HEADER TRANSFERASE 24-DEC-13 4O7H
TITLE CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE FROM RHODOSPIRILLUM
TITLE 2 RUBRUM F11, TARGET EFI-507460
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM F11;
SOURCE 3 ORGANISM_TAXID: 1036743;
SOURCE 4 STRAIN: ATCC 11170 / NCIB 8255;
SOURCE 5 GENE: F11_00115, RRU_A0022;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KIM,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,S.R.WASSERMAN,
AUTHOR 2 S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,M.STEAD,
AUTHOR 3 B.HILLERICH,J.LOVE,R.D.SEIDEL,H.J.IMKER,J.D.ATTONITO,J.A.GERLT,
AUTHOR 4 S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)
REVDAT 3 20-SEP-23 4O7H 1 REMARK
REVDAT 2 15-JAN-14 4O7H 1 AUTHOR
REVDAT 1 08-JAN-14 4O7H 0
JRNL AUTH J.KIM,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,
JRNL AUTH 2 S.R.WASSERMAN,S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,
JRNL AUTH 3 S.CHOWDHURY,B.EVANS,M.STEAD,B.HILLERICH,J.LOVE,R.D.SEIDEL,
JRNL AUTH 4 H.J.IMKER,J.D.ATTONITO,J.A.GERLT,S.C.ALMO,
JRNL AUTH 5 ENZYME FUNCTION INITIATIVE (EFI)
JRNL TITL CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE FROM
JRNL TITL 2 RHODOSPIRILLUM RUBRUM F11, TARGET EFI-507460
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 54113
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2907
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3797
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 185
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3554
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.42000
REMARK 3 B13 (A**2) : 0.32000
REMARK 3 B23 (A**2) : -0.62000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.641
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3704 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3513 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5055 ; 1.551 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8055 ; 0.878 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 451 ; 5.501 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;25.356 ;21.930
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 602 ;12.873 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;19.891 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 548 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4158 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 871 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1795 ; 1.523 ; 1.800
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1794 ; 1.522 ; 1.800
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2249 ; 2.315 ; 2.690
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2250 ; 2.314 ; 2.691
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1909 ; 2.053 ; 1.982
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1909 ; 2.051 ; 1.981
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2806 ; 3.190 ; 2.893
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4431 ; 4.480 ;14.722
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4365 ; 4.447 ;14.593
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 222 B 1 222 13593 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4O7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57020
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4MDC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE, 0.085 M
REMARK 280 TRIS:HCL, 25.5% (W/V) PEG 4000, 15% (V/V) GLYCEROL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 B 122
REMARK 465 GLY B 123
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 157 CG OD1 OD2
REMARK 470 ARG A 212 CD NE CZ NH1 NH2
REMARK 470 ARG B 37 CD NE CZ NH1 NH2
REMARK 470 ARG B 118 CD NE CZ NH1 NH2
REMARK 470 SER B 121 OG
REMARK 470 ARG B 212 CD NE CZ NH1 NH2
REMARK 470 ARG B 215 CD NE CZ NH1 NH2
REMARK 470 ASP B 221 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 65 CB TRP B 65 CG -0.118
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 A 215 NE - CZ - NH1 ANGL. DEV. = 3.6 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 63 129.85 91.48
REMARK 500 ARG A 100 -70.11 -103.67
REMARK 500 VAL A 106 -62.66 -132.44
REMARK 500 ASP B 63 131.21 94.10
REMARK 500 ARG B 100 -68.28 -103.87
REMARK 500 VAL B 106 -62.71 -135.29
REMARK 500 ILE B 120 -67.51 -94.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EFI-507460 RELATED DB: TARGETTRACK
DBREF 4O7H A 1 222 UNP G2TFN6 G2TFN6_RHORU 1 222
DBREF 4O7H B 1 222 UNP G2TFN6 G2TFN6_RHORU 1 222
SEQRES 1 A 222 MET ARG ARG LEU TYR HIS HIS GLY LEU SER PRO ALA ALA
SEQRES 2 A 222 ARG LYS VAL ARG VAL ALA LEU ALA GLU LYS ARG LEU ASP
SEQRES 3 A 222 TYR GLU ALA VAL ILE GLU GLU THR TRP ILE ARG ASN GLU
SEQRES 4 A 222 SER PHE LEU ALA MET ASN PRO GLU GLY GLU VAL PRO VAL
SEQRES 5 A 222 LEU VAL GLU ALA ASP GLY LEU THR ILE THR ASP GLY TRP
SEQRES 6 A 222 ALA ILE CYS GLU TYR LEU GLU GLU VAL TYR PRO GLU PRO
SEQRES 7 A 222 SER LEU LEU GLY GLY PRO ALA ALA MET ARG ALA GLU VAL
SEQRES 8 A 222 ARG ARG LEU VAL ALA TRP PHE ASP ARG LYS PHE ASN ARG
SEQRES 9 A 222 GLU VAL THR GLU PRO LEU VAL ARG GLU LYS LEU LEU LYS
SEQRES 10 A 222 ARG VAL ILE SER GLY GLY ALA PRO ASP SER ARG GLN ILE
SEQRES 11 A 222 ARG ALA GLY ARG ALA ASN VAL HIS THR HIS LEU ARG TYR
SEQRES 12 A 222 ILE SER TRP LEU ILE ASP ARG ARG ARG TRP LEU ALA GLY
SEQRES 13 A 222 ASP MET LEU THR TYR ALA ASP ILE THR ALA ALA CYS HIS
SEQRES 14 A 222 LEU SER LEU ILE ASP TYR ALA GLY ASP VAL PRO TRP GLU
SEQRES 15 A 222 ASP HIS PRO GLN ALA LYS GLU TRP TYR ALA LEU VAL LYS
SEQRES 16 A 222 SER ARG PRO SER PHE ARG PRO LEU LEU THR GLU THR ILE
SEQRES 17 A 222 SER PRO ILE ARG PRO PRO ARG HIS TYR ALA ASP LEU ASP
SEQRES 18 A 222 PHE
SEQRES 1 B 222 MET ARG ARG LEU TYR HIS HIS GLY LEU SER PRO ALA ALA
SEQRES 2 B 222 ARG LYS VAL ARG VAL ALA LEU ALA GLU LYS ARG LEU ASP
SEQRES 3 B 222 TYR GLU ALA VAL ILE GLU GLU THR TRP ILE ARG ASN GLU
SEQRES 4 B 222 SER PHE LEU ALA MET ASN PRO GLU GLY GLU VAL PRO VAL
SEQRES 5 B 222 LEU VAL GLU ALA ASP GLY LEU THR ILE THR ASP GLY TRP
SEQRES 6 B 222 ALA ILE CYS GLU TYR LEU GLU GLU VAL TYR PRO GLU PRO
SEQRES 7 B 222 SER LEU LEU GLY GLY PRO ALA ALA MET ARG ALA GLU VAL
SEQRES 8 B 222 ARG ARG LEU VAL ALA TRP PHE ASP ARG LYS PHE ASN ARG
SEQRES 9 B 222 GLU VAL THR GLU PRO LEU VAL ARG GLU LYS LEU LEU LYS
SEQRES 10 B 222 ARG VAL ILE SER GLY GLY ALA PRO ASP SER ARG GLN ILE
SEQRES 11 B 222 ARG ALA GLY ARG ALA ASN VAL HIS THR HIS LEU ARG TYR
SEQRES 12 B 222 ILE SER TRP LEU ILE ASP ARG ARG ARG TRP LEU ALA GLY
SEQRES 13 B 222 ASP MET LEU THR TYR ALA ASP ILE THR ALA ALA CYS HIS
SEQRES 14 B 222 LEU SER LEU ILE ASP TYR ALA GLY ASP VAL PRO TRP GLU
SEQRES 15 B 222 ASP HIS PRO GLN ALA LYS GLU TRP TYR ALA LEU VAL LYS
SEQRES 16 B 222 SER ARG PRO SER PHE ARG PRO LEU LEU THR GLU THR ILE
SEQRES 17 B 222 SER PRO ILE ARG PRO PRO ARG HIS TYR ALA ASP LEU ASP
SEQRES 18 B 222 PHE
FORMUL 3 HOH *198(H2 O)
HELIX 1 1 SER A 10 LYS A 23 1 14
HELIX 2 2 ASN A 38 ASN A 45 1 8
HELIX 3 3 ASP A 63 TYR A 75 1 13
HELIX 4 4 PRO A 84 VAL A 106 1 23
HELIX 5 5 VAL A 106 LEU A 115 1 10
HELIX 6 6 LEU A 115 ILE A 120 1 6
HELIX 7 7 ASP A 126 ARG A 151 1 26
HELIX 8 8 THR A 160 ALA A 176 1 17
HELIX 9 9 PRO A 180 ASP A 183 5 4
HELIX 10 10 HIS A 184 SER A 196 1 13
HELIX 11 11 ARG A 197 SER A 199 5 3
HELIX 12 12 PHE A 200 GLU A 206 1 7
HELIX 13 13 SER B 10 LYS B 23 1 14
HELIX 14 14 ASN B 38 ASN B 45 1 8
HELIX 15 15 ASP B 63 TYR B 75 1 13
HELIX 16 16 PRO B 84 VAL B 106 1 23
HELIX 17 17 VAL B 106 LEU B 115 1 10
HELIX 18 18 LEU B 115 SER B 121 1 7
HELIX 19 19 ASP B 126 ARG B 151 1 26
HELIX 20 20 THR B 160 ALA B 176 1 17
HELIX 21 21 PRO B 180 ASP B 183 5 4
HELIX 22 22 HIS B 184 SER B 196 1 13
HELIX 23 23 ARG B 197 SER B 199 5 3
HELIX 24 24 PHE B 200 GLU B 206 1 7
SHEET 1 A 4 GLU A 28 ILE A 31 0
SHEET 2 A 4 ARG A 3 HIS A 6 1 N LEU A 4 O VAL A 30
SHEET 3 A 4 VAL A 52 VAL A 54 -1 O VAL A 52 N TYR A 5
SHEET 4 A 4 THR A 60 THR A 62 -1 O ILE A 61 N LEU A 53
SHEET 1 B 4 GLU B 28 ILE B 31 0
SHEET 2 B 4 ARG B 3 HIS B 6 1 N LEU B 4 O VAL B 30
SHEET 3 B 4 VAL B 52 VAL B 54 -1 O VAL B 52 N TYR B 5
SHEET 4 B 4 THR B 60 THR B 62 -1 O ILE B 61 N LEU B 53
CISPEP 1 VAL A 50 PRO A 51 0 2.59
CISPEP 2 GLU A 77 PRO A 78 0 -2.34
CISPEP 3 SER A 209 PRO A 210 0 3.66
CISPEP 4 VAL B 50 PRO B 51 0 3.90
CISPEP 5 GLU B 77 PRO B 78 0 -1.05
CISPEP 6 SER B 209 PRO B 210 0 2.13
CRYST1 47.084 48.965 56.559 109.85 106.96 95.20 P 1 2
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 0.021239 0.001932 0.007821 0.00000
SCALE2 0.000000 0.020507 0.008533 0.00000
SCALE3 0.000000 0.000000 0.020021 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
