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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-SEP-07 2R8B
TITLE THE CRYSTAL STRUCTURE OF THE PROTEIN ATU2452 OF UNKNOWN
TITLE 2 FUNCTION FROM AGROBACTERIUM TUMEFACIENS STR. C58
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN ATU2452;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AGR_C_4453P;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS STR. C58;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 STRAIN: C58;
SOURCE 5 ATCC: 33970;
SOURCE 6 GENE: AGR_C_4453, ATU2452;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS APC6088, PROTEIN ATU2452, AGROBACTERIUM TUMEFACIENS STR.
KEYWDS 2 C58, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 4 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 5 17-MAR-09 2R8B 1 JRNL
REVDAT 4 24-FEB-09 2R8B 1 VERSN
REVDAT 3 10-JUN-08 2R8B 1 JRNL
REVDAT 2 20-NOV-07 2R8B 1 JRNL
REVDAT 1 25-SEP-07 2R8B 0
JRNL AUTH K.TAN,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF THE PROTEIN ATU2452 OF
JRNL TITL 2 UNKNOWN FUNCTION FROM AGROBACTERIUM TUMEFACIENS
JRNL TITL 3 STR. C58.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.56 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) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 16991
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 924
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) : 2.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 690
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 31
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : 1.11000
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): 0.435
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.289
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.249
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.219
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
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): 3192 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4326 ; 1.908 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 406 ; 7.742 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;38.584 ;23.239
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 500 ;22.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;27.195 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 468 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2464 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1415 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2159 ; 0.330 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 118 ; 0.159 ; 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): 41 ; 0.274 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.042 ; 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): 2051 ; 0.670 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3228 ; 1.175 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1242 ; 2.108 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1098 ; 3.354 ; 4.500
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 : 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 43 A 245
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3570 39.1790 4.6780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: 0.0198
REMARK 3 T33: -0.1943 T12: -0.1012
REMARK 3 T13: 0.0440 T23: -0.0967
REMARK 3 L TENSOR
REMARK 3 L11: 3.9040 L22: 4.7491
REMARK 3 L33: 6.3186 L12: -1.7625
REMARK 3 L13: -1.5171 L23: 3.9394
REMARK 3 S TENSOR
REMARK 3 S11: -0.2007 S12: 0.0527 S13: -0.4614
REMARK 3 S21: -0.1894 S22: 0.0490 S23: 0.2010
REMARK 3 S31: 0.0805 S32: 0.1583 S33: 0.1517
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 43 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9380 53.3850 36.5700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: -0.0185
REMARK 3 T33: -0.2016 T12: -0.0876
REMARK 3 T13: 0.1120 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 4.7232 L22: 3.5209
REMARK 3 L33: 6.7586 L12: -1.7414
REMARK 3 L13: -3.5588 L23: 1.7442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: -0.2010 S13: -0.1985
REMARK 3 S21: 0.1542 S22: -0.1750 S23: 0.4664
REMARK 3 S31: -0.1595 S32: -0.1689 S33: 0.1546
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY
REMARK 4
REMARK 4 2R8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-07.
REMARK 100 THE RCSB ID CODE IS RCSB044550.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 82.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE, DM, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE, 0.2M K/NA
REMARK 280 TARTRATE, 2.0M AMMONIUM SULFATE, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.45200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.57750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.36350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.57750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.45200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.36350
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/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: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS EXPERIMENTALLY
REMARK 300 UNKNOWN. FROM MOLECULAR PACKING, IT SEEMS TO BE MONOMERIC.
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: 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 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 LEU A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLY A 9
REMARK 465 GLU A 10
REMARK 465 GLU A 11
REMARK 465 THR A 12
REMARK 465 SER A 13
REMARK 465 GLY A 14
REMARK 465 ALA A 15
REMARK 465 ARG A 16
REMARK 465 SER A 17
REMARK 465 LEU A 18
REMARK 465 HIS A 19
REMARK 465 GLU A 20
REMARK 465 ILE A 21
REMARK 465 ALA A 22
REMARK 465 PRO A 23
REMARK 465 PRO A 24
REMARK 465 ALA A 25
REMARK 465 GLU A 26
REMARK 465 LYS A 27
REMARK 465 ALA A 28
REMARK 465 VAL A 29
REMARK 465 ARG A 30
REMARK 465 LYS A 31
REMARK 465 PRO A 32
REMARK 465 LEU A 33
REMARK 465 ASN A 34
REMARK 465 LEU A 35
REMARK 465 LEU A 36
REMARK 465 PRO A 37
REMARK 465 PHE A 38
REMARK 465 ARG A 39
REMARK 465 LYS A 40
REMARK 465 ASP A 41
REMARK 465 THR A 42
REMARK 465 GLY A 247
REMARK 465 GLY A 248
REMARK 465 SER A 249
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 LEU B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 GLY B 9
REMARK 465 GLU B 10
REMARK 465 GLU B 11
REMARK 465 THR B 12
REMARK 465 SER B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 ARG B 16
REMARK 465 SER B 17
REMARK 465 LEU B 18
REMARK 465 HIS B 19
REMARK 465 GLU B 20
REMARK 465 ILE B 21
REMARK 465 ALA B 22
REMARK 465 PRO B 23
REMARK 465 PRO B 24
REMARK 465 ALA B 25
REMARK 465 GLU B 26
REMARK 465 LYS B 27
REMARK 465 ALA B 28
REMARK 465 VAL B 29
REMARK 465 ARG B 30
REMARK 465 LYS B 31
REMARK 465 PRO B 32
REMARK 465 LEU B 33
REMARK 465 ASN B 34
REMARK 465 LEU B 35
REMARK 465 LEU B 36
REMARK 465 PRO B 37
REMARK 465 PHE B 38
REMARK 465 ARG B 39
REMARK 465 LYS B 40
REMARK 465 ASP B 41
REMARK 465 THR B 42
REMARK 465 GLY B 247
REMARK 465 GLY B 248
REMARK 465 SER B 249
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 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH2 ANGL. DEV. = -3.9 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 ASP A 72 -160.40 -166.89
REMARK 500 HIS A 99 85.10 17.12
REMARK 500 SER A 147 -114.05 58.70
REMARK 500 PRO A 225 -178.35 -67.36
REMARK 500 HIS B 99 87.11 21.98
REMARK 500 SER B 147 -111.15 53.04
REMARK 500 ALA B 244 -29.78 -35.30
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 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: (11X,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 THR A 45 24.3 L L OUTSIDE RANGE
REMARK 500 VAL A 189 22.9 L L OUTSIDE RANGE
REMARK 500 THR B 45 24.7 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 SO4 A 250
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 250
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC6088 RELATED DB: TARGETDB
DBREF 2R8B A 1 247 UNP Q8UCN1 Q8UCN1_AGRT5 1 247
DBREF 2R8B B 1 247 UNP Q8UCN1 Q8UCN1_AGRT5 1 247
SEQADV 2R8B GLY A -1 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B HIS A 0 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B GLY A 248 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B SER A 249 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B GLY B -1 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B HIS B 0 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B GLY B 248 UNP Q8UCN1 EXPRESSION TAG
SEQADV 2R8B SER B 249 UNP Q8UCN1 EXPRESSION TAG
SEQRES 1 A 251 GLY HIS MSE PRO ARG PRO SER LEU ARG ARG GLY GLU GLU
SEQRES 2 A 251 THR SER GLY ALA ARG SER LEU HIS GLU ILE ALA PRO PRO
SEQRES 3 A 251 ALA GLU LYS ALA VAL ARG LYS PRO LEU ASN LEU LEU PRO
SEQRES 4 A 251 PHE ARG LYS ASP THR PRO MSE THR LYS ASP SER TYR PHE
SEQRES 5 A 251 HIS LYS SER ARG ALA GLY VAL ALA GLY ALA PRO LEU PHE
SEQRES 6 A 251 VAL LEU LEU HIS GLY THR GLY GLY ASP GLU ASN GLN PHE
SEQRES 7 A 251 PHE ASP PHE GLY ALA ARG LEU LEU PRO GLN ALA THR ILE
SEQRES 8 A 251 LEU SER PRO VAL GLY ASP VAL SER GLU HIS GLY ALA ALA
SEQRES 9 A 251 ARG PHE PHE ARG ARG THR GLY GLU GLY VAL TYR ASP MSE
SEQRES 10 A 251 VAL ASP LEU GLU ARG ALA THR GLY LYS MSE ALA ASP PHE
SEQRES 11 A 251 ILE LYS ALA ASN ARG GLU HIS TYR GLN ALA GLY PRO VAL
SEQRES 12 A 251 ILE GLY LEU GLY PHE SER ASN GLY ALA ASN ILE LEU ALA
SEQRES 13 A 251 ASN VAL LEU ILE GLU GLN PRO GLU LEU PHE ASP ALA ALA
SEQRES 14 A 251 VAL LEU MSE HIS PRO LEU ILE PRO PHE GLU PRO LYS ILE
SEQRES 15 A 251 SER PRO ALA LYS PRO THR ARG ARG VAL LEU ILE THR ALA
SEQRES 16 A 251 GLY GLU ARG ASP PRO ILE CYS PRO VAL GLN LEU THR LYS
SEQRES 17 A 251 ALA LEU GLU GLU SER LEU LYS ALA GLN GLY GLY THR VAL
SEQRES 18 A 251 GLU THR VAL TRP HIS PRO GLY GLY HIS GLU ILE ARG SER
SEQRES 19 A 251 GLY GLU ILE ASP ALA VAL ARG GLY PHE LEU ALA ALA TYR
SEQRES 20 A 251 GLY GLY GLY SER
SEQRES 1 B 251 GLY HIS MSE PRO ARG PRO SER LEU ARG ARG GLY GLU GLU
SEQRES 2 B 251 THR SER GLY ALA ARG SER LEU HIS GLU ILE ALA PRO PRO
SEQRES 3 B 251 ALA GLU LYS ALA VAL ARG LYS PRO LEU ASN LEU LEU PRO
SEQRES 4 B 251 PHE ARG LYS ASP THR PRO MSE THR LYS ASP SER TYR PHE
SEQRES 5 B 251 HIS LYS SER ARG ALA GLY VAL ALA GLY ALA PRO LEU PHE
SEQRES 6 B 251 VAL LEU LEU HIS GLY THR GLY GLY ASP GLU ASN GLN PHE
SEQRES 7 B 251 PHE ASP PHE GLY ALA ARG LEU LEU PRO GLN ALA THR ILE
SEQRES 8 B 251 LEU SER PRO VAL GLY ASP VAL SER GLU HIS GLY ALA ALA
SEQRES 9 B 251 ARG PHE PHE ARG ARG THR GLY GLU GLY VAL TYR ASP MSE
SEQRES 10 B 251 VAL ASP LEU GLU ARG ALA THR GLY LYS MSE ALA ASP PHE
SEQRES 11 B 251 ILE LYS ALA ASN ARG GLU HIS TYR GLN ALA GLY PRO VAL
SEQRES 12 B 251 ILE GLY LEU GLY PHE SER ASN GLY ALA ASN ILE LEU ALA
SEQRES 13 B 251 ASN VAL LEU ILE GLU GLN PRO GLU LEU PHE ASP ALA ALA
SEQRES 14 B 251 VAL LEU MSE HIS PRO LEU ILE PRO PHE GLU PRO LYS ILE
SEQRES 15 B 251 SER PRO ALA LYS PRO THR ARG ARG VAL LEU ILE THR ALA
SEQRES 16 B 251 GLY GLU ARG ASP PRO ILE CYS PRO VAL GLN LEU THR LYS
SEQRES 17 B 251 ALA LEU GLU GLU SER LEU LYS ALA GLN GLY GLY THR VAL
SEQRES 18 B 251 GLU THR VAL TRP HIS PRO GLY GLY HIS GLU ILE ARG SER
SEQRES 19 B 251 GLY GLU ILE ASP ALA VAL ARG GLY PHE LEU ALA ALA TYR
SEQRES 20 B 251 GLY GLY GLY SER
MODRES 2R8B MSE A 44 MET SELENOMETHIONINE
MODRES 2R8B MSE A 115 MET SELENOMETHIONINE
MODRES 2R8B MSE A 125 MET SELENOMETHIONINE
MODRES 2R8B MSE A 170 MET SELENOMETHIONINE
MODRES 2R8B MSE B 44 MET SELENOMETHIONINE
MODRES 2R8B MSE B 115 MET SELENOMETHIONINE
MODRES 2R8B MSE B 125 MET SELENOMETHIONINE
MODRES 2R8B MSE B 170 MET SELENOMETHIONINE
HET MSE A 44 8
HET MSE A 115 8
HET MSE A 125 8
HET MSE A 170 8
HET MSE B 44 8
HET MSE B 115 8
HET MSE B 125 8
HET MSE B 170 8
HET SO4 A 250 5
HET SO4 B 250 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *17(H2 O)
HELIX 1 1 PHE A 76 LEU A 84 1 9
HELIX 2 2 THR A 108 VAL A 112 5 5
HELIX 3 3 ASP A 114 GLN A 137 1 24
HELIX 4 4 SER A 147 GLN A 160 1 14
HELIX 5 5 PRO A 201 GLY A 216 1 16
HELIX 6 6 ARG A 231 ALA A 243 1 13
HELIX 7 7 ALA A 244 GLY A 246 5 3
HELIX 8 8 MSE B 44 SER B 48 5 5
HELIX 9 9 PHE B 76 ARG B 82 1 7
HELIX 10 10 ASP B 114 GLN B 137 1 24
HELIX 11 11 SER B 147 GLN B 160 1 14
HELIX 12 12 PRO B 201 GLY B 216 1 16
HELIX 13 13 ARG B 231 LEU B 242 1 12
HELIX 14 14 ALA B 243 GLY B 246 5 4
SHEET 1 A 7 HIS A 51 ARG A 54 0
SHEET 2 A 7 THR A 88 PRO A 92 -1 O SER A 91 N LYS A 52
SHEET 3 A 7 LEU A 62 LEU A 66 1 N PHE A 63 O THR A 88
SHEET 4 A 7 VAL A 141 PHE A 146 1 O ILE A 142 N LEU A 62
SHEET 5 A 7 ALA A 166 MSE A 170 1 O MSE A 170 N GLY A 145
SHEET 6 A 7 ARG A 188 GLY A 194 1 O LEU A 190 N LEU A 169
SHEET 7 A 7 THR A 218 HIS A 224 1 O GLU A 220 N ILE A 191
SHEET 1 B 2 VAL A 96 GLU A 98 0
SHEET 2 B 2 ALA A 101 ARG A 103 -1 O ALA A 101 N GLU A 98
SHEET 1 C 7 HIS B 51 ARG B 54 0
SHEET 2 C 7 THR B 88 PRO B 92 -1 O SER B 91 N LYS B 52
SHEET 3 C 7 LEU B 62 LEU B 66 1 N PHE B 63 O THR B 88
SHEET 4 C 7 VAL B 141 PHE B 146 1 O ILE B 142 N LEU B 62
SHEET 5 C 7 ALA B 166 MSE B 170 1 O MSE B 170 N GLY B 145
SHEET 6 C 7 ARG B 188 GLY B 194 1 O LEU B 190 N LEU B 169
SHEET 7 C 7 THR B 218 HIS B 224 1 O GLU B 220 N ILE B 191
SHEET 1 D 2 VAL B 96 GLU B 98 0
SHEET 2 D 2 ALA B 101 ARG B 103 -1 O ARG B 103 N VAL B 96
LINK C PRO A 43 N MSE A 44 1555 1555 1.34
LINK C MSE A 44 N THR A 45 1555 1555 1.33
LINK C ASP A 114 N MSE A 115 1555 1555 1.34
LINK C MSE A 115 N VAL A 116 1555 1555 1.34
LINK C LYS A 124 N MSE A 125 1555 1555 1.34
LINK C MSE A 125 N ALA A 126 1555 1555 1.33
LINK C LEU A 169 N MSE A 170 1555 1555 1.32
LINK C MSE A 170 N HIS A 171 1555 1555 1.33
LINK C PRO B 43 N MSE B 44 1555 1555 1.35
LINK C MSE B 44 N THR B 45 1555 1555 1.33
LINK C ASP B 114 N MSE B 115 1555 1555 1.33
LINK C MSE B 115 N VAL B 116 1555 1555 1.34
LINK C LYS B 124 N MSE B 125 1555 1555 1.33
LINK C MSE B 125 N ALA B 126 1555 1555 1.33
LINK C LEU B 169 N MSE B 170 1555 1555 1.32
LINK C MSE B 170 N HIS B 171 1555 1555 1.33
SITE 1 AC1 6 THR A 69 ARG A 103 PHE A 105 TYR A 113
SITE 2 AC1 6 ASN A 148 ASN A 151
SITE 1 AC2 5 ARG B 103 PHE B 105 TYR B 113 ASN B 148
SITE 2 AC2 5 ASN B 151
CRYST1 58.904 58.727 165.155 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 0.016977 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006055 0.00000
TER 1555 GLY A 246
TER 3110 GLY B 246
MASTER 451 0 10 14 18 0 4 6 3135 2 90 40
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