HEADER CHAPERONE 16-NOV-11 3UO2
TITLE JAC1 CO-CHAPERONE FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: J-TYPE CO-CHAPERONE JAC1, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: J-TYPE ACCESSORY CHAPERONE 1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: JAC1, SEO2, YGL018C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, CO-CHAPERONE, J-PROTEIN, IRON SULFUR CLUSTER
KEYWDS 3 BIOGENESIS, SSQ1 HSP70 CHAPERONE, ISU PROTEINS, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,R.MULLIGAN,L.BIGELOW,J.MARSZALEK,E.A.CRAIG,R.DUTKIEWICZ,
AUTHOR 2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 5 13-SEP-23 3UO2 1 REMARK
REVDAT 4 08-NOV-17 3UO2 1 REMARK
REVDAT 3 23-MAY-12 3UO2 1 AUTHOR
REVDAT 2 21-MAR-12 3UO2 1 JRNL
REVDAT 1 14-DEC-11 3UO2 0
JRNL AUTH S.J.CIESIELSKI,B.A.SCHILKE,J.OSIPIUK,L.BIGELOW,R.MULLIGAN,
JRNL AUTH 2 J.MAJEWSKA,A.JOACHIMIAK,J.MARSZALEK,E.A.CRAIG,R.DUTKIEWICZ
JRNL TITL INTERACTION OF J-PROTEIN CO-CHAPERONE JAC1 WITH FE-S
JRNL TITL 2 SCAFFOLD ISU IS INDISPENSABLE IN VIVO AND CONSERVED IN
JRNL TITL 3 EVOLUTION.
JRNL REF J.MOL.BIOL. V. 417 1 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22306468
JRNL DOI 10.1016/J.JMB.2012.01.022
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 20697
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1065
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) : 2.13
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1254
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2585
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.22000
REMARK 3 B22 (A**2) : -2.24000
REMARK 3 B33 (A**2) : 3.45000
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): 0.221
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.422
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2729 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1926 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3696 ; 1.747 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4725 ; 0.982 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 5.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;40.312 ;25.208
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 542 ;18.027 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;24.699 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 402 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2971 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 529 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 10 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8083 29.4701 -0.0152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0832 T22: 0.0226
REMARK 3 T33: 0.0345 T12: 0.0131
REMARK 3 T13: -0.0245 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.6463 L22: 2.2253
REMARK 3 L33: 1.9657 L12: -0.8394
REMARK 3 L13: 1.2926 L23: -0.2908
REMARK 3 S TENSOR
REMARK 3 S11: -0.1027 S12: -0.1697 S13: -0.2285
REMARK 3 S21: 0.1724 S22: 0.0436 S23: 0.0903
REMARK 3 S31: -0.2036 S32: -0.0569 S33: 0.0591
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 11 B 184
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4632 47.8220 -24.5707
REMARK 3 T TENSOR
REMARK 3 T11: 0.1463 T22: 0.2200
REMARK 3 T33: 0.0480 T12: 0.0415
REMARK 3 T13: -0.0054 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.8379 L22: 3.9614
REMARK 3 L33: 2.7636 L12: -1.7867
REMARK 3 L13: 1.8850 L23: -2.4322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0758 S13: 0.1541
REMARK 3 S21: 0.1293 S22: -0.1003 S23: -0.1751
REMARK 3 S31: 0.0671 S32: 0.1449 S33: 0.0752
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3UO2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000068995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20799
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 29.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 22.90
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 23.30
REMARK 200 R MERGE FOR SHELL (I) : 0.89400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, HKL-3000
REMARK 200 STARTING MODEL: PDB ENTRY 3BVO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES BUFFER, 0.2 M AMMONIUM
REMARK 280 ACETATE, 25% PEG-3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 29.80300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.76150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.27400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.76150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.80300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.27400
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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 47
REMARK 465 HIS A 48
REMARK 465 PRO A 49
REMARK 465 ASP A 50
REMARK 465 MET A 51
REMARK 465 ALA A 52
REMARK 465 GLN A 53
REMARK 465 GLN A 54
REMARK 465 GLY A 55
REMARK 465 GLN A 179
REMARK 465 LEU A 180
REMARK 465 GLU A 181
REMARK 465 MET A 182
REMARK 465 ASN A 183
REMARK 465 HIS A 184
REMARK 465 PHE B 10
REMARK 465 ALA B 45
REMARK 465 GLN B 46
REMARK 465 HIS B 47
REMARK 465 HIS B 48
REMARK 465 PRO B 49
REMARK 465 ASP B 50
REMARK 465 MET B 51
REMARK 465 ALA B 52
REMARK 465 GLN B 53
REMARK 465 GLN B 54
REMARK 465 GLY B 55
REMARK 465 SER B 56
REMARK 465 GLU B 57
REMARK 465 GLN B 58
REMARK 465 GLU B 91
REMARK 465 GLN B 92
REMARK 465 THR B 93
REMARK 465 SER B 94
REMARK 465 ASN B 95
REMARK 465 GLU B 96
REMARK 465 VAL B 97
REMARK 465 THR B 98
REMARK 465 THR B 99
REMARK 465 SER B 100
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 HIS B 112 CG HIS B 112 CD2 0.066
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 B 134 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 PRO B 176 C - N - CA ANGL. DEV. = 9.9 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 ARG A 84 15.64 -140.19
REMARK 500 ASP A 101 59.32 -109.37
REMARK 500 THR B 89 45.92 -75.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC102101 RELATED DB: TARGETDB
DBREF 3UO2 A 10 184 UNP P53193 JAC1_YEAST 10 184
DBREF 3UO2 B 10 184 UNP P53193 JAC1_YEAST 10 184
SEQRES 1 A 175 PHE THR SER THR PHE TYR GLU LEU PHE PRO LYS THR PHE
SEQRES 2 A 175 PRO LYS LYS LEU PRO ILE TRP THR ILE ASP GLN SER ARG
SEQRES 3 A 175 LEU ARG LYS GLU TYR ARG GLN LEU GLN ALA GLN HIS HIS
SEQRES 4 A 175 PRO ASP MET ALA GLN GLN GLY SER GLU GLN SER SER THR
SEQRES 5 A 175 LEU ASN GLN ALA TYR HIS THR LEU LYS ASP PRO LEU ARG
SEQRES 6 A 175 ARG SER GLN TYR MET LEU LYS LEU LEU ARG ASN ILE ASP
SEQRES 7 A 175 LEU THR GLN GLU GLN THR SER ASN GLU VAL THR THR SER
SEQRES 8 A 175 ASP PRO GLN LEU LEU LEU LYS VAL LEU ASP ILE HIS ASP
SEQRES 9 A 175 GLU LEU SER GLN MET ASP ASP GLU ALA GLY VAL LYS LEU
SEQRES 10 A 175 LEU GLU LYS GLN ASN LYS GLU ARG ILE GLN ASP ILE GLU
SEQRES 11 A 175 ALA GLN LEU GLY GLN CYS TYR ASN ASP LYS ASP TYR ALA
SEQRES 12 A 175 ALA ALA VAL LYS LEU THR VAL GLU LEU LYS TYR TRP TYR
SEQRES 13 A 175 ASN LEU ALA LYS ALA PHE LYS ASP TRP ALA PRO GLY LYS
SEQRES 14 A 175 GLN LEU GLU MET ASN HIS
SEQRES 1 B 175 PHE THR SER THR PHE TYR GLU LEU PHE PRO LYS THR PHE
SEQRES 2 B 175 PRO LYS LYS LEU PRO ILE TRP THR ILE ASP GLN SER ARG
SEQRES 3 B 175 LEU ARG LYS GLU TYR ARG GLN LEU GLN ALA GLN HIS HIS
SEQRES 4 B 175 PRO ASP MET ALA GLN GLN GLY SER GLU GLN SER SER THR
SEQRES 5 B 175 LEU ASN GLN ALA TYR HIS THR LEU LYS ASP PRO LEU ARG
SEQRES 6 B 175 ARG SER GLN TYR MET LEU LYS LEU LEU ARG ASN ILE ASP
SEQRES 7 B 175 LEU THR GLN GLU GLN THR SER ASN GLU VAL THR THR SER
SEQRES 8 B 175 ASP PRO GLN LEU LEU LEU LYS VAL LEU ASP ILE HIS ASP
SEQRES 9 B 175 GLU LEU SER GLN MET ASP ASP GLU ALA GLY VAL LYS LEU
SEQRES 10 B 175 LEU GLU LYS GLN ASN LYS GLU ARG ILE GLN ASP ILE GLU
SEQRES 11 B 175 ALA GLN LEU GLY GLN CYS TYR ASN ASP LYS ASP TYR ALA
SEQRES 12 B 175 ALA ALA VAL LYS LEU THR VAL GLU LEU LYS TYR TRP TYR
SEQRES 13 B 175 ASN LEU ALA LYS ALA PHE LYS ASP TRP ALA PRO GLY LYS
SEQRES 14 B 175 GLN LEU GLU MET ASN HIS
FORMUL 3 HOH *63(H2 O)
HELIX 1 1 THR A 13 PHE A 18 5 6
HELIX 2 2 ASP A 32 GLN A 46 1 15
HELIX 3 3 GLU A 57 ASP A 71 1 15
HELIX 4 4 ASP A 71 ASN A 85 1 15
HELIX 5 5 GLN A 90 SER A 100 1 11
HELIX 6 6 ASP A 101 MET A 118 1 18
HELIX 7 7 ASP A 120 ASP A 148 1 29
HELIX 8 8 ASP A 150 ASP A 173 1 24
HELIX 9 9 ASP B 32 GLN B 44 1 13
HELIX 10 10 SER B 60 ASP B 71 1 12
HELIX 11 11 ASP B 71 ASN B 85 1 15
HELIX 12 12 PRO B 102 MET B 118 1 17
HELIX 13 13 ASP B 120 ASP B 148 1 29
HELIX 14 14 ASP B 150 TRP B 174 1 25
CRYST1 59.606 60.548 99.523 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 0.016777 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
