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HEADER HYDROLASE 11-AUG-20 7JQX
TITLE CRYSTAL STRUCTURE OF CFL1 WILD-TYPE FROM BURKHOLDERIA CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CIF-LIKE 1 WILD-TYPE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA (STRAIN ATCC BAA-245 /
SOURCE 3 DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610);
SOURCE 4 ORGANISM_TAXID: 216591;
SOURCE 5 STRAIN: ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
SOURCE 6 CF5610;
SOURCE 7 GENE: BCAM1529;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OCTAMER, ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.TAHER,D.R.MADDEN
REVDAT 1 17-MAR-21 7JQX 0
JRNL AUTH N.M.TAHER,K.L.HVORECNY,C.M.BURKE,M.S.A.GILMAN,G.E.HEUSSLER,
JRNL AUTH 2 J.ADOLF-BRYFOGLE,C.D.BAHL,G.A.O'TOOLE,D.R.MADDEN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TWO CIF-LIKE
JRNL TITL 2 EPOXIDE HYDROLASES FROM BURKHOLDERIA CENOCEPACIA
JRNL REF CURR RES STRUCT BIOL 2021
JRNL REFN ESSN 2665-928X
JRNL DOI 10.1016/J.CRSTBI.2021.02.002
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 76601
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 5672
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 5672
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 5672
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7JQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1000249036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS-II
REMARK 200 BEAMLINE : 17-ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76696
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 750 MM POTASSIUM SODIUM TARTRATE, 100
REMARK 280 MM HEPES PH 8.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 66.07500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 170.85000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 66.07500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 170.85000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 66.07500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 170.85000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 66.07500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 170.85000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 66.07500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 170.85000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 66.07500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 170.85000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 66.07500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 170.85000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 66.07500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 66.07500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 170.85000
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -132.15000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -132.15000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -132.15000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -132.15000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
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 463 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 MET A 1
REMARK 465 GLN A 2
REMARK 465 ASN A 3
REMARK 465 GLU A 4
REMARK 465 ARG A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 GLN A 8
REMARK 465 SER A 9
REMARK 465 MET A 10
REMARK 465 ALA A 305
REMARK 465 ALA A 306
REMARK 465 SER A 307
REMARK 465 GLY A 308
REMARK 465 ARG A 309
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ASN B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 SER B 9
REMARK 465 MET B 10
REMARK 465 ALA B 305
REMARK 465 ALA B 306
REMARK 465 SER B 307
REMARK 465 GLY B 308
REMARK 465 ARG B 309
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 ASN C 3
REMARK 465 GLU C 4
REMARK 465 ARG C 5
REMARK 465 SER C 6
REMARK 465 GLU C 7
REMARK 465 GLN C 8
REMARK 465 SER C 9
REMARK 465 MET C 10
REMARK 465 ALA C 305
REMARK 465 ALA C 306
REMARK 465 SER C 307
REMARK 465 GLY C 308
REMARK 465 ARG C 309
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 ASN D 3
REMARK 465 GLU D 4
REMARK 465 ARG D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 GLN D 8
REMARK 465 SER D 9
REMARK 465 MET D 10
REMARK 465 ALA D 305
REMARK 465 ALA D 306
REMARK 465 SER D 307
REMARK 465 GLY D 308
REMARK 465 ARG D 309
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 THR A 115 -54.77 -139.27
REMARK 500 ASP A 123 -125.01 52.22
REMARK 500 ASP A 147 -39.32 71.60
REMARK 500 ASP A 177 -36.50 75.91
REMARK 500 SER A 258 -116.61 -130.00
REMARK 500 TRP A 285 76.08 -112.45
REMARK 500 THR B 115 -40.81 -134.56
REMARK 500 ASP B 123 -127.88 51.33
REMARK 500 ASP B 147 -39.31 71.82
REMARK 500 ASP B 177 -36.89 76.28
REMARK 500 SER B 258 -115.73 -127.35
REMARK 500 TRP B 285 77.58 -109.04
REMARK 500 LYS C 91 77.17 -119.98
REMARK 500 THR C 115 -56.44 -132.44
REMARK 500 ASP C 123 -128.03 52.28
REMARK 500 ASP C 147 -39.26 70.77
REMARK 500 ASP C 177 -37.89 75.07
REMARK 500 SER C 258 -116.01 -127.70
REMARK 500 TRP C 285 77.34 -112.46
REMARK 500 ASP D 34 -119.80 56.16
REMARK 500 THR D 115 -51.40 -139.37
REMARK 500 ASP D 123 -124.39 52.67
REMARK 500 ASP D 147 -39.98 71.08
REMARK 500 ASP D 177 -36.63 76.75
REMARK 500 SER D 258 -114.95 -127.84
REMARK 500 TRP D 285 77.12 -110.16
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7JQX A 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQX B 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQX C 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQX D 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
SEQRES 1 A 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 A 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 A 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 A 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 A 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 A 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 A 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 A 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 A 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 A 309 HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR
SEQRES 11 A 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 A 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 A 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 A 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 A 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 A 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 A 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 A 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 A 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 A 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 A 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 A 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 A 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 A 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 B 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 B 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 B 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 B 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 B 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 B 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 B 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 B 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 B 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 B 309 HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR
SEQRES 11 B 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 B 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 B 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 B 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 B 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 B 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 B 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 B 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 B 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 B 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 B 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 B 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 B 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 B 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 C 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 C 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 C 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 C 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 C 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 C 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 C 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 C 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 C 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 C 309 HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR
SEQRES 11 C 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 C 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 C 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 C 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 C 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 C 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 C 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 C 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 C 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 C 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 C 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 C 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 C 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 C 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 D 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 D 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 D 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 D 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 D 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 D 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 D 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 D 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 D 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 D 309 HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR
SEQRES 11 D 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 D 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 D 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 D 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 D 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 D 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 D 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 D 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 D 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 D 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 D 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 D 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 D 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 D 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
FORMUL 5 HOH *604(H2 O)
HELIX 1 AA1 GLY A 21 ARG A 25 1 5
HELIX 2 AA2 THR A 60 ARG A 65 5 6
HELIX 3 AA3 VAL A 67 ASP A 74 1 8
HELIX 4 AA4 ASP A 97 LEU A 112 1 16
HELIX 5 AA5 ASP A 123 TRP A 136 1 14
HELIX 6 AA6 THR A 153 ALA A 163 1 11
HELIX 7 AA7 ASP A 164 ILE A 167 5 4
HELIX 8 AA8 TRP A 168 GLN A 174 1 7
HELIX 9 AA9 ASP A 177 ALA A 184 1 8
HELIX 10 AB1 LYS A 186 THR A 199 1 14
HELIX 11 AB2 SER A 204 ALA A 216 1 13
HELIX 12 AB3 GLY A 219 ALA A 230 1 12
HELIX 13 AB4 ALA A 230 MET A 242 1 13
HELIX 14 AB5 ALA A 261 GLU A 269 1 9
HELIX 15 AB6 TRP A 285 ASN A 290 1 6
HELIX 16 AB7 ASN A 290 GLU A 304 1 15
HELIX 17 AB8 GLY B 21 ARG B 25 1 5
HELIX 18 AB9 THR B 60 ARG B 65 5 6
HELIX 19 AC1 VAL B 67 ASP B 74 1 8
HELIX 20 AC2 ASP B 97 LEU B 112 1 16
HELIX 21 AC3 ASP B 123 TRP B 136 1 14
HELIX 22 AC4 THR B 153 SER B 162 1 10
HELIX 23 AC5 ASP B 164 ILE B 167 5 4
HELIX 24 AC6 TRP B 168 GLN B 174 1 7
HELIX 25 AC7 ASP B 177 ALA B 184 1 8
HELIX 26 AC8 LYS B 186 THR B 199 1 14
HELIX 27 AC9 SER B 204 ALA B 216 1 13
HELIX 28 AD1 GLY B 219 ALA B 230 1 12
HELIX 29 AD2 ALA B 230 MET B 242 1 13
HELIX 30 AD3 ALA B 261 GLU B 269 1 9
HELIX 31 AD4 TRP B 285 ASN B 290 1 6
HELIX 32 AD5 ASN B 290 GLU B 304 1 15
HELIX 33 AD6 GLY C 21 ARG C 25 1 5
HELIX 34 AD7 THR C 60 ARG C 65 5 6
HELIX 35 AD8 VAL C 67 ASP C 74 1 8
HELIX 36 AD9 ASP C 97 LEU C 112 1 16
HELIX 37 AE1 ASP C 123 TRP C 136 1 14
HELIX 38 AE2 THR C 153 SER C 162 1 10
HELIX 39 AE3 ASP C 164 ILE C 167 5 4
HELIX 40 AE4 TRP C 168 GLN C 174 1 7
HELIX 41 AE5 ASP C 177 ALA C 184 1 8
HELIX 42 AE6 LYS C 186 THR C 199 1 14
HELIX 43 AE7 SER C 204 ALA C 216 1 13
HELIX 44 AE8 GLY C 219 ALA C 230 1 12
HELIX 45 AE9 ALA C 230 MET C 242 1 13
HELIX 46 AF1 ALA C 261 GLU C 269 1 9
HELIX 47 AF2 TRP C 285 ASN C 290 1 6
HELIX 48 AF3 ASN C 290 GLU C 304 1 15
HELIX 49 AF4 GLY D 21 PHE D 26 1 6
HELIX 50 AF5 THR D 60 ARG D 65 5 6
HELIX 51 AF6 VAL D 67 ASP D 74 1 8
HELIX 52 AF7 ASP D 97 LEU D 112 1 16
HELIX 53 AF8 ASP D 123 TRP D 136 1 14
HELIX 54 AF9 THR D 153 SER D 162 1 10
HELIX 55 AG1 ASP D 164 ILE D 167 5 4
HELIX 56 AG2 TRP D 168 GLN D 174 1 7
HELIX 57 AG3 ASP D 177 ALA D 184 1 8
HELIX 58 AG4 LYS D 186 THR D 199 1 14
HELIX 59 AG5 SER D 204 ALA D 216 1 13
HELIX 60 AG6 GLY D 219 ALA D 230 1 12
HELIX 61 AG7 ALA D 230 MET D 242 1 13
HELIX 62 AG8 ALA D 261 GLU D 269 1 9
HELIX 63 AG9 TRP D 285 ASN D 290 1 6
HELIX 64 AH1 ASN D 290 GLU D 304 1 15
SHEET 1 AA1 8 PHE A 26 GLN A 32 0
SHEET 2 AA1 8 ARG A 37 GLY A 43 -1 O LEU A 38 N ALA A 31
SHEET 3 AA1 8 ARG A 77 ASP A 82 -1 O ASP A 82 N HIS A 39
SHEET 4 AA1 8 MET A 50 LEU A 54 1 N VAL A 51 O ARG A 77
SHEET 5 AA1 8 ILE A 117 ARG A 122 1 O VAL A 120 N VAL A 52
SHEET 6 AA1 8 ILE A 140 LEU A 146 1 O ALA A 144 N LEU A 119
SHEET 7 AA1 8 VAL A 250 GLY A 255 1 O LEU A 251 N MET A 145
SHEET 8 AA1 8 VAL A 274 ALA A 279 1 O ALA A 279 N ALA A 254
SHEET 1 AA2 8 PHE B 26 GLN B 32 0
SHEET 2 AA2 8 ARG B 37 GLY B 43 -1 O LEU B 38 N ALA B 31
SHEET 3 AA2 8 ARG B 77 ASP B 82 -1 O ALA B 80 N VAL B 41
SHEET 4 AA2 8 MET B 50 LEU B 54 1 N VAL B 51 O ARG B 77
SHEET 5 AA2 8 ILE B 117 ARG B 122 1 O HIS B 118 N VAL B 52
SHEET 6 AA2 8 ILE B 140 LEU B 146 1 O ALA B 144 N LEU B 119
SHEET 7 AA2 8 VAL B 250 GLY B 255 1 O LEU B 251 N MET B 145
SHEET 8 AA2 8 VAL B 274 ALA B 279 1 O ALA B 279 N ALA B 254
SHEET 1 AA3 8 PHE C 26 GLN C 32 0
SHEET 2 AA3 8 ARG C 37 GLY C 43 -1 O TYR C 40 N ARG C 29
SHEET 3 AA3 8 ARG C 77 ASP C 82 -1 O ALA C 80 N VAL C 41
SHEET 4 AA3 8 MET C 50 LEU C 54 1 N VAL C 51 O VAL C 79
SHEET 5 AA3 8 ILE C 117 ARG C 122 1 O HIS C 118 N VAL C 52
SHEET 6 AA3 8 ILE C 140 LEU C 146 1 O VAL C 141 N ILE C 117
SHEET 7 AA3 8 VAL C 250 GLY C 255 1 O LEU C 251 N MET C 145
SHEET 8 AA3 8 VAL C 274 ALA C 279 1 O ARG C 275 N VAL C 250
SHEET 1 AA4 8 SER D 27 LEU D 33 0
SHEET 2 AA4 8 VAL D 36 GLY D 43 -1 O TYR D 40 N ARG D 29
SHEET 3 AA4 8 ARG D 77 ASP D 82 -1 O ALA D 80 N VAL D 41
SHEET 4 AA4 8 MET D 50 LEU D 54 1 N VAL D 51 O ARG D 77
SHEET 5 AA4 8 ILE D 117 ARG D 122 1 O HIS D 118 N MET D 50
SHEET 6 AA4 8 ILE D 140 LEU D 146 1 O ALA D 144 N LEU D 119
SHEET 7 AA4 8 VAL D 250 GLY D 255 1 O LEU D 251 N MET D 145
SHEET 8 AA4 8 VAL D 274 ALA D 279 1 O ALA D 279 N ALA D 254
CISPEP 1 TRP A 57 PRO A 58 0 -4.92
CISPEP 2 TRP B 57 PRO B 58 0 -3.46
CISPEP 3 TRP C 57 PRO C 58 0 -4.44
CISPEP 4 TRP D 57 PRO D 58 0 -3.19
CRYST1 132.150 132.150 341.700 90.00 90.00 90.00 I 4 2 2 64
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 0.007567 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007567 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002927 0.00000
TER 2320 GLU A 304
TER 4640 GLU B 304
TER 6960 GLU C 304
TER 9280 GLU D 304
MASTER 403 0 0 64 32 0 0 6 9880 4 0 96
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