HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-AUG-08 3E5Z
TITLE X-RAY STRUCTURE OF THE PUTATIVE GLUCONOLACTONASE IN PROTEIN FAMILY
TITLE 2 PF08450. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET DRR130.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE GLUCONOLACTONASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DR_0277;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 21-23C
KEYWDS X-RAY NESG Q9RXN3 GLUCONOLACTONASE, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.KUZIN,M.ABASHIDZE,J.SEETHARAMAN,D.WANG,L.MAO,M.MAGLAQUI,R.XIAO,
AUTHOR 2 J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,S.N.TONG,G.T.MONTELIONE,L.TONG,
AUTHOR 3 J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 25-OCT-17 3E5Z 1 REMARK
REVDAT 3 13-JUL-11 3E5Z 1 VERSN
REVDAT 2 24-FEB-09 3E5Z 1 VERSN
REVDAT 1 30-SEP-08 3E5Z 0
JRNL AUTH A.P.KUZIN,M.ABASHIDZE,J.SEETHARAMAN,D.WANG,L.MAO,M.MAGLAQUI,
JRNL AUTH 2 R.XIAO,J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,S.N.TONG,
JRNL AUTH 3 G.T.MONTELIONE,L.TONG,J.F.HUNT
JRNL TITL X-RAY STRUCTURE OF THE PUTATIVE GLUCONOLACTONASE IN PROTEIN
JRNL TITL 2 FAMILY PF08450. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
JRNL TITL 3 TARGET DRR130.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35195
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1867
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2029
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 239
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.69000
REMARK 3 B22 (A**2) : -2.50000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.885
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4616 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6284 ; 1.301 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 578 ; 6.238 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;31.528 ;23.246
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 690 ;13.881 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.457 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 652 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3684 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1978 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3076 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 276 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 39 ; 0.272 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.108 ; 0.200
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): 2942 ; 0.754 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4598 ; 1.118 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1916 ; 1.692 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1686 ; 2.642 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 298 B 429
REMARK 3 RESIDUE RANGE : A 298 A 404
REMARK 3 RESIDUE RANGE : B 297 B 297
REMARK 3 RESIDUE RANGE : A 297 A 297
REMARK 3 RESIDUE RANGE : B 2 B 291
REMARK 3 RESIDUE RANGE : A 2 A 291
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9275 50.1732 56.7859
REMARK 3 T TENSOR
REMARK 3 T11: -0.1250 T22: -0.0158
REMARK 3 T33: -0.0795 T12: -0.0064
REMARK 3 T13: -0.0103 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 0.1144 L22: 2.0537
REMARK 3 L33: 0.7122 L12: -0.1485
REMARK 3 L13: -0.0788 L23: 1.0589
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: -0.0001 S13: -0.0028
REMARK 3 S21: -0.0034 S22: -0.0343 S23: 0.0306
REMARK 3 S31: -0.0578 S32: -0.0281 S33: 0.0178
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: NULL
REMARK 4
REMARK 4 3E5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048917.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81184
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NACL 0.1M TOPS 18% PEG 3350, MGL2
REMARK 280 AS ADDITIVE, PH 9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.70000
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 1
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 MSE B 1
REMARK 465 HIS B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
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 LEU A 223 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU B 223 CA - CB - CG ANGL. DEV. = 14.9 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 GLU A 64 -62.27 -104.11
REMARK 500 ASN A 72 -97.47 -123.53
REMARK 500 SER A 116 88.17 174.45
REMARK 500 ASN A 175 -89.21 -139.52
REMARK 500 ASN A 201 37.06 -73.17
REMARK 500 ALA A 202 134.71 68.44
REMARK 500 ASP A 221 -92.40 -99.23
REMARK 500 VAL A 275 66.28 -113.72
REMARK 500 SER A 276 -105.70 64.87
REMARK 500 GLU B 64 -63.00 -101.92
REMARK 500 ASN B 72 -98.57 -125.11
REMARK 500 ASN B 115 -72.54 -69.88
REMARK 500 SER B 116 92.08 175.99
REMARK 500 PRO B 133 -167.76 -79.65
REMARK 500 ASN B 175 -89.20 -139.12
REMARK 500 ASN B 201 -155.59 -85.98
REMARK 500 ALA B 202 79.50 -62.61
REMARK 500 ARG B 203 -9.73 57.09
REMARK 500 GLU B 205 -157.41 -78.05
REMARK 500 ASP B 221 -94.50 -90.84
REMARK 500 VAL B 275 73.43 -113.46
REMARK 500 SER B 276 -103.31 54.95
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 MG A 297 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 118 OD1
REMARK 620 2 ASN A 175 OD1 77.5
REMARK 620 3 ASP A 221 OD1 146.7 74.4
REMARK 620 4 HOH A 331 O 106.3 76.7 84.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 297 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 118 OD1
REMARK 620 2 ASN B 175 OD1 80.0
REMARK 620 3 ASP B 221 OD1 156.5 80.1
REMARK 620 4 HOH B 418 O 81.1 86.4 85.4
REMARK 620 5 HOH B 382 O 69.2 126.3 133.7 128.2
REMARK 620 6 HOH B 328 O 111.1 76.9 76.2 156.9 74.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 297
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: DRR130 RELATED DB: TARGETDB
DBREF 3E5Z A 1 288 UNP Q9RXN3 Q9RXN3_DEIRA 1 288
DBREF 3E5Z B 1 288 UNP Q9RXN3 Q9RXN3_DEIRA 1 288
SEQADV 3E5Z LEU A 289 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z GLU A 290 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 291 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 292 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 293 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 294 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 295 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS A 296 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z LEU B 289 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z GLU B 290 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 291 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 292 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 293 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 294 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 295 UNP Q9RXN3 EXPRESSION TAG
SEQADV 3E5Z HIS B 296 UNP Q9RXN3 EXPRESSION TAG
SEQRES 1 A 296 MSE THR LEU ARG ALA ALA ARG PRO GLU PHE LEU ASP LEU
SEQRES 2 A 296 PHE PRO ALA GLY ALA GLU ALA ARG ARG LEU ALA ASP GLY
SEQRES 3 A 296 PHE THR TRP THR GLU GLY PRO VAL TYR VAL PRO ALA ARG
SEQRES 4 A 296 SER ALA VAL ILE PHE SER ASP VAL ARG GLN ASN ARG THR
SEQRES 5 A 296 TRP ALA TRP SER ASP ASP GLY GLN LEU SER PRO GLU MSE
SEQRES 6 A 296 HIS PRO SER HIS HIS GLN ASN GLY HIS CYS LEU ASN LYS
SEQRES 7 A 296 GLN GLY HIS LEU ILE ALA CYS SER HIS GLY LEU ARG ARG
SEQRES 8 A 296 LEU GLU ARG GLN ARG GLU PRO GLY GLY GLU TRP GLU SER
SEQRES 9 A 296 ILE ALA ASP SER PHE GLU GLY LYS LYS LEU ASN SER PRO
SEQRES 10 A 296 ASN ASP VAL CYS LEU ALA PRO ASP GLY SER LEU TRP PHE
SEQRES 11 A 296 SER ASP PRO THR TYR GLY ILE ASP LYS PRO GLU GLU GLY
SEQRES 12 A 296 TYR GLY GLY GLU MSE GLU LEU PRO GLY ARG TRP VAL PHE
SEQRES 13 A 296 ARG LEU ALA PRO ASP GLY THR LEU SER ALA PRO ILE ARG
SEQRES 14 A 296 ASP ARG VAL LYS PRO ASN GLY LEU ALA PHE LEU PRO SER
SEQRES 15 A 296 GLY ASN LEU LEU VAL SER ASP THR GLY ASP ASN ALA THR
SEQRES 16 A 296 HIS ARG TYR CYS LEU ASN ALA ARG GLY GLU THR GLU TYR
SEQRES 17 A 296 GLN GLY VAL HIS PHE THR VAL GLU PRO GLY LYS THR ASP
SEQRES 18 A 296 GLY LEU ARG VAL ASP ALA GLY GLY LEU ILE TRP ALA SER
SEQRES 19 A 296 ALA GLY ASP GLY VAL HIS VAL LEU THR PRO ASP GLY ASP
SEQRES 20 A 296 GLU LEU GLY ARG VAL LEU THR PRO GLN THR THR SER ASN
SEQRES 21 A 296 LEU CYS PHE GLY GLY PRO GLU GLY ARG THR LEU TYR MSE
SEQRES 22 A 296 THR VAL SER THR GLU PHE TRP SER ILE GLU THR ASN VAL
SEQRES 23 A 296 ARG GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 296 MSE THR LEU ARG ALA ALA ARG PRO GLU PHE LEU ASP LEU
SEQRES 2 B 296 PHE PRO ALA GLY ALA GLU ALA ARG ARG LEU ALA ASP GLY
SEQRES 3 B 296 PHE THR TRP THR GLU GLY PRO VAL TYR VAL PRO ALA ARG
SEQRES 4 B 296 SER ALA VAL ILE PHE SER ASP VAL ARG GLN ASN ARG THR
SEQRES 5 B 296 TRP ALA TRP SER ASP ASP GLY GLN LEU SER PRO GLU MSE
SEQRES 6 B 296 HIS PRO SER HIS HIS GLN ASN GLY HIS CYS LEU ASN LYS
SEQRES 7 B 296 GLN GLY HIS LEU ILE ALA CYS SER HIS GLY LEU ARG ARG
SEQRES 8 B 296 LEU GLU ARG GLN ARG GLU PRO GLY GLY GLU TRP GLU SER
SEQRES 9 B 296 ILE ALA ASP SER PHE GLU GLY LYS LYS LEU ASN SER PRO
SEQRES 10 B 296 ASN ASP VAL CYS LEU ALA PRO ASP GLY SER LEU TRP PHE
SEQRES 11 B 296 SER ASP PRO THR TYR GLY ILE ASP LYS PRO GLU GLU GLY
SEQRES 12 B 296 TYR GLY GLY GLU MSE GLU LEU PRO GLY ARG TRP VAL PHE
SEQRES 13 B 296 ARG LEU ALA PRO ASP GLY THR LEU SER ALA PRO ILE ARG
SEQRES 14 B 296 ASP ARG VAL LYS PRO ASN GLY LEU ALA PHE LEU PRO SER
SEQRES 15 B 296 GLY ASN LEU LEU VAL SER ASP THR GLY ASP ASN ALA THR
SEQRES 16 B 296 HIS ARG TYR CYS LEU ASN ALA ARG GLY GLU THR GLU TYR
SEQRES 17 B 296 GLN GLY VAL HIS PHE THR VAL GLU PRO GLY LYS THR ASP
SEQRES 18 B 296 GLY LEU ARG VAL ASP ALA GLY GLY LEU ILE TRP ALA SER
SEQRES 19 B 296 ALA GLY ASP GLY VAL HIS VAL LEU THR PRO ASP GLY ASP
SEQRES 20 B 296 GLU LEU GLY ARG VAL LEU THR PRO GLN THR THR SER ASN
SEQRES 21 B 296 LEU CYS PHE GLY GLY PRO GLU GLY ARG THR LEU TYR MSE
SEQRES 22 B 296 THR VAL SER THR GLU PHE TRP SER ILE GLU THR ASN VAL
SEQRES 23 B 296 ARG GLY LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3E5Z MSE A 65 MET SELENOMETHIONINE
MODRES 3E5Z MSE A 148 MET SELENOMETHIONINE
MODRES 3E5Z MSE A 273 MET SELENOMETHIONINE
MODRES 3E5Z MSE B 65 MET SELENOMETHIONINE
MODRES 3E5Z MSE B 148 MET SELENOMETHIONINE
MODRES 3E5Z MSE B 273 MET SELENOMETHIONINE
HET MSE A 65 8
HET MSE A 148 8
HET MSE A 273 8
HET MSE B 65 8
HET MSE B 148 8
HET MSE B 273 8
HET MG A 297 1
HET MG B 297 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *239(H2 O)
HELIX 1 1 ARG A 7 PHE A 14 5 8
HELIX 2 2 PRO A 37 ARG A 39 5 3
HELIX 3 3 ARG A 48 ASN A 50 5 3
HELIX 4 4 THR A 134 LYS A 139 1 6
HELIX 5 5 PRO A 140 GLY A 143 5 4
HELIX 6 6 ARG B 7 PHE B 14 5 8
HELIX 7 7 PRO B 37 ARG B 39 5 3
HELIX 8 8 THR B 134 LYS B 139 1 6
HELIX 9 9 PRO B 140 GLY B 143 5 4
SHEET 1 A 5 LEU A 3 ALA A 5 0
SHEET 2 A 5 GLU A 248 LEU A 253 -1 O ARG A 251 N ARG A 4
SHEET 3 A 5 GLY A 238 LEU A 242 -1 N VAL A 241 O LEU A 249
SHEET 4 A 5 ILE A 231 ALA A 235 -1 N ALA A 233 O HIS A 240
SHEET 5 A 5 LEU A 223 VAL A 225 -1 N ARG A 224 O TRP A 232
SHEET 1 B 4 ARG A 21 ALA A 24 0
SHEET 2 B 4 GLU A 278 GLU A 283 -1 O PHE A 279 N LEU A 23
SHEET 3 B 4 THR A 270 VAL A 275 -1 N MSE A 273 O TRP A 280
SHEET 4 B 4 ASN A 260 GLY A 264 -1 N CYS A 262 O TYR A 272
SHEET 1 C 4 THR A 30 VAL A 36 0
SHEET 2 C 4 ALA A 41 ASP A 46 -1 O ALA A 41 N VAL A 36
SHEET 3 C 4 ARG A 51 SER A 56 -1 O TRP A 53 N PHE A 44
SHEET 4 C 4 LEU A 61 MSE A 65 -1 O SER A 62 N ALA A 54
SHEET 1 D 4 GLN A 71 LEU A 76 0
SHEET 2 D 4 LEU A 82 SER A 86 -1 O ILE A 83 N CYS A 75
SHEET 3 D 4 ARG A 91 GLN A 95 -1 O GLN A 95 N LEU A 82
SHEET 4 D 4 TRP A 102 ALA A 106 -1 O ILE A 105 N LEU A 92
SHEET 1 E 2 SER A 108 PHE A 109 0
SHEET 2 E 2 LYS A 112 LYS A 113 -1 O LYS A 112 N PHE A 109
SHEET 1 F 4 VAL A 120 LEU A 122 0
SHEET 2 F 4 LEU A 128 ASP A 132 -1 O TRP A 129 N CYS A 121
SHEET 3 F 4 TRP A 154 LEU A 158 -1 O PHE A 156 N PHE A 130
SHEET 4 F 4 LEU A 164 ILE A 168 -1 O SER A 165 N ARG A 157
SHEET 1 G 4 PRO A 174 PHE A 179 0
SHEET 2 G 4 LEU A 185 ASP A 189 -1 O SER A 188 N ASN A 175
SHEET 3 G 4 ALA A 194 LEU A 200 -1 O HIS A 196 N VAL A 187
SHEET 4 G 4 THR A 206 PHE A 213 -1 O GLN A 209 N ARG A 197
SHEET 1 H 5 LEU B 3 ALA B 5 0
SHEET 2 H 5 GLU B 248 LEU B 253 -1 O ARG B 251 N ARG B 4
SHEET 3 H 5 GLY B 238 LEU B 242 -1 N VAL B 241 O GLY B 250
SHEET 4 H 5 ILE B 231 ALA B 235 -1 N ALA B 233 O HIS B 240
SHEET 5 H 5 LEU B 223 VAL B 225 -1 N ARG B 224 O TRP B 232
SHEET 1 I 4 ARG B 21 ALA B 24 0
SHEET 2 I 4 GLU B 278 GLU B 283 -1 O PHE B 279 N LEU B 23
SHEET 3 I 4 THR B 270 VAL B 275 -1 N MSE B 273 O TRP B 280
SHEET 4 I 4 ASN B 260 GLY B 264 -1 N CYS B 262 O TYR B 272
SHEET 1 J 4 THR B 30 VAL B 36 0
SHEET 2 J 4 ALA B 41 ASP B 46 -1 O SER B 45 N GLU B 31
SHEET 3 J 4 ARG B 51 SER B 56 -1 O ARG B 51 N ASP B 46
SHEET 4 J 4 LEU B 61 MSE B 65 -1 O SER B 62 N ALA B 54
SHEET 1 K 4 GLN B 71 LEU B 76 0
SHEET 2 K 4 LEU B 82 SER B 86 -1 O ILE B 83 N CYS B 75
SHEET 3 K 4 ARG B 91 GLN B 95 -1 O GLN B 95 N LEU B 82
SHEET 4 K 4 GLU B 103 ALA B 106 -1 O ILE B 105 N LEU B 92
SHEET 1 L 2 SER B 108 PHE B 109 0
SHEET 2 L 2 LYS B 112 LYS B 113 -1 O LYS B 112 N PHE B 109
SHEET 1 M 4 VAL B 120 LEU B 122 0
SHEET 2 M 4 LEU B 128 SER B 131 -1 O TRP B 129 N CYS B 121
SHEET 3 M 4 VAL B 155 LEU B 158 -1 O LEU B 158 N LEU B 128
SHEET 4 M 4 LEU B 164 ILE B 168 -1 O SER B 165 N ARG B 157
SHEET 1 N 4 PRO B 174 PHE B 179 0
SHEET 2 N 4 LEU B 185 ASP B 189 -1 O LEU B 186 N ALA B 178
SHEET 3 N 4 ALA B 194 LEU B 200 -1 O HIS B 196 N VAL B 187
SHEET 4 N 4 THR B 206 PHE B 213 -1 O GLN B 209 N ARG B 197
SSBOND 1 CYS A 199 CYS B 199 1555 1565 2.54
LINK C GLU A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N HIS A 66 1555 1555 1.33
LINK C GLU A 147 N MSE A 148 1555 1555 1.32
LINK C MSE A 148 N GLU A 149 1555 1555 1.33
LINK C TYR A 272 N MSE A 273 1555 1555 1.33
LINK C MSE A 273 N THR A 274 1555 1555 1.33
LINK C GLU B 64 N MSE B 65 1555 1555 1.32
LINK C MSE B 65 N HIS B 66 1555 1555 1.33
LINK C GLU B 147 N MSE B 148 1555 1555 1.32
LINK C MSE B 148 N GLU B 149 1555 1555 1.33
LINK C TYR B 272 N MSE B 273 1555 1555 1.33
LINK C MSE B 273 N THR B 274 1555 1555 1.33
LINK OD1 ASN A 118 MG MG A 297 1555 1555 2.33
LINK OD1 ASN A 175 MG MG A 297 1555 1555 2.25
LINK OD1 ASP A 221 MG MG A 297 1555 1555 2.20
LINK OD1 ASN B 118 MG MG B 297 1555 1555 2.38
LINK OD1 ASN B 175 MG MG B 297 1555 1555 2.20
LINK OD1 ASP B 221 MG MG B 297 1555 1555 2.22
LINK MG MG A 297 O HOH A 331 1555 1555 2.32
LINK MG MG B 297 O HOH B 418 1555 1555 2.47
LINK MG MG B 297 O HOH B 382 1555 1555 2.38
LINK MG MG B 297 O HOH B 328 1555 1555 2.28
CISPEP 1 HIS A 66 PRO A 67 0 -4.48
CISPEP 2 GLU A 216 PRO A 217 0 -5.18
CISPEP 3 HIS B 66 PRO B 67 0 -1.76
CISPEP 4 GLU B 216 PRO B 217 0 2.18
SITE 1 AC1 7 GLU A 31 ASN A 118 ASN A 175 ASP A 221
SITE 2 AC1 7 HOH A 331 HOH A 348 HOH A 369
SITE 1 AC2 7 GLU B 31 ASN B 118 ASN B 175 ASP B 221
SITE 2 AC2 7 HOH B 328 HOH B 382 HOH B 418
CRYST1 44.420 93.400 76.990 90.00 98.67 90.00 P 1 21 1 4
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 0.022512 0.000000 0.003433 0.00000
SCALE2 0.000000 0.010707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
