HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-SEP-07 2R6U
TITLE CRYSTAL STRUCTURE OF GENE PRODUCT RHA04853 FROM RHODOCOCCUS SP. RHA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 101510;
SOURCE 4 STRAIN: RHA1;
SOURCE 5 GENE: RHA04853, RHA1_RO04536;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDM68
KEYWDS STRUCTURAL GENOMICS, PSI-2, RHA04853, MCSG, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,X.XU,J.GU,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK,MIDWEST CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 4 21-FEB-24 2R6U 1 SEQADV
REVDAT 3 13-JUL-11 2R6U 1 VERSN
REVDAT 2 24-FEB-09 2R6U 1 VERSN
REVDAT 1 25-SEP-07 2R6U 0
JRNL AUTH R.ZHANG,X.XU,J.GU,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF GENE PRODUCT RHA04853 FROM
JRNL TITL 2 RHODOCOCCUS SP. RHA1.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 79299
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4173
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5208
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 276
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3875
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 667
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 16.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : -0.30000
REMARK 3 B33 (A**2) : 0.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.327
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3978 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2654 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5398 ; 1.550 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6414 ; 0.910 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 508 ; 7.404 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;36.390 ;23.690
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 600 ;12.323 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;17.290 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 575 ; 0.178 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4569 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 854 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 868 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2924 ; 0.220 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1986 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2183 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 517 ; 0.184 ; 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): 19 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.235 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.151 ; 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): 3218 ; 1.458 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1063 ; 0.237 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4039 ; 1.518 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1716 ; 2.567 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1359 ; 3.487 ; 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 : 8
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -4 A 55
REMARK 3 RESIDUE RANGE : A 56 A 125
REMARK 3 RESIDUE RANGE : B 1 B 55
REMARK 3 RESIDUE RANGE : B 56 B 125
REMARK 3 RESIDUE RANGE : C -1 C 55
REMARK 3 RESIDUE RANGE : C 56 C 124
REMARK 3 RESIDUE RANGE : D -5 D 55
REMARK 3 RESIDUE RANGE : D 56 D 125
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8770 34.2600 45.8230
REMARK 3 T TENSOR
REMARK 3 T11: -0.0593 T22: -0.0632
REMARK 3 T33: -0.0303 T12: 0.0034
REMARK 3 T13: -0.0147 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.9814 L22: 0.3909
REMARK 3 L33: 0.4409 L12: 0.0082
REMARK 3 L13: -0.1704 L23: 0.0899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: -0.0019 S13: -0.0538
REMARK 3 S21: -0.0095 S22: 0.0070 S23: 0.0394
REMARK 3 S31: 0.0011 S32: -0.0167 S33: 0.0325
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2R6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 0.97940
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
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 : 79299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 58.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA(OAC), 0.2M AMMONIUM ACETATE,
REMARK 280 30% PEG 4000, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 44.52400
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 300 REMARK: THIS PROTEIN EXISTED AS DIMER. THERE ARE TWO DIMERS IN THE
REMARK 300 ASYMMTRIC UNIT: MOL.A/MOL.C, MOL.B/MOL.D
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: 4240 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3910 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 GLY A 126
REMARK 465 SER A 127
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 PRO B 34
REMARK 465 ASP B 35
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 ARG C 125
REMARK 465 GLY C 126
REMARK 465 SER C 127
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 GLY D 126
REMARK 465 SER D 127
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CB MET D 63 O HOH D 284 1.86
REMARK 500 OE2 GLU C 81 O HOH C 279 1.91
REMARK 500 O HOH A 202 O HOH B 294 2.11
REMARK 500 O HOH A 195 O HOH A 290 2.15
REMARK 500 OG SER C 49 O HOH C 278 2.15
REMARK 500 OE2 GLU D 88 O HOH D 285 2.16
REMARK 500 CB MET B 63 O HOH B 283 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 C 4 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 4 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLY D 91 N - CA - C ANGL. DEV. = -16.3 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 37 56.39 38.24
REMARK 500 ASP D 35 -35.81 -36.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU D 90 GLY D 91 -47.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC7282 RELATED DB: TARGETDB
DBREF 2R6U A 1 125 UNP Q0S814 Q0S814_RHOSR 1 125
DBREF 2R6U B 1 125 UNP Q0S814 Q0S814_RHOSR 1 125
DBREF 2R6U C 1 125 UNP Q0S814 Q0S814_RHOSR 1 125
DBREF 2R6U D 1 125 UNP Q0S814 Q0S814_RHOSR 1 125
SEQADV 2R6U MET A -20 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY A -19 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER A -18 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER A -17 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -16 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -15 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -14 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -13 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -12 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS A -11 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER A -10 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER A -9 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY A -8 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ARG A -7 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLU A -6 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ASN A -5 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U LEU A -4 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U TYR A -3 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U PHE A -2 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLN A -1 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY A 0 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY A 126 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER A 127 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U MET B -20 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY B -19 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER B -18 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER B -17 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -16 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -15 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -14 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -13 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -12 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS B -11 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER B -10 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER B -9 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY B -8 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ARG B -7 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLU B -6 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ASN B -5 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U LEU B -4 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U TYR B -3 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U PHE B -2 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLN B -1 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY B 0 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY B 126 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER B 127 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U MET C -20 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY C -19 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER C -18 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER C -17 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -16 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -15 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -14 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -13 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -12 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS C -11 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER C -10 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER C -9 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY C -8 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ARG C -7 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLU C -6 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ASN C -5 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U LEU C -4 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U TYR C -3 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U PHE C -2 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLN C -1 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY C 0 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY C 126 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER C 127 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U MET D -20 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY D -19 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER D -18 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER D -17 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -16 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -15 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -14 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -13 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -12 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U HIS D -11 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER D -10 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER D -9 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY D -8 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ARG D -7 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLU D -6 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U ASN D -5 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U LEU D -4 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U TYR D -3 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U PHE D -2 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLN D -1 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY D 0 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U GLY D 126 UNP Q0S814 EXPRESSION TAG
SEQADV 2R6U SER D 127 UNP Q0S814 EXPRESSION TAG
SEQRES 1 A 148 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 148 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLY ARG ILE
SEQRES 3 A 148 VAL HIS PHE GLU ILE PRO PHE ASP ASP GLY ASP ARG ALA
SEQRES 4 A 148 ARG ALA PHE TYR ARG ASP ALA PHE GLY TRP ALA ILE ALA
SEQRES 5 A 148 GLU ILE PRO ASP MET ASP TYR SER MET VAL THR THR GLY
SEQRES 6 A 148 PRO VAL GLY GLU SER GLY MET PRO ASP GLU PRO GLY TYR
SEQRES 7 A 148 ILE ASN GLY GLY MET MET GLN ARG GLY GLU VAL THR THR
SEQRES 8 A 148 PRO VAL VAL THR VAL ASP VAL GLU SER ILE GLU SER ALA
SEQRES 9 A 148 LEU GLU ARG ILE GLU SER LEU GLY GLY LYS THR VAL THR
SEQRES 10 A 148 GLY ARG THR PRO VAL GLY ASN MET GLY PHE ALA ALA TYR
SEQRES 11 A 148 PHE THR ASP SER GLU GLY ASN VAL VAL GLY LEU TRP GLU
SEQRES 12 A 148 THR ALA ARG GLY SER
SEQRES 1 B 148 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 148 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLY ARG ILE
SEQRES 3 B 148 VAL HIS PHE GLU ILE PRO PHE ASP ASP GLY ASP ARG ALA
SEQRES 4 B 148 ARG ALA PHE TYR ARG ASP ALA PHE GLY TRP ALA ILE ALA
SEQRES 5 B 148 GLU ILE PRO ASP MET ASP TYR SER MET VAL THR THR GLY
SEQRES 6 B 148 PRO VAL GLY GLU SER GLY MET PRO ASP GLU PRO GLY TYR
SEQRES 7 B 148 ILE ASN GLY GLY MET MET GLN ARG GLY GLU VAL THR THR
SEQRES 8 B 148 PRO VAL VAL THR VAL ASP VAL GLU SER ILE GLU SER ALA
SEQRES 9 B 148 LEU GLU ARG ILE GLU SER LEU GLY GLY LYS THR VAL THR
SEQRES 10 B 148 GLY ARG THR PRO VAL GLY ASN MET GLY PHE ALA ALA TYR
SEQRES 11 B 148 PHE THR ASP SER GLU GLY ASN VAL VAL GLY LEU TRP GLU
SEQRES 12 B 148 THR ALA ARG GLY SER
SEQRES 1 C 148 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 148 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLY ARG ILE
SEQRES 3 C 148 VAL HIS PHE GLU ILE PRO PHE ASP ASP GLY ASP ARG ALA
SEQRES 4 C 148 ARG ALA PHE TYR ARG ASP ALA PHE GLY TRP ALA ILE ALA
SEQRES 5 C 148 GLU ILE PRO ASP MET ASP TYR SER MET VAL THR THR GLY
SEQRES 6 C 148 PRO VAL GLY GLU SER GLY MET PRO ASP GLU PRO GLY TYR
SEQRES 7 C 148 ILE ASN GLY GLY MET MET GLN ARG GLY GLU VAL THR THR
SEQRES 8 C 148 PRO VAL VAL THR VAL ASP VAL GLU SER ILE GLU SER ALA
SEQRES 9 C 148 LEU GLU ARG ILE GLU SER LEU GLY GLY LYS THR VAL THR
SEQRES 10 C 148 GLY ARG THR PRO VAL GLY ASN MET GLY PHE ALA ALA TYR
SEQRES 11 C 148 PHE THR ASP SER GLU GLY ASN VAL VAL GLY LEU TRP GLU
SEQRES 12 C 148 THR ALA ARG GLY SER
SEQRES 1 D 148 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 148 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLY ARG ILE
SEQRES 3 D 148 VAL HIS PHE GLU ILE PRO PHE ASP ASP GLY ASP ARG ALA
SEQRES 4 D 148 ARG ALA PHE TYR ARG ASP ALA PHE GLY TRP ALA ILE ALA
SEQRES 5 D 148 GLU ILE PRO ASP MET ASP TYR SER MET VAL THR THR GLY
SEQRES 6 D 148 PRO VAL GLY GLU SER GLY MET PRO ASP GLU PRO GLY TYR
SEQRES 7 D 148 ILE ASN GLY GLY MET MET GLN ARG GLY GLU VAL THR THR
SEQRES 8 D 148 PRO VAL VAL THR VAL ASP VAL GLU SER ILE GLU SER ALA
SEQRES 9 D 148 LEU GLU ARG ILE GLU SER LEU GLY GLY LYS THR VAL THR
SEQRES 10 D 148 GLY ARG THR PRO VAL GLY ASN MET GLY PHE ALA ALA TYR
SEQRES 11 D 148 PHE THR ASP SER GLU GLY ASN VAL VAL GLY LEU TRP GLU
SEQRES 12 D 148 THR ALA ARG GLY SER
FORMUL 5 HOH *667(H2 O)
HELIX 1 1 ASP A 14 GLY A 27 1 14
HELIX 2 2 SER A 79 LEU A 90 1 12
HELIX 3 3 ASP B 14 GLY B 27 1 14
HELIX 4 4 SER B 79 LEU B 90 1 12
HELIX 5 5 ASP C 14 GLY C 27 1 14
HELIX 6 6 PRO C 34 ASP C 37 5 4
HELIX 7 7 SER C 79 LEU C 90 1 12
HELIX 8 8 ASP D 14 GLY D 27 1 14
HELIX 9 9 PRO D 34 ASP D 37 5 4
HELIX 10 10 SER D 79 GLU D 88 1 10
SHEET 1 A 8 ALA A 29 ILE A 33 0
SHEET 2 A 8 TYR A 38 THR A 42 -1 O TYR A 38 N ILE A 33
SHEET 3 A 8 GLY A 60 GLN A 64 -1 O GLY A 60 N VAL A 41
SHEET 4 A 8 ILE A 5 PHE A 12 1 N ILE A 10 O GLY A 61
SHEET 5 A 8 VAL A 72 ASP A 76 -1 O VAL A 72 N GLU A 9
SHEET 6 A 8 VAL A 117 THR A 123 1 O GLY A 119 N VAL A 73
SHEET 7 A 8 GLY A 105 THR A 111 -1 N PHE A 110 O VAL A 118
SHEET 8 A 8 LYS A 93 VAL A 101 -1 N LYS A 93 O THR A 111
SHEET 1 B 8 ALA B 29 GLU B 32 0
SHEET 2 B 8 SER B 39 THR B 42 -1 O MET B 40 N ALA B 31
SHEET 3 B 8 GLY B 60 GLN B 64 -1 O GLY B 60 N VAL B 41
SHEET 4 B 8 ILE B 5 PHE B 12 1 N PHE B 12 O MET B 63
SHEET 5 B 8 VAL B 72 ASP B 76 -1 O VAL B 72 N GLU B 9
SHEET 6 B 8 VAL B 117 THR B 123 1 O GLY B 119 N VAL B 73
SHEET 7 B 8 GLY B 105 THR B 111 -1 N PHE B 106 O GLU B 122
SHEET 8 B 8 LYS B 93 VAL B 101 -1 N VAL B 95 O TYR B 109
SHEET 1 C 8 ALA C 29 ILE C 33 0
SHEET 2 C 8 TYR C 38 THR C 42 -1 O THR C 42 N ALA C 29
SHEET 3 C 8 GLY C 60 GLN C 64 -1 O GLY C 60 N VAL C 41
SHEET 4 C 8 ILE C 5 PHE C 12 1 N PHE C 12 O MET C 63
SHEET 5 C 8 VAL C 72 ASP C 76 -1 O VAL C 72 N GLU C 9
SHEET 6 C 8 VAL C 117 THR C 123 1 O GLY C 119 N VAL C 73
SHEET 7 C 8 GLY C 105 THR C 111 -1 N PHE C 110 O VAL C 118
SHEET 8 C 8 LYS C 93 VAL C 101 -1 N VAL C 95 O TYR C 109
SHEET 1 D 8 ALA D 29 ILE D 33 0
SHEET 2 D 8 TYR D 38 THR D 42 -1 O TYR D 38 N ILE D 33
SHEET 3 D 8 GLY D 60 GLN D 64 -1 O GLY D 60 N VAL D 41
SHEET 4 D 8 ILE D 5 PHE D 12 1 N ILE D 10 O GLY D 61
SHEET 5 D 8 VAL D 72 ASP D 76 -1 O VAL D 72 N GLU D 9
SHEET 6 D 8 VAL D 117 THR D 123 1 O GLY D 119 N VAL D 75
SHEET 7 D 8 GLY D 105 THR D 111 -1 N PHE D 106 O GLU D 122
SHEET 8 D 8 LYS D 93 VAL D 101 -1 N VAL D 101 O GLY D 105
CISPEP 1 PRO A 34 ASP A 35 0 5.75
CRYST1 51.411 89.048 58.913 90.00 94.09 90.00 P 1 21 1 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 0.019451 0.000000 0.001391 0.00000
SCALE2 0.000000 0.011230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
