HEADER STRUCTURAL PROTEIN/DNA 14-JUN-05 1ZZI
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE THIRD KH DOMAIN OF HNRNP K IN
TITLE 2 COMPLEX WITH SSDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*TP*CP*CP*CP*C)-3';
COMPND 3 CHAIN: C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K;
COMPND 7 CHAIN: A, B;
COMPND 8 FRAGMENT: KH3 DOMAIN;
COMPND 9 SYNONYM: HNRNP K, TRANSFORMATION UP-REGULATED NUCLEAR PROTEIN, TUNP;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS PROTEIN-SSDNA COMPLEX, STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.H.BACKE,A.C.MESSIAS,R.B.RAVELLI,M.SATTLER,S.CUSACK
REVDAT 4 13-MAR-24 1ZZI 1 SEQADV
REVDAT 3 13-JUL-11 1ZZI 1 VERSN
REVDAT 2 24-FEB-09 1ZZI 1 VERSN
REVDAT 1 09-AUG-05 1ZZI 0
JRNL AUTH P.H.BACKE,A.C.MESSIAS,R.B.RAVELLI,M.SATTLER,S.CUSACK
JRNL TITL X-RAY CRYSTALLOGRAPHIC AND NMR STUDIES OF THE THIRD KH
JRNL TITL 2 DOMAIN OF HNRNP K IN COMPLEX WITH SINGLE-STRANDED NUCLEIC
JRNL TITL 3 ACIDS
JRNL REF STRUCTURE V. 13 1055 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16004877
JRNL DOI 10.1016/J.STR.2005.04.008
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 15030
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 795
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 866
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1235
REMARK 3 NUCLEIC ACID ATOMS : 209
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 136
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : 0.88000
REMARK 3 B33 (A**2) : -1.32000
REMARK 3 B12 (A**2) : 0.44000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.410
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1488 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2041 ; 1.894 ; 2.147
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 161 ; 5.866 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;38.096 ;25.926
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 243 ;16.098 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;24.933 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 236 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1029 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 785 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1065 ; 0.321 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 157 ; 0.162 ; 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): 75 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.203 ; 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): 815 ; 1.071 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1293 ; 1.742 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 764 ; 2.768 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 748 ; 3.793 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 89
REMARK 3 RESIDUE RANGE : C 1 C 6
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9725 39.5546 21.0852
REMARK 3 T TENSOR
REMARK 3 T11: -0.1696 T22: -0.1753
REMARK 3 T33: -0.1178 T12: 0.0086
REMARK 3 T13: -0.0125 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.7683 L22: 1.9498
REMARK 3 L33: 13.0701 L12: -0.0850
REMARK 3 L13: 2.8545 L23: -0.4235
REMARK 3 S TENSOR
REMARK 3 S11: 0.1452 S12: -0.1007 S13: -0.2148
REMARK 3 S21: -0.0017 S22: -0.0329 S23: 0.0872
REMARK 3 S31: 0.5184 S32: -0.3394 S33: -0.1123
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 11 B 89
REMARK 3 RESIDUE RANGE : D 2 D 6
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9822 39.8017 -0.9654
REMARK 3 T TENSOR
REMARK 3 T11: -0.1368 T22: -0.1809
REMARK 3 T33: -0.1449 T12: 0.0421
REMARK 3 T13: -0.0080 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.6045 L22: 2.8770
REMARK 3 L33: 5.3514 L12: -0.1595
REMARK 3 L13: 0.7431 L23: 2.3654
REMARK 3 S TENSOR
REMARK 3 S11: 0.0645 S12: -0.0550 S13: 0.1095
REMARK 3 S21: -0.1630 S22: -0.2221 S23: 0.1032
REMARK 3 S31: -0.1630 S32: -0.2875 S33: 0.1576
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-02
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94
REMARK 200 MONOCHROMATOR : KHOZU DUAL CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15859
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 34.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS HCL, MAGNESIUM
REMARK 280 CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.96367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.92733
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.92733
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.96367
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: ASYMMETRIC UNIT CONTAINS TWO KH3-SSDNA COMPLEXES (CHAINS A+
REMARK 300 C AND B+D) WITH APPROXIMATELY 2-FOLD NCS
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 APPLY THE FOLLOWING TO CHAINS: C, 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 8
REMARK 465 ALA B 9
REMARK 465 MET B 10
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 DC D 1 O5' C5' C4' O4' C3' C2' C1'
REMARK 470 DC D 1 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC D 1 C6
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 DC D 6 O3' DC D 6 C3' -0.053
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 DC C 4 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT D 2 O4' - C1' - N1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 DC D 3 O4' - C1' - N1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 DC D 4 N3 - C2 - O2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DC D 6 O4' - C1' - N1 ANGL. DEV. = -12.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZZJ RELATED DB: PDB
REMARK 900 RELATED ID: 1ZZK RELATED DB: PDB
DBREF 1ZZI A 11 89 UNP P61978 HNRPK_HUMAN 385 463
DBREF 1ZZI B 11 89 UNP P61978 HNRPK_HUMAN 385 463
DBREF 1ZZI C 1 6 PDB 1ZZI 1ZZI 1 6
DBREF 1ZZI D 1 6 PDB 1ZZI 1ZZI 1 6
SEQADV 1ZZI GLY A 8 UNP P61978 CLONING ARTIFACT
SEQADV 1ZZI ALA A 9 UNP P61978 CLONING ARTIFACT
SEQADV 1ZZI MET A 10 UNP P61978 CLONING ARTIFACT
SEQADV 1ZZI GLY B 8 UNP P61978 CLONING ARTIFACT
SEQADV 1ZZI ALA B 9 UNP P61978 CLONING ARTIFACT
SEQADV 1ZZI MET B 10 UNP P61978 CLONING ARTIFACT
SEQRES 1 C 6 DC DT DC DC DC DC
SEQRES 1 D 6 DC DT DC DC DC DC
SEQRES 1 A 82 GLY ALA MET GLY PRO ILE ILE THR THR GLN VAL THR ILE
SEQRES 2 A 82 PRO LYS ASP LEU ALA GLY SER ILE ILE GLY LYS GLY GLY
SEQRES 3 A 82 GLN ARG ILE LYS GLN ILE ARG HIS GLU SER GLY ALA SER
SEQRES 4 A 82 ILE LYS ILE ASP GLU PRO LEU GLU GLY SER GLU ASP ARG
SEQRES 5 A 82 ILE ILE THR ILE THR GLY THR GLN ASP GLN ILE GLN ASN
SEQRES 6 A 82 ALA GLN TYR LEU LEU GLN ASN SER VAL LYS GLN TYR SER
SEQRES 7 A 82 GLY LYS PHE PHE
SEQRES 1 B 82 GLY ALA MET GLY PRO ILE ILE THR THR GLN VAL THR ILE
SEQRES 2 B 82 PRO LYS ASP LEU ALA GLY SER ILE ILE GLY LYS GLY GLY
SEQRES 3 B 82 GLN ARG ILE LYS GLN ILE ARG HIS GLU SER GLY ALA SER
SEQRES 4 B 82 ILE LYS ILE ASP GLU PRO LEU GLU GLY SER GLU ASP ARG
SEQRES 5 B 82 ILE ILE THR ILE THR GLY THR GLN ASP GLN ILE GLN ASN
SEQRES 6 B 82 ALA GLN TYR LEU LEU GLN ASN SER VAL LYS GLN TYR SER
SEQRES 7 B 82 GLY LYS PHE PHE
FORMUL 5 HOH *136(H2 O)
HELIX 1 1 LEU A 24 GLY A 30 1 7
HELIX 2 2 GLY A 33 GLY A 44 1 12
HELIX 3 3 THR A 66 GLN A 83 1 18
HELIX 4 4 LEU B 24 GLY B 30 1 7
HELIX 5 5 GLY B 33 GLY B 44 1 12
HELIX 6 6 THR B 66 VAL B 81 1 16
HELIX 7 7 LYS B 82 TYR B 84 5 3
SHEET 1 A 3 ILE A 14 PRO A 21 0
SHEET 2 A 3 ASP A 58 GLY A 65 -1 O ILE A 63 N THR A 16
SHEET 3 A 3 SER A 46 ILE A 49 -1 N SER A 46 O THR A 64
SHEET 1 B 3 ILE B 14 PRO B 21 0
SHEET 2 B 3 ASP B 58 GLY B 65 -1 O GLY B 65 N ILE B 14
SHEET 3 B 3 SER B 46 ILE B 49 -1 N SER B 46 O THR B 64
CRYST1 52.590 52.590 104.891 90.00 90.00 120.00 P 31 2 1 12
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 0.019015 0.010978 0.000000 0.00000
SCALE2 0.000000 0.021957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009534 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
