HEADER DNA BINDING PROTEIN 01-NOV-10 3PGG
TITLE CRYSTAL STRUCTURE OF CRYPTOSPORIDIUM PARVUM U6 SNRNA-ASSOCIATED SM-
TITLE 2 LIKE PROTEIN LSM5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM5. SM DOMAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;
SOURCE 3 ORGANISM_TAXID: 5807;
SOURCE 4 GENE: CGD7_4580;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P28-LIC-THROMBIN DERIVED FROM PET28
KEYWDS U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN, LSM5, DNA BINDING PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,M.GAO,Y.ZHAO,J.LEW,G.A.WASNEY,I.KOZIERADZKI,M.VEDADI,
AUTHOR 2 A.EDWARDS,C.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,A.BOCHKAREV,R.HUI,
AUTHOR 3 J.ARTZ,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 21-FEB-24 3PGG 1 REMARK
REVDAT 2 08-NOV-17 3PGG 1 REMARK
REVDAT 1 02-FEB-11 3PGG 0
SPRSDE 02-FEB-11 3PGG 2FWK
JRNL AUTH M.VEDADI,J.LEW,J.ARTZ,M.AMANI,Y.ZHAO,A.DONG,G.A.WASNEY,
JRNL AUTH 2 M.GAO,T.HILLS,S.BROKX,W.QIU,S.SHARMA,A.DIASSITI,Z.ALAM,
JRNL AUTH 3 M.MELONE,A.MULICHAK,A.WERNIMONT,J.BRAY,P.LOPPNAU,
JRNL AUTH 4 O.PLOTNIKOVA,K.NEWBERRY,E.SUNDARARAJAN,S.HOUSTON,J.WALKER,
JRNL AUTH 5 W.TEMPEL,A.BOCHKAREV,I.KOZIERADZKI,A.EDWARDS,C.ARROWSMITH,
JRNL AUTH 6 D.ROOS,K.KAIN,R.HUI
JRNL TITL GENOME-SCALE PROTEIN EXPRESSION AND STRUCTURAL BIOLOGY OF
JRNL TITL 2 PLASMODIUM FALCIPARUM AND RELATED APICOMPLEXAN ORGANISMS.
JRNL REF MOL.BIOCHEM.PARASITOL. V. 151 100 2007
JRNL REFN ISSN 0166-6851
JRNL PMID 17125854
JRNL DOI 10.1016/J.MOLBIOPARA.2006.10.011
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 15457
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 809
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) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1083
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1154
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.84000
REMARK 3 B22 (A**2) : -5.84000
REMARK 3 B33 (A**2) : 11.68000
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): 0.033
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.207
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.261
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1166 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1578 ; 1.298 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 154 ; 9.373 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 46 ;34.889 ;25.652
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 186 ;16.031 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;16.450 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 190 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 862 ; 0.017 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 772 ; 2.010 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1221 ; 3.186 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 394 ; 4.606 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 357 ; 6.773 ; 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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.601
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H+K,-K,-L
REMARK 3 TWIN FRACTION : 0.399
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 : 1.40
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 3PGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VERIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 54.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.79500
REMARK 200 R SYM FOR SHELL (I) : 0.79500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER V. 1.3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.05 M NA CITRATE, 100 MM BISTRIS
REMARK 280 PH6.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-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 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 0.00000
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 0.00000
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 0.00000
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 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 300 REMARK: HEXAMERIC
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 101.16300
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 50.58150
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 87.60973
REMARK 350 BIOMT3 3 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 SER A 1
REMARK 465 TYR A 2
REMARK 465 LYS A 3
REMARK 465 VAL A 4
REMARK 465 ASN A 5
REMARK 465 TYR A 6
REMARK 465 MET A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 PRO A 11
REMARK 465 ALA A 12
REMARK 465 ASN A 13
REMARK 465 LYS A 14
REMARK 465 SER A 15
REMARK 465 GLN A 16
REMARK 465 GLY A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 ASN A 20
REMARK 465 GLN A 21
REMARK 465 LYS A 22
REMARK 465 GLY A 23
REMARK 465 GLY A 24
REMARK 465 GLU A 78
REMARK 465 GLU A 79
REMARK 465 ASP A 80
REMARK 465 ILE A 81
REMARK 465 SER A 82
REMARK 465 GLY A 83
REMARK 465 GLY A 84
REMARK 465 ASN A 85
REMARK 465 LYS A 86
REMARK 465 LYS A 87
REMARK 465 LEU A 88
REMARK 465 ASP A 114
REMARK 465 PRO A 115
REMARK 465 ASP A 116
REMARK 465 SER A 117
REMARK 465 PHE A 118
REMARK 465 ASN A 119
REMARK 465 PHE A 120
REMARK 465 SER A 121
REMARK 465 SER B 1
REMARK 465 TYR B 2
REMARK 465 LYS B 3
REMARK 465 VAL B 4
REMARK 465 ASN B 5
REMARK 465 TYR B 6
REMARK 465 MET B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 PRO B 11
REMARK 465 ALA B 12
REMARK 465 ASN B 13
REMARK 465 LYS B 14
REMARK 465 SER B 15
REMARK 465 GLN B 16
REMARK 465 GLY B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 ASN B 20
REMARK 465 GLN B 21
REMARK 465 LYS B 22
REMARK 465 ASP B 77
REMARK 465 GLU B 78
REMARK 465 GLU B 79
REMARK 465 ASP B 80
REMARK 465 ILE B 81
REMARK 465 SER B 82
REMARK 465 GLY B 83
REMARK 465 GLY B 84
REMARK 465 ASN B 85
REMARK 465 LYS B 86
REMARK 465 LYS B 87
REMARK 465 LEU B 88
REMARK 465 PRO B 115
REMARK 465 ASP B 116
REMARK 465 SER B 117
REMARK 465 PHE B 118
REMARK 465 ASN B 119
REMARK 465 PHE B 120
REMARK 465 SER B 121
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 ASN A 25 CG OD1 ND2
REMARK 470 ILE A 26 CD1
REMARK 470 ILE A 27 CG1 CG2 CD1
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 ILE A 37 CD1
REMARK 470 LYS A 75 CG CD CE NZ
REMARK 470 ASP A 77 CG OD1 OD2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 91 CG1 CG2
REMARK 470 LYS B 35 CD CE NZ
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 ARG B 56 CZ NH1 NH2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 LYS B 89 CG CD CE NZ
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 95 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 ASP B 114 CG OD1 OD2
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 GLU A 97 -125.44 -102.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 67 -11.21
REMARK 500 ILE A 99 -10.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3PGG A 1 121 UNP Q5CXX3 Q5CXX3_CRYPV 1 121
DBREF 3PGG B 1 121 UNP Q5CXX3 Q5CXX3_CRYPV 1 121
SEQRES 1 A 121 SER TYR LYS VAL ASN TYR MET SER GLU THR PRO ALA ASN
SEQRES 2 A 121 LYS SER GLN GLY GLY SER ASN GLN LYS GLY GLY ASN ILE
SEQRES 3 A 121 ILE LEU PRO LEU ALA LEU ILE ASP LYS CYS ILE GLY ASN
SEQRES 4 A 121 ARG ILE TYR VAL VAL MET LYS GLY ASP LYS GLU PHE SER
SEQRES 5 A 121 GLY VAL LEU ARG GLY PHE ASP GLU TYR VAL ASN MET VAL
SEQRES 6 A 121 LEU ASP ASP VAL GLN GLU TYR GLY PHE LYS ALA ASP GLU
SEQRES 7 A 121 GLU ASP ILE SER GLY GLY ASN LYS LYS LEU LYS ARG VAL
SEQRES 8 A 121 MET VAL ASN ARG LEU GLU THR ILE LEU LEU SER GLY ASN
SEQRES 9 A 121 ASN VAL ALA MET LEU VAL PRO GLY GLY ASP PRO ASP SER
SEQRES 10 A 121 PHE ASN PHE SER
SEQRES 1 B 121 SER TYR LYS VAL ASN TYR MET SER GLU THR PRO ALA ASN
SEQRES 2 B 121 LYS SER GLN GLY GLY SER ASN GLN LYS GLY GLY ASN ILE
SEQRES 3 B 121 ILE LEU PRO LEU ALA LEU ILE ASP LYS CYS ILE GLY ASN
SEQRES 4 B 121 ARG ILE TYR VAL VAL MET LYS GLY ASP LYS GLU PHE SER
SEQRES 5 B 121 GLY VAL LEU ARG GLY PHE ASP GLU TYR VAL ASN MET VAL
SEQRES 6 B 121 LEU ASP ASP VAL GLN GLU TYR GLY PHE LYS ALA ASP GLU
SEQRES 7 B 121 GLU ASP ILE SER GLY GLY ASN LYS LYS LEU LYS ARG VAL
SEQRES 8 B 121 MET VAL ASN ARG LEU GLU THR ILE LEU LEU SER GLY ASN
SEQRES 9 B 121 ASN VAL ALA MET LEU VAL PRO GLY GLY ASP PRO ASP SER
SEQRES 10 B 121 PHE ASN PHE SER
FORMUL 3 HOH *27(H2 O)
HELIX 1 1 LEU A 28 CYS A 36 1 9
HELIX 2 2 SER A 102 ASN A 104 5 3
HELIX 3 3 LEU B 28 CYS B 36 1 9
SHEET 1 A 3 ARG A 90 LEU A 96 0
SHEET 2 A 3 MET A 64 PHE A 74 -1 N GLU A 71 O ASN A 94
SHEET 3 A 3 ILE A 99 LEU A 101 -1 O LEU A 101 N MET A 64
SHEET 1 B10 ARG A 90 LEU A 96 0
SHEET 2 B10 MET A 64 PHE A 74 -1 N GLU A 71 O ASN A 94
SHEET 3 B10 GLU A 50 PHE A 58 -1 N VAL A 54 O ASP A 67
SHEET 4 B10 ARG A 40 MET A 45 -1 N ILE A 41 O GLY A 53
SHEET 5 B10 VAL A 106 PRO A 111 -1 O VAL A 110 N TYR A 42
SHEET 6 B10 ARG B 90 LEU B 101 -1 O LEU B 100 N LEU A 109
SHEET 7 B10 MET B 64 PHE B 74 -1 N GLY B 73 O VAL B 91
SHEET 8 B10 LYS B 49 PHE B 58 -1 N VAL B 54 O ASP B 67
SHEET 9 B10 ARG B 40 MET B 45 -1 N ILE B 41 O GLY B 53
SHEET 10 B10 VAL B 106 VAL B 110 -1 O MET B 108 N VAL B 44
CRYST1 101.163 101.163 49.092 90.00 90.00 120.00 P 3 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 0.009885 0.005707 0.000000 0.00000
SCALE2 0.000000 0.011414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
