1.33
LINK C MSE B 1 N PRO B 2 1555 1555 1.35
LINK C LYS B 53 N MSE B 54 1555 1555 1.33
LINK C MSE B 54 N GLU B 55 1555 1555 1.32
LINK C ASP B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N ILE B 96 1555 1555 1.32
LINK C LYS C 53 N MSE C 54 1555 1555 1.33
LINK C MSE C 54 N GLU C 55 1555 1555 1.33
LINK C ASP C 94 N MSE C 95 1555 1555 1.33
LINK C MSE C 95 N ILE C 96 1555 1555 1.33
LINK C LYS D 53 N MSE D 54 1555 1555 1.33
LINK C MSE D 54 N GLU D 55 1555 1555 1.32
LINK C ASP D 94 N MSE D 95 1555 1555 1.33
LINK C MSE D 95 N ILE D 96 1555 1555 1.33
LINK C LYS E 53 N MSE E 54 1555 1555 1.33
LINK C MSE E 54 N GLU E 55 1555 1555 1.33
LINK C ASP E 94 N MSE E 95 1555 1555 1.33
LINK C MSE E 95 N ILE E 96 1555 1555 1.33
LINK C LYS F 53 N MSE F 54 1555 1555 1.32
LINK C MSE F 54 N GLU F 55 1555 1555 1.32
LINK C ASP F 94 N MSE F 95 1555 1555 1.33
LINK C MSE F 95 N ILE F 96 1555 1555 1.32
CISPEP 1 MSE B 1 PRO B 2 0 -1.75
CRYST1 105.095 170.247 128.126 90.00 90.00 90.00 C 2 2 21 48
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 0.009515 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007805 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
