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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-NOV-07 3BDV
TITLE CRYSTAL STRUCTURE OF YDEN-LIKE PROTEIN OF UNKNOWN FUNCTION
TITLE 2 (DUF1234) (YP_051181.1) FROM ERWINIA CAROTOVORA SUBSP.
TITLE 3 ATROSEPTICA SCRI1043 AT 1.66 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN DUF1234;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERWINIA CAROTOVORA SUBSP. ATROSEPTICA
SOURCE 3 SCRI1043;
SOURCE 4 ORGANISM_COMMON: BACTERIA;
SOURCE 5 STRAIN: SCRI 1043;
SOURCE 6 ATCC: BAA-672;
SOURCE 7 GENE: YP_051181.1, ECA3091;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS YP_051181.1, YDEN-LIKE PROTEIN OF UNKNOWN FUNCTION
KEYWDS 2 (DUF1234), ALPHA/BETA HYDROLASE FAMILY OF UNKNOWN FUNCTION
KEYWDS 3 (DUF1234), STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 4 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2,
KEYWDS 5 STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 27-NOV-07 3BDV 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF YDEN-LIKE PROTEIN OF UNKNOWN
JRNL TITL 2 FUNCTION (DUF1234) (YP_051181.1) FROM ERWINIA
JRNL TITL 3 CAROTOVORA SUBSP. ATROSEPTICA SCRI1043 AT 1.66 A
JRNL TITL 4 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.66 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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 41889
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2112
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2909
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3445
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.67000
REMARK 3 B22 (A**2) : -1.48000
REMARK 3 B33 (A**2) : 0.81000
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): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.078
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
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): 3246 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2197 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4459 ; 1.485 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5341 ; 0.991 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 424 ; 5.114 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;36.857 ;23.416
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 526 ;13.691 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.559 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 487 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3686 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 694 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 679 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2414 ; 0.214 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1572 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1712 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 210 ; 0.167 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 9 ; 0.092 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 19 ; 0.213 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 54 ; 0.296 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.142 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 2 ; 0.089 ; 0.200
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): 2021 ; 1.962 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 779 ; 0.657 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3179 ; 2.698 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1441 ; 4.183 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1254 ; 5.683 ;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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 188 4
REMARK 3 1 B 5 B 188 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2351 ; 0.350 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2351 ; 1.150 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 0 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2477 77.5532 33.5788
REMARK 3 T TENSOR
REMARK 3 T11: -0.0379 T22: -0.0120
REMARK 3 T33: -0.0521 T12: 0.0261
REMARK 3 T13: -0.0059 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.7355 L22: 1.5386
REMARK 3 L33: 0.4078 L12: 0.0911
REMARK 3 L13: -0.1064 L23: -0.4348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.0179 S13: 0.0278
REMARK 3 S21: 0.2141 S22: 0.0611 S23: 0.0834
REMARK 3 S31: -0.1029 S32: -0.0433 S33: -0.0626
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 : B 4 B 188
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8661 89.5320 8.9302
REMARK 3 T TENSOR
REMARK 3 T11: -0.0371 T22: -0.0122
REMARK 3 T33: -0.0337 T12: -0.0142
REMARK 3 T13: -0.0081 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5454 L22: 2.6590
REMARK 3 L33: 0.9486 L12: 0.3481
REMARK 3 L13: 0.0789 L23: 0.1095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0833 S12: 0.0502 S13: -0.0487
REMARK 3 S21: -0.3404 S22: 0.0773 S23: -0.0657
REMARK 3 S31: 0.0548 S32: -0.0024 S33: 0.0060
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. ATOM RECORDS CONTAIN RESIDUAL B FACTORS
REMARK 3 ONLY. 3. 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
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 4. CALCIUM IONS, CHLORIDE IONS AND ETHYLENE
REMARK 3 GLYCOL MODELED ARE PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS.
REMARK 4
REMARK 4 3BDV COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB045396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91840, 0.97953, 0.97939
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS
REMARK 200 IN K-B GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41954
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 42.563
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M CA(OAC)2, 10.0% PEG
REMARK 280 8000, 0.1M IMIDAZOLE PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 17.82750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.04750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.65100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.04750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.82750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.65100
REMARK 290 SMTRY3 4 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 ASN B 189
REMARK 465 ARG B 190
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 THR A 4 OG1 CG2
REMARK 470 GLU A 5 CD OE1 OE2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 GLN A 54 CD OE1 NE2
REMARK 470 THR B 4 OG1 CG2
REMARK 470 GLU B 5 CG CD OE1 OE2
REMARK 470 ARG B 26 NE CZ NH1 NH2
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 GLN B 54 CG CD OE1 NE2
REMARK 470 GLU B 96 CD OE1 OE2
REMARK 470 GLN B 148 OE1 NE2
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 ASP A 27 170.27 73.14
REMARK 500 SER A 81 -119.99 58.12
REMARK 500 ASP B 27 169.44 67.69
REMARK 500 SER B 81 -118.22 57.04
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 CA A 191 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 46 O
REMARK 620 2 GLU A 67 OE1 83.1
REMARK 620 3 GLU A 67 OE2 87.5 50.1
REMARK 620 4 HOH A 268 O 164.2 91.1 77.6
REMARK 620 5 HOH A 342 O 115.8 84.4 127.0 78.1
REMARK 620 6 HOH A 239 O 83.5 121.0 72.2 87.0 151.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 191 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 185 O
REMARK 620 2 ASP B 151 OD2 109.2
REMARK 620 3 EDO A 195 O1 80.9 137.1
REMARK 620 4 EDO A 195 O2 88.8 63.7 75.3
REMARK 620 5 HOH A 242 O 92.5 140.2 77.7 152.4
REMARK 620 6 HOH B 248 O 75.8 81.9 139.9 135.2 71.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 192 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 EDO A 194 O2
REMARK 620 2 EDO A 194 O1 63.4
REMARK 620 3 HOH A 367 O 75.3 63.5
REMARK 620 4 HOH A 285 O 126.6 69.3 62.1
REMARK 620 5 HOH A 313 O 81.4 141.7 94.5 130.0
REMARK 620 6 HOH A 265 O 165.5 131.1 110.1 66.4 84.7
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 379345 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.
DBREF 3BDV A 1 190 UNP Q6D2K4 Q6D2K4_ERWCT 1 190
DBREF 3BDV B 1 190 UNP Q6D2K4 Q6D2K4_ERWCT 1 190
SEQADV 3BDV GLY A 0 UNP Q6D2K4 LEADER SEQUENCE
SEQADV 3BDV GLY B 0 UNP Q6D2K4 LEADER SEQUENCE
SEQRES 1 A 191 GLY MSE GLN THR THR GLU ILE ASP LEU ARG LEU THR GLU
SEQRES 2 A 191 VAL SER GLN GLN LEU THR MSE VAL LEU VAL PRO GLY LEU
SEQRES 3 A 191 ARG ASP SER ASP ASP GLU HIS TRP GLN SER HIS TRP GLU
SEQRES 4 A 191 ARG ARG PHE PRO HIS TRP GLN ARG ILE ARG GLN ARG GLU
SEQRES 5 A 191 TRP TYR GLN ALA ASP LEU ASP ARG TRP VAL LEU ALA ILE
SEQRES 6 A 191 ARG ARG GLU LEU SER VAL CYS THR GLN PRO VAL ILE LEU
SEQRES 7 A 191 ILE GLY HIS SER PHE GLY ALA LEU ALA ALA CYS HIS VAL
SEQRES 8 A 191 VAL GLN GLN GLY GLN GLU GLY ILE ALA GLY VAL MSE LEU
SEQRES 9 A 191 VAL ALA PRO ALA GLU PRO MSE ARG PHE GLU ILE ASP ASP
SEQRES 10 A 191 ARG ILE GLN ALA SER PRO LEU SER VAL PRO THR LEU THR
SEQRES 11 A 191 PHE ALA SER HIS ASN ASP PRO LEU MSE SER PHE THR ARG
SEQRES 12 A 191 ALA GLN TYR TRP ALA GLN ALA TRP ASP SER GLU LEU VAL
SEQRES 13 A 191 ASP VAL GLY GLU ALA GLY HIS ILE ASN ALA GLU ALA GLY
SEQRES 14 A 191 PHE GLY PRO TRP GLU TYR GLY LEU LYS ARG LEU ALA GLU
SEQRES 15 A 191 PHE SER GLU ILE LEU ILE PRO ASN ARG
SEQRES 1 B 191 GLY MSE GLN THR THR GLU ILE ASP LEU ARG LEU THR GLU
SEQRES 2 B 191 VAL SER GLN GLN LEU THR MSE VAL LEU VAL PRO GLY LEU
SEQRES 3 B 191 ARG ASP SER ASP ASP GLU HIS TRP GLN SER HIS TRP GLU
SEQRES 4 B 191 ARG ARG PHE PRO HIS TRP GLN ARG ILE ARG GLN ARG GLU
SEQRES 5 B 191 TRP TYR GLN ALA ASP LEU ASP ARG TRP VAL LEU ALA ILE
SEQRES 6 B 191 ARG ARG GLU LEU SER VAL CYS THR GLN PRO VAL ILE LEU
SEQRES 7 B 191 ILE GLY HIS SER PHE GLY ALA LEU ALA ALA CYS HIS VAL
SEQRES 8 B 191 VAL GLN GLN GLY GLN GLU GLY ILE ALA GLY VAL MSE LEU
SEQRES 9 B 191 VAL ALA PRO ALA GLU PRO MSE ARG PHE GLU ILE ASP ASP
SEQRES 10 B 191 ARG ILE GLN ALA SER PRO LEU SER VAL PRO THR LEU THR
SEQRES 11 B 191 PHE ALA SER HIS ASN ASP PRO LEU MSE SER PHE THR ARG
SEQRES 12 B 191 ALA GLN TYR TRP ALA GLN ALA TRP ASP SER GLU LEU VAL
SEQRES 13 B 191 ASP VAL GLY GLU ALA GLY HIS ILE ASN ALA GLU ALA GLY
SEQRES 14 B 191 PHE GLY PRO TRP GLU TYR GLY LEU LYS ARG LEU ALA GLU
SEQRES 15 B 191 PHE SER GLU ILE LEU ILE PRO ASN ARG
MODRES 3BDV MSE A 1 MET SELENOMETHIONINE
MODRES 3BDV MSE A 19 MET SELENOMETHIONINE
MODRES 3BDV MSE A 102 MET SELENOMETHIONINE
MODRES 3BDV MSE A 110 MET SELENOMETHIONINE
MODRES 3BDV MSE A 138 MET SELENOMETHIONINE
MODRES 3BDV MSE B 19 MET SELENOMETHIONINE
MODRES 3BDV MSE B 102 MET SELENOMETHIONINE
MODRES 3BDV MSE B 110 MET SELENOMETHIONINE
MODRES 3BDV MSE B 138 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 19 8
HET MSE A 102 8
HET MSE A 110 8
HET MSE A 138 8
HET MSE B 19 13
HET MSE B 102 13
HET MSE B 110 13
HET MSE B 138 13
HET CA A 191 1
HET CA A 192 1
HET CA B 191 1
HET CL A 193 1
HET CL B 192 1
HET EDO A 194 4
HET EDO B 193 4
HET EDO A 195 4
HET EDO A 196 4
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 3 CA 3(CA 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 8 EDO 4(C2 H6 O2)
FORMUL 12 HOH *295(H2 O)
HELIX 1 1 GLN A 2 GLN A 15 1 14
HELIX 2 2 HIS A 32 PHE A 41 1 10
HELIX 3 3 ASP A 56 VAL A 70 1 15
HELIX 4 4 SER A 81 GLN A 93 1 13
HELIX 5 5 GLU A 108 GLU A 113 5 6
HELIX 6 6 SER A 139 ASP A 151 1 13
HELIX 7 7 ASN A 164 GLY A 168 5 5
HELIX 8 8 TRP A 172 ILE A 185 1 14
HELIX 9 9 THR B 4 GLN B 15 1 12
HELIX 10 10 HIS B 32 PHE B 41 1 10
HELIX 11 11 ASP B 56 VAL B 70 1 15
HELIX 12 12 SER B 81 GLN B 93 1 13
HELIX 13 13 GLU B 108 GLU B 113 5 6
HELIX 14 14 SER B 139 ASP B 151 1 13
HELIX 15 15 ASN B 164 GLY B 168 5 5
HELIX 16 16 TRP B 172 ILE B 185 1 14
SHEET 1 A 6 GLN A 45 ARG A 46 0
SHEET 2 A 6 THR A 18 VAL A 22 1 N MSE A 19 O GLN A 45
SHEET 3 A 6 VAL A 75 HIS A 80 1 O ILE A 78 N VAL A 22
SHEET 4 A 6 ILE A 98 VAL A 104 1 O MSE A 102 N LEU A 77
SHEET 5 A 6 THR A 127 ALA A 131 1 O LEU A 128 N LEU A 103
SHEET 6 A 6 GLU A 153 ASP A 156 1 O VAL A 155 N THR A 129
SHEET 1 B 6 GLN B 45 ARG B 46 0
SHEET 2 B 6 THR B 18 VAL B 22 1 N MSE B 19 O GLN B 45
SHEET 3 B 6 VAL B 75 HIS B 80 1 O ILE B 78 N VAL B 22
SHEET 4 B 6 ILE B 98 VAL B 104 1 O MSE B 102 N LEU B 77
SHEET 5 B 6 THR B 127 ALA B 131 1 O LEU B 128 N LEU B 103
SHEET 6 B 6 GLU B 153 ASP B 156 1 O VAL B 155 N THR B 129
LINK O ARG A 46 CA CA A 191 1555 1555 2.44
LINK OE1 GLU A 67 CA CA A 191 1555 1555 2.53
LINK OE2 GLU A 67 CA CA A 191 1555 1555 2.56
LINK O ILE A 185 CA CA B 191 1555 1555 2.37
LINK OD2 ASP B 151 CA CA B 191 1555 1555 2.47
LINK CA CA A 192 O2 EDO A 194 1555 1555 2.51
LINK CA CA A 192 O1 EDO A 194 1555 1555 2.52
LINK CA CA B 191 O1 EDO A 195 1555 1555 2.41
LINK CA CA B 191 O2 EDO A 195 1555 1555 2.24
LINK CA CA A 191 O HOH A 268 1555 1555 2.44
LINK CA CA A 191 O HOH A 342 1555 1555 2.27
LINK CA CA A 191 O HOH A 239 1555 1555 2.37
LINK CA CA A 192 O BHOH A 367 1555 1555 2.88
LINK CA CA A 192 O HOH A 285 1555 1555 2.34
LINK CA CA A 192 O HOH A 313 1555 1555 2.32
LINK CA CA A 192 O HOH A 265 1555 1555 2.40
LINK CA CA B 191 O HOH A 242 1555 1555 2.39
LINK CA CA B 191 O HOH B 248 1555 1555 2.46
CISPEP 1 PHE A 169 GLY A 170 0 10.63
CISPEP 2 PHE B 169 GLY B 170 0 15.04
CRYST1 35.655 93.302 104.095 90.00 90.00 90.00 P 21 21 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 0.028047 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009607 0.00000
TER 1571 ARG A 190
TER 3126 PRO B 188
MASTER 386 0 18 16 12 0 0 6 3445 2 128 30
END |