HEADER OXIDOREDUCTASE 25-JAN-07 2OO5
TITLE STRUCTURE OF TRANSHYDROGENASE (DI.H2NADH)2(DIII.NADP+)1 ASYMMETRIC
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD(P) TRANSHYDROGENASE SUBUNIT ALPHA PART 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PYRIDINE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT ALPHA 1;
COMPND 5 NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT ALPHA 1; PROTON-
COMPND 6 TRANSLOCATING TRANSHYDROGENASE COMPONENT 1; DI;
COMPND 7 EC: 1.6.1.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NAD(P) TRANSHYDROGENASE SUBUNIT BETA;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: RESIDUES 262-464;
COMPND 13 SYNONYM: PYRIDINE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT BETA;
COMPND 14 NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT BETA; PROTON-
COMPND 15 TRANSLOCATING TRANSHYDROGENASE NADP(H)-BINDING COMPONENT; DIII;
COMPND 16 EC: 1.6.1.2;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE 3 ORGANISM_TAXID: 1085;
SOURCE 4 GENE: PNTAA, NNTA1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C600;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCD1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE 12 ORGANISM_TAXID: 1085;
SOURCE 13 GENE: PNTB, NNTB;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PNIC2
KEYWDS ROSSMANN FOLD; NAD(H)-BINDING SITE; NADP(H)-BINDING SITE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BHAKTA,J.B.JACKSON
REVDAT 4 30-AUG-23 2OO5 1 REMARK
REVDAT 3 24-FEB-09 2OO5 1 VERSN
REVDAT 2 10-APR-07 2OO5 1 JRNL
REVDAT 1 13-MAR-07 2OO5 0
JRNL AUTH T.BHAKTA,S.J.WHITEHEAD,J.S.SNAITH,T.R.DAFFORN,J.WILKIE,
JRNL AUTH 2 S.RAJESH,S.A.WHITE,J.B.JACKSON
JRNL TITL STRUCTURES OF THE DI(2)DIII(1) COMPLEX OF
JRNL TITL 2 PROTON-TRANSLOCATING TRANSHYDROGENASE WITH BOUND, INACTIVE
JRNL TITL 3 ANALOGUES OF NADH AND NADPH REVEAL ACTIVE SITE GEOMETRIES
JRNL REF BIOCHEMISTRY V. 46 3304 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17323922
JRNL DOI 10.1021/BI061843R
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 27507
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1396
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1928
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6899
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.34000
REMARK 3 B22 (A**2) : -0.91000
REMARK 3 B33 (A**2) : 1.25000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.390
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.283
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.859
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7162 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6792 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9733 ; 1.252 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15809 ; 0.934 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 931 ; 7.606 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 242 ;37.147 ;24.876
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1239 ;14.661 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;14.041 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1173 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7808 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1251 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1325 ; 0.142 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6628 ; 0.124 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3411 ; 0.147 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 3818 ; 0.079 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 240 ; 0.127 ; 0.500
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): 12 ; 0.063 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.108 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.095 ; 0.500
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): 6015 ; 0.974 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1902 ; 0.135 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7475 ; 1.149 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2820 ; 0.619 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2258 ; 0.970 ; 3.000
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 : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 269
REMARK 3 RESIDUE RANGE : B 1 B 280
REMARK 3 RESIDUE RANGE : C 30 C 202
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9347 55.9314 119.4688
REMARK 3 T TENSOR
REMARK 3 T11: -0.0944 T22: -0.1236
REMARK 3 T33: -0.0830 T12: -0.0020
REMARK 3 T13: -0.0170 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.9510 L22: 0.6430
REMARK 3 L33: 0.5113 L12: -0.0210
REMARK 3 L13: 0.3322 L23: -0.0601
REMARK 3 S TENSOR
REMARK 3 S11: 0.1265 S12: -0.0242 S13: -0.0132
REMARK 3 S21: -0.0909 S22: -0.0400 S23: -0.0081
REMARK 3 S31: 0.0378 S32: 0.0540 S33: -0.0866
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 2OO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041377.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27548
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 80.163
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : 0.22700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1U2D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 4000, 10% GLYCEROL, 100MM
REMARK 280 TRIS, 75MM LITHIUM SULPHATE, VAPOR DIFFUSION, TEMPERATURE 277K,
REMARK 280 PH 8
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 35.59950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.86050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.51250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.86050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.59950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.51250
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 381
REMARK 465 GLN A 382
REMARK 465 GLY A 383
REMARK 465 ALA A 384
REMARK 465 GLY B 381
REMARK 465 GLN B 382
REMARK 465 GLY B 383
REMARK 465 ALA B 384
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 ALA B 68 N - CA - C ANGL. DEV. = -18.0 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 ALA A 17 44.63 -95.30
REMARK 500 VAL A 74 -71.02 -84.84
REMARK 500 VAL A 180 66.32 -106.48
REMARK 500 VAL A 221 -53.94 -127.22
REMARK 500 ASP A 222 96.46 -161.78
REMARK 500 VAL A 327 51.39 -115.73
REMARK 500 LEU A 379 -65.51 90.55
REMARK 500 ALA B 17 53.87 -92.31
REMARK 500 VAL B 74 -66.42 -94.98
REMARK 500 VAL B 180 61.67 -119.50
REMARK 500 ASP B 222 87.03 -164.15
REMARK 500 ALA B 225 -40.67 156.93
REMARK 500 ALA B 297 41.98 -107.75
REMARK 500 LEU B 379 41.23 -104.19
REMARK 500 ASN C 45 47.56 -98.03
REMARK 500 GLU C 76 38.46 -98.54
REMARK 500 ASN C 131 -74.05 -149.10
REMARK 500 PHE C 180 60.76 -100.38
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 SER B 66 GLN B 67 -124.17
REMARK 500 GLN B 67 ALA B 68 -102.52
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 B 385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TXD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TXD B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U2D RELATED DB: PDB
REMARK 900 RELATED ID: 1HZZ RELATED DB: PDB
REMARK 900 RELATED ID: 2OOR RELATED DB: PDB
DBREF 2OO5 A 1 384 UNP P0C186 PNTAA_RHORU 1 384
DBREF 2OO5 B 1 384 UNP P0C186 PNTAA_RHORU 1 384
DBREF 2OO5 C 30 203 UNP P0C188 PNTB_RHORU 291 464
SEQRES 1 A 384 MET LYS ILE ALA ILE PRO LYS GLU ARG ARG PRO GLY GLU
SEQRES 2 A 384 ASP ARG VAL ALA ILE SER PRO GLU VAL VAL LYS LYS LEU
SEQRES 3 A 384 VAL GLY LEU GLY PHE GLU VAL ILE VAL GLU GLN GLY ALA
SEQRES 4 A 384 GLY VAL GLY ALA SER ILE THR ASP ASP ALA LEU THR ALA
SEQRES 5 A 384 ALA GLY ALA THR ILE ALA SER THR ALA ALA GLN ALA LEU
SEQRES 6 A 384 SER GLN ALA ASP VAL VAL TRP LYS VAL GLN ARG PRO MET
SEQRES 7 A 384 THR ALA GLU GLU GLY THR ASP GLU VAL ALA LEU ILE LYS
SEQRES 8 A 384 GLU GLY ALA VAL LEU MET CYS HIS LEU GLY ALA LEU THR
SEQRES 9 A 384 ASN ARG PRO VAL VAL GLU ALA LEU THR LYS ARG LYS ILE
SEQRES 10 A 384 THR ALA TYR ALA MET GLU LEU MET PRO ARG ILE SER ARG
SEQRES 11 A 384 ALA GLN SER MET ASP ILE LEU SER SER GLN SER ASN LEU
SEQRES 12 A 384 ALA GLY TYR ARG ALA VAL ILE ASP GLY ALA TYR GLU PHE
SEQRES 13 A 384 ALA ARG ALA PHE PRO MET MET MET THR ALA ALA GLY THR
SEQRES 14 A 384 VAL PRO PRO ALA ARG VAL LEU VAL PHE GLY VAL GLY VAL
SEQRES 15 A 384 ALA GLY LEU GLN ALA ILE ALA THR ALA LYS ARG LEU GLY
SEQRES 16 A 384 ALA VAL VAL MET ALA THR ASP VAL ARG ALA ALA THR LYS
SEQRES 17 A 384 GLU GLN VAL GLU SER LEU GLY GLY LYS PHE ILE THR VAL
SEQRES 18 A 384 ASP ASP GLU ALA MET LYS THR ALA GLU THR ALA GLY GLY
SEQRES 19 A 384 TYR ALA LYS GLU MET GLY GLU GLU PHE ARG LYS LYS GLN
SEQRES 20 A 384 ALA GLU ALA VAL LEU LYS GLU LEU VAL LYS THR ASP ILE
SEQRES 21 A 384 ALA ILE THR THR ALA LEU ILE PRO GLY LYS PRO ALA PRO
SEQRES 22 A 384 VAL LEU ILE THR GLU GLU MET VAL THR LYS MET LYS PRO
SEQRES 23 A 384 GLY SER VAL ILE ILE ASP LEU ALA VAL GLU ALA GLY GLY
SEQRES 24 A 384 ASN CYS PRO LEU SER GLU PRO GLY LYS ILE VAL VAL LYS
SEQRES 25 A 384 HIS GLY VAL LYS ILE VAL GLY HIS THR ASN VAL PRO SER
SEQRES 26 A 384 ARG VAL ALA ALA ASP ALA SER PRO LEU PHE ALA LYS ASN
SEQRES 27 A 384 LEU LEU ASN PHE LEU THR PRO HIS VAL ASP LYS ASP THR
SEQRES 28 A 384 LYS THR LEU VAL MET LYS LEU GLU ASP GLU THR VAL SER
SEQRES 29 A 384 GLY THR CYS VAL THR ARG ASP GLY ALA ILE VAL HIS PRO
SEQRES 30 A 384 ALA LEU THR GLY GLN GLY ALA
SEQRES 1 B 384 MET LYS ILE ALA ILE PRO LYS GLU ARG ARG PRO GLY GLU
SEQRES 2 B 384 ASP ARG VAL ALA ILE SER PRO GLU VAL VAL LYS LYS LEU
SEQRES 3 B 384 VAL GLY LEU GLY PHE GLU VAL ILE VAL GLU GLN GLY ALA
SEQRES 4 B 384 GLY VAL GLY ALA SER ILE THR ASP ASP ALA LEU THR ALA
SEQRES 5 B 384 ALA GLY ALA THR ILE ALA SER THR ALA ALA GLN ALA LEU
SEQRES 6 B 384 SER GLN ALA ASP VAL VAL TRP LYS VAL GLN ARG PRO MET
SEQRES 7 B 384 THR ALA GLU GLU GLY THR ASP GLU VAL ALA LEU ILE LYS
SEQRES 8 B 384 GLU GLY ALA VAL LEU MET CYS HIS LEU GLY ALA LEU THR
SEQRES 9 B 384 ASN ARG PRO VAL VAL GLU ALA LEU THR LYS ARG LYS ILE
SEQRES 10 B 384 THR ALA TYR ALA MET GLU LEU MET PRO ARG ILE SER ARG
SEQRES 11 B 384 ALA GLN SER MET ASP ILE LEU SER SER GLN SER ASN LEU
SEQRES 12 B 384 ALA GLY TYR ARG ALA VAL ILE ASP GLY ALA TYR GLU PHE
SEQRES 13 B 384 ALA ARG ALA PHE PRO MET MET MET THR ALA ALA GLY THR
SEQRES 14 B 384 VAL PRO PRO ALA ARG VAL LEU VAL PHE GLY VAL GLY VAL
SEQRES 15 B 384 ALA GLY LEU GLN ALA ILE ALA THR ALA LYS ARG LEU GLY
SEQRES 16 B 384 ALA VAL VAL MET ALA THR ASP VAL ARG ALA ALA THR LYS
SEQRES 17 B 384 GLU GLN VAL GLU SER LEU GLY GLY LYS PHE ILE THR VAL
SEQRES 18 B 384 ASP ASP GLU ALA MET LYS THR ALA GLU THR ALA GLY GLY
SEQRES 19 B 384 TYR ALA LYS GLU MET GLY GLU GLU PHE ARG LYS LYS GLN
SEQRES 20 B 384 ALA GLU ALA VAL LEU LYS GLU LEU VAL LYS THR ASP ILE
SEQRES 21 B 384 ALA ILE THR THR ALA LEU ILE PRO GLY LYS PRO ALA PRO
SEQRES 22 B 384 VAL LEU ILE THR GLU GLU MET VAL THR LYS MET LYS PRO
SEQRES 23 B 384 GLY SER VAL ILE ILE ASP LEU ALA VAL GLU ALA GLY GLY
SEQRES 24 B 384 ASN CYS PRO LEU SER GLU PRO GLY LYS ILE VAL VAL LYS
SEQRES 25 B 384 HIS GLY VAL LYS ILE VAL GLY HIS THR ASN VAL PRO SER
SEQRES 26 B 384 ARG VAL ALA ALA ASP ALA SER PRO LEU PHE ALA LYS ASN
SEQRES 27 B 384 LEU LEU ASN PHE LEU THR PRO HIS VAL ASP LYS ASP THR
SEQRES 28 B 384 LYS THR LEU VAL MET LYS LEU GLU ASP GLU THR VAL SER
SEQRES 29 B 384 GLY THR CYS VAL THR ARG ASP GLY ALA ILE VAL HIS PRO
SEQRES 30 B 384 ALA LEU THR GLY GLN GLY ALA
SEQRES 1 C 174 SER VAL LYS ALA GLY SER ALA GLU ASP ALA ALA PHE ILE
SEQRES 2 C 174 MET LYS ASN ALA SER LYS VAL ILE ILE VAL PRO GLY TYR
SEQRES 3 C 174 GLY MET ALA VAL ALA GLN ALA GLN HIS ALA LEU ARG GLU
SEQRES 4 C 174 MET ALA ASP VAL LEU LYS LYS GLU GLY VAL GLU VAL SER
SEQRES 5 C 174 TYR ALA ILE HIS PRO VAL ALA GLY ARG MET PRO GLY HIS
SEQRES 6 C 174 MET ASN VAL LEU LEU ALA GLU ALA ASN VAL PRO TYR ASP
SEQRES 7 C 174 GLU VAL PHE GLU LEU GLU GLU ILE ASN SER SER PHE GLN
SEQRES 8 C 174 THR ALA ASP VAL ALA PHE VAL ILE GLY ALA ASN ASP VAL
SEQRES 9 C 174 THR ASN PRO ALA ALA LYS THR ASP PRO SER SER PRO ILE
SEQRES 10 C 174 TYR GLY MET PRO ILE LEU ASP VAL GLU LYS ALA GLY THR
SEQRES 11 C 174 VAL LEU PHE ILE LYS ARG SER MET ALA SER GLY TYR ALA
SEQRES 12 C 174 GLY VAL GLU ASN GLU LEU PHE PHE ARG ASN ASN THR MET
SEQRES 13 C 174 MET LEU PHE GLY ASP ALA LYS LYS MET THR GLU GLN ILE
SEQRES 14 C 174 VAL GLN ALA MET ASN
HET SO4 A 385 5
HET SO4 A 386 5
HET TXD A 500 44
HET SO4 B 385 5
HET SO4 B 386 5
HET TXD B 600 44
HET NAP C 400 48
HETNAM SO4 SULFATE ION
HETNAM TXD 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 TXD 2(C21 H31 N7 O14 P2)
FORMUL 10 NAP C21 H28 N7 O17 P3
FORMUL 11 HOH *27(H2 O)
HELIX 1 1 SER A 19 GLY A 30 1 12
HELIX 2 2 THR A 46 GLY A 54 1 9
HELIX 3 3 THR A 60 SER A 66 1 7
HELIX 4 4 THR A 79 GLY A 83 5 5
HELIX 5 5 ASP A 85 ILE A 90 1 6
HELIX 6 6 ASN A 105 ARG A 115 1 11
HELIX 7 7 GLU A 123 MET A 125 5 3
HELIX 8 8 ILE A 128 MET A 134 5 7
HELIX 9 9 ASP A 135 PHE A 156 1 22
HELIX 10 10 GLY A 181 LEU A 194 1 14
HELIX 11 11 ALA A 206 LEU A 214 1 9
HELIX 12 12 ASP A 222 THR A 228 1 7
HELIX 13 13 MET A 239 VAL A 256 1 18
HELIX 14 14 THR A 277 LYS A 283 1 7
HELIX 15 15 ALA A 294 GLY A 298 5 5
HELIX 16 16 ASN A 322 ARG A 326 5 5
HELIX 17 17 VAL A 327 THR A 344 1 18
HELIX 18 18 PRO A 345 VAL A 347 5 3
HELIX 19 19 ASP A 360 CYS A 367 1 8
HELIX 20 20 SER B 19 GLY B 30 1 12
HELIX 21 21 THR B 46 GLY B 54 1 9
HELIX 22 22 THR B 60 SER B 66 1 7
HELIX 23 23 THR B 79 GLY B 83 5 5
HELIX 24 24 GLU B 86 ILE B 90 5 5
HELIX 25 25 ASN B 105 ARG B 115 1 11
HELIX 26 26 GLU B 123 MET B 125 5 3
HELIX 27 27 ILE B 128 MET B 134 5 7
HELIX 28 28 ASP B 135 PHE B 156 1 22
HELIX 29 29 GLY B 181 LEU B 194 1 14
HELIX 30 30 ALA B 206 SER B 213 1 8
HELIX 31 31 ASP B 222 LYS B 227 1 6
HELIX 32 32 GLY B 240 VAL B 256 1 17
HELIX 33 33 THR B 277 MET B 284 1 8
HELIX 34 34 ALA B 294 GLY B 298 5 5
HELIX 35 35 ASN B 322 ARG B 326 5 5
HELIX 36 36 VAL B 327 THR B 344 1 18
HELIX 37 37 ASP B 360 THR B 366 1 7
HELIX 38 38 HIS B 376 THR B 380 5 5
HELIX 39 39 SER C 35 ASN C 45 1 11
HELIX 40 40 GLY C 54 GLN C 61 1 8
HELIX 41 41 ALA C 62 GLU C 76 1 15
HELIX 42 42 GLY C 93 ALA C 102 1 10
HELIX 43 43 PRO C 105 ASP C 107 5 3
HELIX 44 44 LEU C 112 ASN C 116 1 5
HELIX 45 45 SER C 117 GLN C 120 5 4
HELIX 46 46 PRO C 136 ASP C 141 1 6
HELIX 47 47 ASP C 153 ALA C 157 5 5
HELIX 48 48 ASN C 176 PHE C 180 5 5
HELIX 49 49 ASP C 190 MET C 202 1 13
SHEET 1 A 6 THR A 56 ALA A 58 0
SHEET 2 A 6 GLU A 32 GLU A 36 1 N VAL A 33 O THR A 56
SHEET 3 A 6 LYS A 2 ILE A 5 1 N ILE A 3 O ILE A 34
SHEET 4 A 6 VAL A 70 GLN A 75 1 O VAL A 70 N ALA A 4
SHEET 5 A 6 VAL A 95 HIS A 99 1 O HIS A 99 N VAL A 74
SHEET 6 A 6 THR A 118 ALA A 121 1 O TYR A 120 N LEU A 96
SHEET 1 B 2 MET A 163 THR A 165 0
SHEET 2 B 2 GLY A 168 VAL A 170 -1 O VAL A 170 N MET A 163
SHEET 1 C 7 LYS A 217 PHE A 218 0
SHEET 2 C 7 VAL A 197 THR A 201 1 N ALA A 200 O LYS A 217
SHEET 3 C 7 ARG A 174 PHE A 178 1 N VAL A 175 O VAL A 197
SHEET 4 C 7 ILE A 260 THR A 263 1 O ILE A 262 N PHE A 178
SHEET 5 C 7 VAL A 289 ASP A 292 1 O ILE A 291 N ALA A 261
SHEET 6 C 7 VAL A 315 GLY A 319 1 O VAL A 318 N ILE A 290
SHEET 7 C 7 LYS A 308 LYS A 312 -1 N VAL A 310 O ILE A 317
SHEET 1 D 8 THR B 56 ALA B 58 0
SHEET 2 D 8 GLU B 32 GLU B 36 1 N VAL B 33 O THR B 56
SHEET 3 D 8 LYS B 2 ILE B 5 1 N ILE B 3 O ILE B 34
SHEET 4 D 8 VAL B 70 TRP B 72 1 O VAL B 70 N ALA B 4
SHEET 5 D 8 VAL B 95 CYS B 98 1 O VAL B 95 N VAL B 71
SHEET 6 D 8 THR B 118 ALA B 121 1 O THR B 118 N LEU B 96
SHEET 7 D 8 CYS B 367 ARG B 370 -1 O VAL B 368 N ALA B 119
SHEET 8 D 8 ALA B 373 ILE B 374 -1 O ALA B 373 N ARG B 370
SHEET 1 E 2 MET B 163 MET B 164 0
SHEET 2 E 2 THR B 169 VAL B 170 -1 O VAL B 170 N MET B 163
SHEET 1 F 7 LYS B 217 PHE B 218 0
SHEET 2 F 7 VAL B 197 THR B 201 1 N VAL B 198 O LYS B 217
SHEET 3 F 7 ARG B 174 PHE B 178 1 N VAL B 175 O MET B 199
SHEET 4 F 7 ILE B 260 THR B 263 1 O ILE B 262 N LEU B 176
SHEET 5 F 7 VAL B 289 ASP B 292 1 O ILE B 291 N THR B 263
SHEET 6 F 7 VAL B 315 GLY B 319 1 O VAL B 318 N ILE B 290
SHEET 7 F 7 LYS B 308 LYS B 312 -1 N VAL B 310 O ILE B 317
SHEET 1 G 2 VAL B 347 ASP B 348 0
SHEET 2 G 2 THR B 353 LEU B 354 -1 O THR B 353 N ASP B 348
SHEET 1 H 6 VAL C 109 GLU C 111 0
SHEET 2 H 6 GLU C 79 ILE C 84 1 N ILE C 84 O PHE C 110
SHEET 3 H 6 LYS C 48 PRO C 53 1 N VAL C 49 O GLU C 79
SHEET 4 H 6 VAL C 124 ILE C 128 1 O PHE C 126 N VAL C 52
SHEET 5 H 6 THR C 159 LYS C 164 1 O ILE C 163 N VAL C 127
SHEET 6 H 6 THR C 184 PHE C 188 1 O LEU C 187 N PHE C 162
SITE 1 AC1 3 ARG A 147 ARG A 326 TYR B 154
SITE 1 AC2 5 THR A 169 PRO A 171 SO4 A 386 ASP B 330
SITE 2 AC2 5 PRO B 333
SITE 1 AC3 4 TYR A 154 LYS A 316 ARG B 147 ARG B 326
SITE 1 AC4 5 ARG A 158 HOH A 501 HOH A 510 PRO B 333
SITE 2 AC4 5 SO4 B 386
SITE 1 AC5 24 SER B 129 TXD B 600 GLY C 54 TYR C 55
SITE 2 AC5 24 GLY C 56 ALA C 60 VAL C 87 GLY C 89
SITE 3 AC5 24 ARG C 90 MET C 91 PRO C 92 GLY C 129
SITE 4 AC5 24 ALA C 130 ASN C 131 ASP C 132 VAL C 133
SITE 5 AC5 24 LYS C 164 ARG C 165 SER C 166 GLY C 170
SITE 6 AC5 24 TYR C 171 GLY C 189 ASP C 190 ALA C 191
SITE 1 AC6 18 ARG A 127 ILE A 128 GLN A 132 ASP A 135
SITE 2 AC6 18 GLY A 179 GLY A 181 VAL A 182 ASP A 202
SITE 3 AC6 18 VAL A 203 ARG A 204 GLY A 234 ALA A 236
SITE 4 AC6 18 GLN A 247 THR A 264 ALA A 265 LEU A 266
SITE 5 AC6 18 PRO A 273 LEU A 275
SITE 1 AC7 24 ARG B 127 ILE B 128 SER B 129 GLN B 132
SITE 2 AC7 24 SER B 138 GLY B 179 VAL B 180 GLY B 181
SITE 3 AC7 24 VAL B 182 ASP B 202 VAL B 203 ARG B 204
SITE 4 AC7 24 GLY B 234 TYR B 235 ALA B 236 GLN B 247
SITE 5 AC7 24 THR B 264 ALA B 265 LEU B 266 PRO B 273
SITE 6 AC7 24 LEU B 275 HOH B 607 TYR C 171 NAP C 400
CRYST1 71.199 101.025 131.721 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 0.014045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007592 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
