HEADER VIRAL PROTEIN 14-MAY-15 4ZTI
TITLE EBOLA VIRUS NUCLEOPROTEIN BOUND TO VP35 CHAPERONING PEPTIDE P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYMERASE COFACTOR VP35,NUCLEOPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP Q05127 RESIDUES 15-59,UNP P18272 RESIDUES 33-367;
COMPND 5 SYNONYM: NUCLEOCAPSID PROTEIN,PROTEIN N;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZAIRE EBOLAVIRUS (STRAIN MAYINGA-76);
SOURCE 3 ORGANISM_COMMON: ZEBOV;
SOURCE 4 ORGANISM_TAXID: 128952;
SOURCE 5 STRAIN: MAYINGA-76;
SOURCE 6 GENE: VP35, NP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET46
KEYWDS NUCLEOPROTEIN, CHAPERONE, RNA-BINDNG, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.N.KIRCHDOERFER,D.M.ABELSON,E.O.SAPHIRE
REVDAT 4 27-SEP-23 4ZTI 1 REMARK
REVDAT 3 04-DEC-19 4ZTI 1 REMARK
REVDAT 2 27-SEP-17 4ZTI 1 SOURCE REMARK
REVDAT 1 27-MAY-15 4ZTI 0
JRNL AUTH R.N.KIRCHDOERFER,D.M.ABELSON,S.LI,M.R.WOOD,E.O.SAPHIRE
JRNL TITL EBOLA VIRUS NUCLEOPROTEIN BOUND TO VP35 CHAPERONING PEPTIDE
JRNL TITL 2 P212121
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38215
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2050
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2741
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.25000
REMARK 3 B22 (A**2) : 1.96000
REMARK 3 B33 (A**2) : 1.29000
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): 0.273
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
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): 5381 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5282 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7256 ; 1.482 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12082 ; 3.701 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 666 ; 4.416 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;41.388 ;24.252
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 949 ;15.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.870 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 819 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6113 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1293 ; 0.009 ; 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): 2685 ; 4.359 ; 6.044
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2684 ; 4.356 ; 6.042
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3341 ; 6.339 ; 9.031
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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4ZTI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03318
REMARK 200 MONOCHROMATOR : DOUBLE SI(111) CRYSTAL CRYO
REMARK 200 -COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.15100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 1.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 4ZTA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M SODIUM FORMATE, 100 MM SODIUM
REMARK 280 ACETATE PH 4.4, VAPOR DIFFUSION, SITTING DROP, 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 47.44050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.05300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.47550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.05300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.44050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.47550
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 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 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 GLY A -13
REMARK 465 THR A -12
REMARK 465 GLN A -11
REMARK 465 ASN A -10
REMARK 465 ASP A -9
REMARK 465 ARG A -8
REMARK 465 MET A -7
REMARK 465 ILE A 20
REMARK 465 GLU A 21
REMARK 465 ASN A 22
REMARK 465 ASN A 23
REMARK 465 PRO A 24
REMARK 465 GLY A 25
REMARK 465 LEU A 26
REMARK 465 CYS A 27
REMARK 465 GLN A 31
REMARK 465 MET A 32
REMARK 465 GLN A 33
REMARK 465 GLY A 34
REMARK 465 ILE A 35
REMARK 465 VAL A 36
REMARK 465 ARG A 37
REMARK 465 PRO A 122
REMARK 465 ALA A 123
REMARK 465 VAL A 124
REMARK 465 SER A 125
REMARK 465 SER A 126
REMARK 465 GLY A 127
REMARK 465 LYS A 128
REMARK 465 ASN A 129
REMARK 465 ILE A 130
REMARK 465 LYS A 131
REMARK 465 MET A 137
REMARK 465 PRO A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 GLU A 141
REMARK 465 THR A 142
REMARK 465 THR A 143
REMARK 465 GLU A 144
REMARK 465 LEU A 363
REMARK 465 ASP A 364
REMARK 465 HIS A 365
REMARK 465 LEU A 366
REMARK 465 GLY A 367
REMARK 465 GLY B -13
REMARK 465 THR B -12
REMARK 465 GLN B -11
REMARK 465 ASN B -10
REMARK 465 ASP B -9
REMARK 465 ARG B -8
REMARK 465 MET B -7
REMARK 465 GLU B 21
REMARK 465 ASN B 22
REMARK 465 ASN B 23
REMARK 465 PRO B 24
REMARK 465 GLY B 25
REMARK 465 LEU B 26
REMARK 465 CYS B 27
REMARK 465 TYR B 28
REMARK 465 ALA B 29
REMARK 465 SER B 30
REMARK 465 GLN B 31
REMARK 465 MET B 32
REMARK 465 GLN B 33
REMARK 465 GLY B 34
REMARK 465 ILE B 35
REMARK 465 VAL B 36
REMARK 465 ARG B 37
REMARK 465 PRO B 122
REMARK 465 ALA B 123
REMARK 465 VAL B 124
REMARK 465 SER B 125
REMARK 465 SER B 126
REMARK 465 GLY B 127
REMARK 465 LYS B 128
REMARK 465 ASN B 129
REMARK 465 ALA B 136
REMARK 465 MET B 137
REMARK 465 PRO B 138
REMARK 465 GLU B 139
REMARK 465 GLU B 140
REMARK 465 GLU B 141
REMARK 465 THR B 142
REMARK 465 THR B 143
REMARK 465 GLU B 144
REMARK 465 ALA B 145
REMARK 465 LEU B 366
REMARK 465 GLY B 367
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 PHE A 17 49.48 -85.38
REMARK 500 CYS A 18 -157.42 -84.97
REMARK 500 ASN A 48 47.26 -107.36
REMARK 500 GLN A 67 -109.22 56.82
REMARK 500 ASN A 301 59.06 38.36
REMARK 500 LEU A 308 50.10 -111.48
REMARK 500 CYS B 18 -155.88 -138.80
REMARK 500 ASP B 19 65.22 -119.37
REMARK 500 ASN B 48 60.44 -117.26
REMARK 500 GLN B 67 -110.92 45.85
REMARK 500 GLU B 119 0.39 -62.07
REMARK 500 LYS B 131 -0.40 -59.70
REMARK 500 ALA B 223 123.82 -39.84
REMARK 500 ASN B 301 43.78 35.96
REMARK 500 ASP B 364 45.85 -101.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 509 DISTANCE = 6.27 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZTA RELATED DB: PDB
REMARK 900 4ZTA CONTAINS THE SAME PROTEIN IN SPACE GROUP I212121
REMARK 900 RELATED ID: 4ZTG RELATED DB: PDB
REMARK 900 4ZTG CONTAINS THE SAME PROTEIN IN SPACE GROUP P22121
DBREF 4ZTI A -12 32 UNP Q05127 VP35_EBOZM 15 59
DBREF 4ZTI A 33 367 UNP P18272 NCAP_EBOZM 33 367
DBREF 4ZTI B -12 32 UNP Q05127 VP35_EBOZM 15 59
DBREF 4ZTI B 33 367 UNP P18272 NCAP_EBOZM 33 367
SEQADV 4ZTI GLY A -13 UNP Q05127 EXPRESSION TAG
SEQADV 4ZTI GLY B -13 UNP Q05127 EXPRESSION TAG
SEQRES 1 A 381 GLY THR GLN ASN ASP ARG MET PRO GLY PRO GLU LEU SER
SEQRES 2 A 381 GLY TRP ILE SER GLU GLN LEU MET THR GLY ARG ILE PRO
SEQRES 3 A 381 VAL SER ASP ILE PHE CYS ASP ILE GLU ASN ASN PRO GLY
SEQRES 4 A 381 LEU CYS TYR ALA SER GLN MET GLN GLY ILE VAL ARG GLN
SEQRES 5 A 381 ARG VAL ILE PRO VAL TYR GLN VAL ASN ASN LEU GLU GLU
SEQRES 6 A 381 ILE CYS GLN LEU ILE ILE GLN ALA PHE GLU ALA GLY VAL
SEQRES 7 A 381 ASP PHE GLN GLU SER ALA ASP SER PHE LEU LEU MET LEU
SEQRES 8 A 381 CYS LEU HIS HIS ALA TYR GLN GLY ASP TYR LYS LEU PHE
SEQRES 9 A 381 LEU GLU SER GLY ALA VAL LYS TYR LEU GLU GLY HIS GLY
SEQRES 10 A 381 PHE ARG PHE GLU VAL LYS LYS ARG ASP GLY VAL LYS ARG
SEQRES 11 A 381 LEU GLU GLU LEU LEU PRO ALA VAL SER SER GLY LYS ASN
SEQRES 12 A 381 ILE LYS ARG THR LEU ALA ALA MET PRO GLU GLU GLU THR
SEQRES 13 A 381 THR GLU ALA ASN ALA GLY GLN PHE LEU SER PHE ALA SER
SEQRES 14 A 381 LEU PHE LEU PRO LYS LEU VAL VAL GLY GLU LYS ALA CYS
SEQRES 15 A 381 LEU GLU LYS VAL GLN ARG GLN ILE GLN VAL HIS ALA GLU
SEQRES 16 A 381 GLN GLY LEU ILE GLN TYR PRO THR ALA TRP GLN SER VAL
SEQRES 17 A 381 GLY HIS MET MET VAL ILE PHE ARG LEU MET ARG THR ASN
SEQRES 18 A 381 PHE LEU ILE LYS PHE LEU LEU ILE HIS GLN GLY MET HIS
SEQRES 19 A 381 MET VAL ALA GLY HIS ASP ALA ASN ASP ALA VAL ILE SER
SEQRES 20 A 381 ASN SER VAL ALA GLN ALA ARG PHE SER GLY LEU LEU ILE
SEQRES 21 A 381 VAL LYS THR VAL LEU ASP HIS ILE LEU GLN LYS THR GLU
SEQRES 22 A 381 ARG GLY VAL ARG LEU HIS PRO LEU ALA ARG THR ALA LYS
SEQRES 23 A 381 VAL LYS ASN GLU VAL ASN SER PHE LYS ALA ALA LEU SER
SEQRES 24 A 381 SER LEU ALA LYS HIS GLY GLU TYR ALA PRO PHE ALA ARG
SEQRES 25 A 381 LEU LEU ASN LEU SER GLY VAL ASN ASN LEU GLU HIS GLY
SEQRES 26 A 381 LEU PHE PRO GLN LEU SER ALA ILE ALA LEU GLY VAL ALA
SEQRES 27 A 381 THR ALA HIS GLY SER THR LEU ALA GLY VAL ASN VAL GLY
SEQRES 28 A 381 GLU GLN TYR GLN GLN LEU ARG GLU ALA ALA THR GLU ALA
SEQRES 29 A 381 GLU LYS GLN LEU GLN GLN TYR ALA GLU SER ARG GLU LEU
SEQRES 30 A 381 ASP HIS LEU GLY
SEQRES 1 B 381 GLY THR GLN ASN ASP ARG MET PRO GLY PRO GLU LEU SER
SEQRES 2 B 381 GLY TRP ILE SER GLU GLN LEU MET THR GLY ARG ILE PRO
SEQRES 3 B 381 VAL SER ASP ILE PHE CYS ASP ILE GLU ASN ASN PRO GLY
SEQRES 4 B 381 LEU CYS TYR ALA SER GLN MET GLN GLY ILE VAL ARG GLN
SEQRES 5 B 381 ARG VAL ILE PRO VAL TYR GLN VAL ASN ASN LEU GLU GLU
SEQRES 6 B 381 ILE CYS GLN LEU ILE ILE GLN ALA PHE GLU ALA GLY VAL
SEQRES 7 B 381 ASP PHE GLN GLU SER ALA ASP SER PHE LEU LEU MET LEU
SEQRES 8 B 381 CYS LEU HIS HIS ALA TYR GLN GLY ASP TYR LYS LEU PHE
SEQRES 9 B 381 LEU GLU SER GLY ALA VAL LYS TYR LEU GLU GLY HIS GLY
SEQRES 10 B 381 PHE ARG PHE GLU VAL LYS LYS ARG ASP GLY VAL LYS ARG
SEQRES 11 B 381 LEU GLU GLU LEU LEU PRO ALA VAL SER SER GLY LYS ASN
SEQRES 12 B 381 ILE LYS ARG THR LEU ALA ALA MET PRO GLU GLU GLU THR
SEQRES 13 B 381 THR GLU ALA ASN ALA GLY GLN PHE LEU SER PHE ALA SER
SEQRES 14 B 381 LEU PHE LEU PRO LYS LEU VAL VAL GLY GLU LYS ALA CYS
SEQRES 15 B 381 LEU GLU LYS VAL GLN ARG GLN ILE GLN VAL HIS ALA GLU
SEQRES 16 B 381 GLN GLY LEU ILE GLN TYR PRO THR ALA TRP GLN SER VAL
SEQRES 17 B 381 GLY HIS MET MET VAL ILE PHE ARG LEU MET ARG THR ASN
SEQRES 18 B 381 PHE LEU ILE LYS PHE LEU LEU ILE HIS GLN GLY MET HIS
SEQRES 19 B 381 MET VAL ALA GLY HIS ASP ALA ASN ASP ALA VAL ILE SER
SEQRES 20 B 381 ASN SER VAL ALA GLN ALA ARG PHE SER GLY LEU LEU ILE
SEQRES 21 B 381 VAL LYS THR VAL LEU ASP HIS ILE LEU GLN LYS THR GLU
SEQRES 22 B 381 ARG GLY VAL ARG LEU HIS PRO LEU ALA ARG THR ALA LYS
SEQRES 23 B 381 VAL LYS ASN GLU VAL ASN SER PHE LYS ALA ALA LEU SER
SEQRES 24 B 381 SER LEU ALA LYS HIS GLY GLU TYR ALA PRO PHE ALA ARG
SEQRES 25 B 381 LEU LEU ASN LEU SER GLY VAL ASN ASN LEU GLU HIS GLY
SEQRES 26 B 381 LEU PHE PRO GLN LEU SER ALA ILE ALA LEU GLY VAL ALA
SEQRES 27 B 381 THR ALA HIS GLY SER THR LEU ALA GLY VAL ASN VAL GLY
SEQRES 28 B 381 GLU GLN TYR GLN GLN LEU ARG GLU ALA ALA THR GLU ALA
SEQRES 29 B 381 GLU LYS GLN LEU GLN GLN TYR ALA GLU SER ARG GLU LEU
SEQRES 30 B 381 ASP HIS LEU GLY
FORMUL 3 HOH *223(H2 O)
HELIX 1 AA1 GLY A 0 THR A 8 1 9
HELIX 2 AA2 PRO A 12 ILE A 16 5 5
HELIX 3 AA3 ASN A 48 GLY A 63 1 16
HELIX 4 AA4 PHE A 66 GLU A 68 5 3
HELIX 5 AA5 SER A 69 TYR A 83 1 15
HELIX 6 AA6 ASP A 86 SER A 93 1 8
HELIX 7 AA7 SER A 93 HIS A 102 1 10
HELIX 8 AA8 ARG A 116 LEU A 120 5 5
HELIX 9 AA9 ARG A 132 ALA A 136 5 5
HELIX 10 AB1 ASN A 146 LEU A 156 1 11
HELIX 11 AB2 GLY A 164 GLN A 182 1 19
HELIX 12 AB3 PRO A 188 GLN A 192 5 5
HELIX 13 AB4 SER A 193 ASN A 207 1 15
HELIX 14 AB5 ASN A 207 HIS A 220 1 14
HELIX 15 AB6 ASP A 226 ALA A 239 1 14
HELIX 16 AB7 LEU A 244 ILE A 254 1 11
HELIX 17 AB8 PRO A 266 LYS A 272 5 7
HELIX 18 AB9 VAL A 273 LYS A 289 1 17
HELIX 19 AC1 HIS A 290 ALA A 297 5 8
HELIX 20 AC2 GLY A 304 LEU A 308 5 5
HELIX 21 AC3 GLU A 309 LEU A 312 5 4
HELIX 22 AC4 PHE A 313 ALA A 326 1 14
HELIX 23 AC5 GLY A 337 GLN A 339 5 3
HELIX 24 AC6 TYR A 340 SER A 360 1 21
HELIX 25 AC7 GLY B 0 THR B 8 1 9
HELIX 26 AC8 PRO B 12 ILE B 16 5 5
HELIX 27 AC9 ASN B 48 GLY B 63 1 16
HELIX 28 AD1 PHE B 66 GLU B 68 5 3
HELIX 29 AD2 SER B 69 TYR B 83 1 15
HELIX 30 AD3 ASP B 86 GLU B 92 1 7
HELIX 31 AD4 SER B 93 GLY B 101 1 9
HELIX 32 AD5 ARG B 116 LEU B 120 5 5
HELIX 33 AD6 ALA B 147 LEU B 156 1 10
HELIX 34 AD7 GLY B 164 GLN B 182 1 19
HELIX 35 AD8 PRO B 188 GLN B 192 5 5
HELIX 36 AD9 SER B 193 ASN B 207 1 15
HELIX 37 AE1 ASN B 207 MET B 221 1 15
HELIX 38 AE2 ASP B 226 ALA B 239 1 14
HELIX 39 AE3 LEU B 244 ILE B 254 1 11
HELIX 40 AE4 PRO B 266 LYS B 272 5 7
HELIX 41 AE5 VAL B 273 LYS B 289 1 17
HELIX 42 AE6 HIS B 290 ALA B 297 5 8
HELIX 43 AE7 GLY B 304 LEU B 312 5 9
HELIX 44 AE8 PHE B 313 HIS B 327 1 15
HELIX 45 AE9 TYR B 340 ASP B 364 1 25
SHEET 1 AA1 2 ARG A 39 GLN A 45 0
SHEET 2 AA1 2 PHE A 104 LYS A 110 1 O ARG A 105 N ILE A 41
SHEET 1 AA2 2 LEU A 255 THR A 258 0
SHEET 2 AA2 2 GLY A 261 LEU A 264 -1 O ARG A 263 N GLN A 256
SHEET 1 AA3 2 ARG B 39 GLN B 45 0
SHEET 2 AA3 2 PHE B 104 LYS B 110 1 O ARG B 105 N ILE B 41
SHEET 1 AA4 2 LEU B 255 THR B 258 0
SHEET 2 AA4 2 GLY B 261 LEU B 264 -1 O ARG B 263 N GLN B 256
CRYST1 94.881 94.951 112.106 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 0.010540 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008920 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
