| 3G8Y-pdb | HEADER HYDROLASE 12-FEB-09 3G8Y
TITLE CRYSTAL STRUCTURE OF A PUTATIVE HYDROLASE (BVU_4111) FROM BACTEROIDES
TITLE 2 VULGATUS ATCC 8482 AT 1.90 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUSD/RAGB-ASSOCIATED ESTERASE-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-414;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES VULGATUS ATCC 8482;
SOURCE 3 ORGANISM_TAXID: 435590;
SOURCE 4 STRAIN: DSM 1447 / NCTC 11154;
SOURCE 5 ATCC: 8482;
SOURCE 6 GENE: YP_001301335.1, BVU_4111;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS SUSD/RAGB-ASSOCIATED ESTERASE-LIKE PROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 2 28-JUL-10 3G8Y 1 HEADER TITLE KEYWDS
REVDAT 1 24-FEB-09 3G8Y 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF SUSD/RAGB-ASSOCIATED ESTERASE-LIKE
JRNL TITL 2 PROTEIN (YP_001301335.1) FROM BACTEROIDES VULGATUS ATCC 8482
JRNL TITL 3 AT 1.90 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 44778
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2257
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3023
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 471
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : 0.19000
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): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.810
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3330 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2296 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4511 ; 1.544 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5583 ; 1.025 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 410 ; 4.004 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;30.751 ;23.946
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 537 ;11.594 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ; 9.954 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 475 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3711 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 685 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 711 ; 0.210 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2376 ; 0.178 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1644 ; 0.187 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 1531 ; 0.088 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 581 ; 0.197 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.205 ; 0.500
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): 14 ; 0.152 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.260 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 52 ; 0.188 ; 0.500
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): 2173 ; 1.861 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 804 ; 0.453 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3273 ; 2.602 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1481 ; 4.002 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1238 ; 4.814 ;11.000
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 : NULL
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. PEG MOLECULES FROM CRYSTALLIZATION AND ETHYLENE
REMARK 3 GLYCOL FROM CRYOPROTECTION ARE MODELED IN THIS STRUCTURE. 4.
REMARK 3 UNKNOWN ELECTRON DENSITY IS OBSERVED AND UNMODELED NEAR SER 256
REMARK 3 AND HIS 398.
REMARK 4
REMARK 4 3G8Y COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051572.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91162, 0.97982, 0.97966
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : FLAT COLLIMATING MIRROR, TOROID
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44914
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.399
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : 0.14300
REMARK 200 FOR THE DATA SET : 4.8240
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.77800
REMARK 200 R SYM FOR SHELL (I) : 0.77800
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 20.0% PEG 6000, 0.1M BICINE
REMARK 280 PH 9.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.79533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 215.59067
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 161.69300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 269.48833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.89767
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 107.79533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 215.59067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 269.48833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 161.69300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 53.89767
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE RESULTS FROM SIZE EXCLUSION CHROMATOGRAPHY SUPPORT THE
REMARK 300 ASSIGNMENT OF A DIMER AS A SIGNIFICANT OLIGOMERIZATION STATE.
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: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.7 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 0.500000 0.866025 0.000000 -37.95150
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 65.73393
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 53.89767
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 69 CD OE1 NE2
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 ASP A 161 OD1 OD2
REMARK 470 LYS A 270 CD CE NZ
REMARK 470 LYS A 296 CG CD CE NZ
REMARK 470 ARG A 315 CZ NH1 NH2
REMARK 470 LYS A 373 NZ
REMARK 470 ARG A 410 NH1 NH2
REMARK 470 LYS A 414 CD CE NZ
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 ARG A 93 123.28 -36.02
REMARK 500 LYS A 134 -99.67 -93.11
REMARK 500 ALA A 192 -4.03 83.82
REMARK 500 ASP A 198 -93.57 -113.61
REMARK 500 ASP A 203 -70.34 -162.79
REMARK 500 TRP A 222 -157.95 -108.38
REMARK 500 SER A 256 -126.83 56.29
REMARK 500 GLU A 335 42.93 -141.32
REMARK 500 ASN A 392 42.26 70.14
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 ARG A 93 24.8 L L OUTSIDE RANGE
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 EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 13
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 393239 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
REMARK 999 THE CLONED CONSTRUCT CONTAINS RESIDUES 25-414 OF THE FULL
REMARK 999 LENGTH PROTEIN.
DBREF 3G8Y A 25 414 UNP A6L7P9 A6L7P9_BACV8 25 414
SEQADV 3G8Y GLY A 0 UNP A6L7P9 LEADER SEQUENCE
SEQRES 1 A 391 GLY TYR GLN PRO GLU LYS HIS ALA VAL VAL LYS SER ASP
SEQRES 2 A 391 ARG GLY ASP GLY ARG LEU LEU SER THR TYR ALA ILE VAL
SEQRES 3 A 391 HIS GLU MSE LEU LYS ASP THR HIS PRO GLN TYR ALA TYR
SEQRES 4 A 391 ARG SER GLY MSE SER ALA GLN GLU PHE THR GLN TRP GLN
SEQRES 5 A 391 ASP GLY VAL ARG ALA ALA MSE VAL GLU ILE MSE LYS PHE
SEQRES 6 A 391 PRO GLU ILE LYS ARG GLN PRO SER PRO VAL CYS VAL LYS
SEQRES 7 A 391 THR GLU LYS LYS GLU GLY TYR ILE LEU GLU LYS TRP GLU
SEQRES 8 A 391 PHE TYR PRO PHE PRO LYS SER VAL SER THR PHE LEU VAL
SEQRES 9 A 391 LEU LYS PRO GLU HIS LEU LYS GLY ALA VAL PRO GLY VAL
SEQRES 10 A 391 LEU CYS ILE PRO GLY SER GLY ARG THR LYS GLU GLY LEU
SEQRES 11 A 391 VAL GLY GLU PRO GLY ILE CYS ASP LYS LEU THR GLU ASP
SEQRES 12 A 391 TYR ASN ASN PRO LYS VAL SER MSE ALA LEU ASN MSE VAL
SEQRES 13 A 391 LYS GLU GLY TYR VAL ALA VAL ALA VAL ASP ASN ALA ALA
SEQRES 14 A 391 ALA GLY GLU ALA SER ASP LEU GLU CYS TYR ASP LYS GLY
SEQRES 15 A 391 TRP ASN TYR ASP TYR ASP VAL VAL SER ARG PHE LEU LEU
SEQRES 16 A 391 GLU LEU GLY TRP SER TRP LEU GLY TYR THR SER TYR LEU
SEQRES 17 A 391 ASP MSE GLN VAL LEU ASN TRP MSE LYS ALA GLN SER TYR
SEQRES 18 A 391 ILE ARG LYS ASP ARG ILE VAL ILE SER GLY PHE SER LEU
SEQRES 19 A 391 GLY THR GLU PRO MSE MSE VAL LEU GLY VAL LEU ASP LYS
SEQRES 20 A 391 ASP ILE TYR ALA PHE VAL TYR ASN ASP PHE LEU CYS GLN
SEQRES 21 A 391 THR GLN GLU ARG ALA VAL VAL MSE THR LYS PRO ASP LYS
SEQRES 22 A 391 GLU ASN ARG ARG PRO PHE PRO ASN SER ILE ARG HIS LEU
SEQRES 23 A 391 ILE PRO GLY TYR TRP ARG TYR PHE ASN PHE PRO ASP VAL
SEQRES 24 A 391 VAL ALA SER LEU ALA PRO ARG PRO ILE ILE PHE THR GLU
SEQRES 25 A 391 GLY GLY LEU ASP ARG ASP PHE ARG LEU VAL GLN SER ALA
SEQRES 26 A 391 TYR ALA ALA SER GLY LYS PRO GLU ASN ALA GLU PHE HIS
SEQRES 27 A 391 HIS TYR PRO LYS PHE ALA ASP LYS ALA VAL ARG LYS ASP
SEQRES 28 A 391 VAL GLU HIS LEU ASP GLU GLY LEU ASP SER LYS THR TYR
SEQRES 29 A 391 PHE GLU ALA VAL ASN VAL ASP PRO PRO SER HIS TYR PHE
SEQRES 30 A 391 LYS ASN GLU LEU VAL ILE PRO TRP LEU ARG LYS VAL LEU
SEQRES 31 A 391 LYS
MODRES 3G8Y MSE A 52 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 66 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 82 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 86 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 174 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 178 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 233 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 239 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 262 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 263 MET SELENOMETHIONINE
MODRES 3G8Y MSE A 291 MET SELENOMETHIONINE
HET MSE A 52 8
HET MSE A 66 8
HET MSE A 82 8
HET MSE A 86 8
HET MSE A 174 8
HET MSE A 178 16
HET MSE A 233 8
HET MSE A 239 8
HET MSE A 262 16
HET MSE A 263 8
HET MSE A 291 16
HET EDO A 1 4
HET EDO A 2 4
HET EDO A 3 4
HET EDO A 4 4
HET EDO A 5 4
HET EDO A 6 4
HET EDO A 7 4
HET EDO A 8 4
HET EDO A 9 4
HET EDO A 10 4
HET EDO A 11 4
HET EDO A 12 4
HET PEG A 13 7
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 2 EDO 12(C2 H6 O2)
FORMUL 14 PEG C4 H10 O3
FORMUL 15 HOH *471(H2 O)
HELIX 1 1 GLN A 26 ALA A 31 5 6
HELIX 2 2 SER A 44 ASP A 55 1 12
HELIX 3 3 SER A 67 LYS A 87 1 21
HELIX 4 4 THR A 149 VAL A 154 1 6
HELIX 5 5 CYS A 160 THR A 164 5 5
HELIX 6 6 SER A 173 LYS A 180 1 8
HELIX 7 7 ALA A 193 SER A 197 5 5
HELIX 8 8 LEU A 199 ASP A 203 5 5
HELIX 9 9 ASP A 209 LEU A 220 1 12
HELIX 10 10 SER A 223 ALA A 241 1 19
HELIX 11 11 GLY A 258 ASP A 269 1 12
HELIX 12 12 GLN A 283 MSE A 291 1 9
HELIX 13 13 SER A 305 LEU A 309 5 5
HELIX 14 14 GLY A 312 TYR A 316 5 5
HELIX 15 15 ASN A 318 SER A 325 1 8
HELIX 16 16 LEU A 338 SER A 352 1 15
HELIX 17 17 LYS A 354 GLU A 356 5 3
HELIX 18 18 TYR A 363 ALA A 367 5 5
HELIX 19 19 ASP A 368 ARG A 372 5 5
HELIX 20 20 ASP A 383 VAL A 391 1 9
HELIX 21 21 ASP A 394 HIS A 398 5 5
HELIX 22 22 LYS A 401 LEU A 413 1 13
SHEET 1 A 9 VAL A 98 LYS A 105 0
SHEET 2 A 9 TYR A 108 PHE A 115 -1 O TYR A 108 N LYS A 105
SHEET 3 A 9 SER A 123 PRO A 130 -1 O VAL A 127 N GLU A 111
SHEET 4 A 9 VAL A 184 ALA A 187 -1 O ALA A 185 N LEU A 128
SHEET 5 A 9 VAL A 137 ILE A 143 1 N CYS A 142 O VAL A 186
SHEET 6 A 9 ILE A 245 PHE A 255 1 O ARG A 246 N VAL A 137
SHEET 7 A 9 ALA A 274 ASN A 278 1 O VAL A 276 N GLY A 254
SHEET 8 A 9 ILE A 331 PHE A 333 1 O ILE A 332 N TYR A 277
SHEET 9 A 9 ALA A 358 PHE A 360 1 O GLU A 359 N ILE A 331
LINK C GLU A 51 N MSE A 52 1555 1555 1.33
LINK C MSE A 52 N LEU A 53 1555 1555 1.34
LINK C GLY A 65 N MSE A 66 1555 1555 1.33
LINK C MSE A 66 N SER A 67 1555 1555 1.33
LINK C ALA A 81 N MSE A 82 1555 1555 1.33
LINK C MSE A 82 N VAL A 83 1555 1555 1.33
LINK C ILE A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N LYS A 87 1555 1555 1.33
LINK C SER A 173 N MSE A 174 1555 1555 1.33
LINK C MSE A 174 N ALA A 175 1555 1555 1.33
LINK C ASN A 177 N AMSE A 178 1555 1555 1.33
LINK C ASN A 177 N BMSE A 178 1555 1555 1.33
LINK C AMSE A 178 N VAL A 179 1555 1555 1.33
LINK C BMSE A 178 N VAL A 179 1555 1555 1.33
LINK C ASP A 232 N MSE A 233 1555 1555 1.33
LINK C MSE A 233 N AGLN A 234 1555 1555 1.33
LINK C MSE A 233 N BGLN A 234 1555 1555 1.34
LINK C TRP A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N LYS A 240 1555 1555 1.33
LINK C PRO A 261 N AMSE A 262 1555 1555 1.33
LINK C PRO A 261 N BMSE A 262 1555 1555 1.34
LINK C AMSE A 262 N MSE A 263 1555 1555 1.33
LINK C BMSE A 262 N MSE A 263 1555 1555 1.34
LINK C MSE A 263 N VAL A 264 1555 1555 1.33
LINK C VAL A 290 N AMSE A 291 1555 1555 1.33
LINK C VAL A 290 N BMSE A 291 1555 1555 1.34
LINK C AMSE A 291 N THR A 292 1555 1555 1.34
LINK C BMSE A 291 N THR A 292 1555 1555 1.33
CISPEP 1 ALA A 327 PRO A 328 0 1.77
SITE 1 AC1 5 ARG A 343 ASP A 374 GLU A 376 LYS A 411
SITE 2 AC1 5 HOH A 803
SITE 1 AC2 4 ASP A 279 PHE A 280 PHE A 388 HIS A 398
SITE 1 AC3 6 MSE A 52 ASP A 55 PHE A 118 PRO A 119
SITE 2 AC3 6 HOH A 449 HOH A 656
SITE 1 AC4 5 GLY A 145 SER A 146 ARG A 148 PHE A 255
SITE 2 AC4 5 HOH A 788
SITE 1 AC5 7 ASP A 211 VAL A 212 ARG A 215 ILE A 306
SITE 2 AC5 7 HOH A 517 HOH A 523 HOH A 567
SITE 1 AC6 6 TYR A 60 GLY A 77 GLU A 84 TYR A 316
SITE 2 AC6 6 HOH A 851 HOH A 871
SITE 1 AC7 3 LYS A 87 LEU A 220 GLY A 221
SITE 1 AC8 7 PHE A 366 VAL A 371 LYS A 373 GLU A 389
SITE 2 AC8 7 HOH A 486 HOH A 630 HOH A 689
SITE 1 AC9 8 HOH A 21 THR A 284 HIS A 308 ILE A 310
SITE 2 AC9 8 TYR A 313 TRP A 314 HOH A 562 HOH A 591
SITE 1 BC1 6 TYR A 62 SER A 64 ARG A 343 LEU A 344
SITE 2 BC1 6 HOH A 554 HOH A 650
SITE 1 BC2 4 GLN A 26 GLY A 194 GLU A 195 HOH A 820
SITE 1 BC3 6 LYS A 369 ARG A 372 GLU A 403 PRO A 407
SITE 2 BC3 6 HOH A 599 HOH A 612
SITE 1 BC4 4 SER A 146 GLY A 147 ARG A 148 HOH A 657
CRYST1 75.903 75.903 323.386 90.00 90.00 120.00 P 61 2 2 12
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 0.013175 0.007606 0.000000 0.00000
SCALE2 0.000000 0.015213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003092 0.00000
TER 3191 LYS A 414
MASTER 405 0 24 22 9 0 22 6 3632 1 188 31
END
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