HEADER VIRAL PROTEIN/CYTOKINE 30-APR-15 4ZKB
TITLE THE CHEMOKINE BINDING PROTEIN OF ORF VIRUS COMPLEXED WITH CCL3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOKINE BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 17-286;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: C-C MOTIF CHEMOKINE 3;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 24-92;
COMPND 10 SYNONYM: G0/G1 SWITCH REGULATORY PROTEIN 19-1,MACROPHAGE INFLAMMATORY
COMPND 11 PROTEIN 1-ALPHA,MIP-1-ALPHA,PAT 464.1,SIS-BETA,SMALL-INDUCIBLE
COMPND 12 CYTOKINE A3,TONSILLAR LYMPHOCYTE LD78 ALPHA PROTEIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORF VIRUS (STRAIN NZ2);
SOURCE 3 ORGANISM_COMMON: ORFV;
SOURCE 4 ORGANISM_TAXID: 10259;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-6E;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTT5;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CCL3, G0S19-1, MIP1A, SCYA3;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-6E;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PTT5
KEYWDS COMPLEX, ORF CHEMOKINE BINDING PROTEIN, CCL3, VIRAL PROTEIN-CYTOKINE
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.KNAPP,Y.NAKATANI,K.L.KRAUSE
REVDAT 5 27-SEP-23 4ZKB 1 HETSYN
REVDAT 4 29-JUL-20 4ZKB 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUN-18 4ZKB 1 TITLE SOURCE KEYWDS JRNL
REVDAT 3 2 1 REMARK
REVDAT 2 15-JUL-15 4ZKB 1 JRNL
REVDAT 1 08-JUL-15 4ZKB 0
JRNL AUTH R.M.COUNAGO,K.M.KNAPP,Y.NAKATANI,S.B.FLEMING,M.CORBETT,
JRNL AUTH 2 L.M.WISE,A.A.MERCER,K.L.KRAUSE
JRNL TITL STRUCTURES OF ORF VIRUS CHEMOKINE BINDING PROTEIN IN COMPLEX
JRNL TITL 2 WITH HOST CHEMOKINES REVEAL CLUES TO BROAD BINDING
JRNL TITL 3 SPECIFICITY.
JRNL REF STRUCTURE V. 23 1199 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26095031
JRNL DOI 10.1016/J.STR.2015.04.023
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 12641
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) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 692
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 902
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1852
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08000
REMARK 3 B22 (A**2) : 2.08000
REMARK 3 B33 (A**2) : -4.16000
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): 0.492
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.372
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.353
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.375
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.837
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1959 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1675 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2684 ; 1.444 ; 2.004
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3811 ; 0.795 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 262 ; 7.484 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 67 ;34.426 ;24.328
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 241 ;18.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.997 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2247 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 406 ; 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): 1063 ; 1.587 ; 4.302
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1062 ; 1.587 ; 4.300
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1320 ; 2.635 ; 6.449
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1321 ; 2.634 ; 6.451
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 896 ; 2.659 ; 4.730
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 897 ; 2.657 ; 4.731
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1364 ; 4.285 ; 7.012
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2176 ; 5.335 ;36.541
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2177 ; 5.334 ;36.552
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 11 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4148 -13.6715 12.0863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.3164
REMARK 3 T33: 0.0789 T12: 0.0475
REMARK 3 T13: -0.0304 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 2.0954 L22: 2.4897
REMARK 3 L33: 7.9993 L12: 0.3791
REMARK 3 L13: -1.1720 L23: -1.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0397 S12: -0.4371 S13: 0.0142
REMARK 3 S21: -0.1541 S22: -0.0269 S23: 0.4306
REMARK 3 S31: -0.1817 S32: -0.6727 S33: -0.0128
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 8 B 64
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6106 5.4826 19.8154
REMARK 3 T TENSOR
REMARK 3 T11: 0.8962 T22: 0.7882
REMARK 3 T33: 0.4088 T12: 0.1602
REMARK 3 T13: -0.0728 T23: -0.2088
REMARK 3 L TENSOR
REMARK 3 L11: 6.6921 L22: 5.7028
REMARK 3 L33: 7.7906 L12: 1.6936
REMARK 3 L13: -2.0456 L23: 0.5480
REMARK 3 S TENSOR
REMARK 3 S11: 0.1814 S12: -1.0155 S13: 1.1418
REMARK 3 S21: 0.2215 S22: -0.6392 S23: -0.1688
REMARK 3 S31: -1.6641 S32: -0.1558 S33: 0.4578
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 4ZKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 93.2
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13416
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 47.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.75700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4P5I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE, 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE PH5.6, 2.0M
REMARK 280 AMMONIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.01000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 139.51500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.50500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 139.51500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.50500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.01000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 GLN A 7
REMARK 465 ARG A 8
REMARK 465 SER A 9
REMARK 465 ASN A 10
REMARK 465 GLU A 158
REMARK 465 PRO A 159
REMARK 465 THR A 160
REMARK 465 THR A 161
REMARK 465 THR A 162
REMARK 465 PRO A 163
REMARK 465 PRO A 164
REMARK 465 SER A 165
REMARK 465 PRO A 166
REMARK 465 VAL A 167
REMARK 465 THR A 168
REMARK 465 THR A 169
REMARK 465 THR A 170
REMARK 465 LEU A 171
REMARK 465 SER A 172
REMARK 465 SER A 173
REMARK 465 THR A 174
REMARK 465 THR A 175
REMARK 465 PRO A 176
REMARK 465 ASP A 177
REMARK 465 LEU A 178
REMARK 465 ASN A 179
REMARK 465 GLU A 180
REMARK 465 GLU A 181
REMARK 465 ASN A 182
REMARK 465 THR A 183
REMARK 465 GLU A 184
REMARK 465 ASN A 185
REMARK 465 THR A 186
REMARK 465 PRO A 187
REMARK 465 THR A 188
REMARK 465 THR A 189
REMARK 465 THR A 190
REMARK 465 GLY A 191
REMARK 465 ALA A 192
REMARK 465 SER A 193
REMARK 465 VAL A 194
REMARK 465 ASP A 195
REMARK 465 ARG A 196
REMARK 465 LYS A 197
REMARK 465 ARG A 198
REMARK 465 ASN A 270
REMARK 465 GLU A 271
REMARK 465 ASN A 272
REMARK 465 LEU A 273
REMARK 465 TYR A 274
REMARK 465 PHE A 275
REMARK 465 GLN A 276
REMARK 465 SER B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ASP B 5
REMARK 465 THR B 6
REMARK 465 PRO B 7
REMARK 465 GLN B 21
REMARK 465 ASN B 22
REMARK 465 PHE B 23
REMARK 465 ILE B 24
REMARK 465 ALA B 25
REMARK 465 LYS B 44
REMARK 465 ARG B 45
REMARK 465 SER B 46
REMARK 465 LEU B 65
REMARK 465 GLU B 66
REMARK 465 LEU B 67
REMARK 465 SER B 68
REMARK 465 ALA B 69
REMARK 465 HIS B 70
REMARK 465 HIS B 71
REMARK 465 HIS B 72
REMARK 465 HIS B 73
REMARK 465 HIS B 74
REMARK 465 HIS B 75
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 GLU A 12 CG CD OE1 OE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 ASN A 16 CG OD1 ND2
REMARK 470 SER A 19 OG
REMARK 470 THR A 20 OG1 CG2
REMARK 470 ASN A 22 CG OD1 ND2
REMARK 470 ASP A 23 CG OD1 OD2
REMARK 470 GLU A 58 CG CD OE1 OE2
REMARK 470 ILE A 60 CG1 CG2 CD1
REMARK 470 GLU A 61 CG CD OE1 OE2
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 SER A 63 OG
REMARK 470 THR A 64 OG1 CG2
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 GLN A 123 CG CD OE1 NE2
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 ASP A 151 CG OD1 OD2
REMARK 470 ASN A 152 CG OD1 ND2
REMARK 470 LYS A 154 CG CD CE NZ
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 ASN A 199 CG OD1 ND2
REMARK 470 TYR A 230 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 231 CG CD CE NZ
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 GLU A 233 CG CD OE1 OE2
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 TYR B 14 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 18 CG CD OE1 NE2
REMARK 470 ILE B 19 CG1 CG2 CD1
REMARK 470 ASP B 26 CG OD1 OD2
REMARK 470 TYR B 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B 28 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 THR B 30 OG1 CG2
REMARK 470 SER B 31 OG
REMARK 470 SER B 32 OG
REMARK 470 GLN B 33 CG CD OE1 NE2
REMARK 470 SER B 35 OG
REMARK 470 LYS B 36 CG CD CE NZ
REMARK 470 VAL B 39 CG1 CG2
REMARK 470 ILE B 40 CG1 CG2 CD1
REMARK 470 PHE B 41 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 42 CG CD1 CD2
REMARK 470 THR B 43 OG1 CG2
REMARK 470 VAL B 49 CG1 CG2
REMARK 470 ASP B 52 CG OD1 OD2
REMARK 470 SER B 54 OG
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 GLU B 56 CG CD OE1 OE2
REMARK 470 TRP B 57 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 57 CZ3 CH2
REMARK 470 VAL B 58 CG1 CG2
REMARK 470 GLN B 59 CG CD OE1 NE2
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 TYR B 61 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL B 62 CG1 CG2
REMARK 470 ASP B 64 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL B 58 N VAL B 62 2.12
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 THR A 124 -173.95 -67.96
REMARK 500 CYS A 150 79.08 -106.51
REMARK 500 ASN A 152 -26.04 78.23
REMARK 500 ASP A 229 -0.69 -58.74
REMARK 500 ASP A 254 70.05 -151.44
REMARK 500 ASN A 267 129.31 -35.93
REMARK 500 SER B 31 23.99 -55.42
REMARK 500 GLN B 33 -98.33 65.31
REMARK 500 CYS B 34 170.99 69.33
REMARK 500 ASP B 52 -164.36 -124.90
REMARK 500 SER B 54 -54.80 -156.86
REMARK 500 GLU B 55 -46.01 -154.83
REMARK 500 VAL B 58 -75.02 -48.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZK9 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZKC RELATED DB: PDB
DBREF 4ZKB A 1 270 UNP Q2F862 Q2F862_ORFV 17 286
DBREF 4ZKB B 1 69 UNP P10147 CCL3_HUMAN 24 92
SEQADV 4ZKB GLU A 271 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB ASN A 272 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB LEU A 273 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB TYR A 274 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB PHE A 275 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB GLN A 276 UNP Q2F862 EXPRESSION TAG
SEQADV 4ZKB HIS B 70 UNP P10147 EXPRESSION TAG
SEQADV 4ZKB HIS B 71 UNP P10147 EXPRESSION TAG
SEQADV 4ZKB HIS B 72 UNP P10147 EXPRESSION TAG
SEQADV 4ZKB HIS B 73 UNP P10147 EXPRESSION TAG
SEQADV 4ZKB HIS B 74 UNP P10147 EXPRESSION TAG
SEQADV 4ZKB HIS B 75 UNP P10147 EXPRESSION TAG
SEQRES 1 A 276 ALA PRO LEU LEU GLU SER GLN ARG SER ASN SER GLU GLU
SEQRES 2 A 276 LYS ALA ASN PHE CYS SER THR HIS ASN ASP GLU VAL TYR
SEQRES 3 A 276 ALA ARG PHE ARG LEU GLN MET ARG VAL GLY VAL ARG HIS
SEQRES 4 A 276 SER PRO LEU TYR THR PRO SER ASN MET CYS MET LEU ASP
SEQRES 5 A 276 ILE GLU ASP SER VAL GLU ASP ILE GLU GLU SER THR GLU
SEQRES 6 A 276 LYS GLU TYR ALA SER THR ALA THR GLY GLU ALA ALA GLY
SEQRES 7 A 276 VAL ASN VAL SER VAL ALA LEU VAL GLY GLU GLY VAL SER
SEQRES 8 A 276 ILE PRO PHE SER TYR ILE GLY LEU GLY PHE ASN PRO SER
SEQRES 9 A 276 LEU GLU ASP SER TYR LEU TYR VAL ASN VAL SER SER ARG
SEQRES 10 A 276 ALA PRO TRP VAL LYS GLN THR SER ASP LEU SER ALA ASN
SEQRES 11 A 276 GLY GLY TRP GLY ILE LYS GLN VAL LEU GLU LYS GLU LEU
SEQRES 12 A 276 LEU ALA ILE GLN ILE GLY CYS ASP ASN GLN LYS PHE PRO
SEQRES 13 A 276 GLU GLU PRO THR THR THR PRO PRO SER PRO VAL THR THR
SEQRES 14 A 276 THR LEU SER SER THR THR PRO ASP LEU ASN GLU GLU ASN
SEQRES 15 A 276 THR GLU ASN THR PRO THR THR THR GLY ALA SER VAL ASP
SEQRES 16 A 276 ARG LYS ARG ASN PRO ALA ASP ILE ASP PHE SER LEU LEU
SEQRES 17 A 276 VAL ASP PRO ARG CYS VAL THR SER VAL ASP LEU HIS VAL
SEQRES 18 A 276 GLU LEU ARG ASP ALA CYS ILE ASP TYR LYS GLN GLU SER
SEQRES 19 A 276 PRO LEU SER LEU LYS GLY LYS TYR GLY ASP GLY GLU LEU
SEQRES 20 A 276 VAL LYS LYS GLU ILE LYS ASP VAL GLY LYS ASN HIS ASN
SEQRES 21 A 276 MET CYS SER LEU ASN LEU ASN PRO GLY ASN GLU ASN LEU
SEQRES 22 A 276 TYR PHE GLN
SEQRES 1 B 75 SER LEU ALA ALA ASP THR PRO THR ALA CYS CYS PHE SER
SEQRES 2 B 75 TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA ASP
SEQRES 3 B 75 TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY VAL
SEQRES 4 B 75 ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA ASP
SEQRES 5 B 75 PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP LEU
SEQRES 6 B 75 GLU LEU SER ALA HIS HIS HIS HIS HIS HIS
MODRES 4ZKB NAG C 1 NAG -D
MODRES 4ZKB NAG C 2 NAG -D
MODRES 4ZKB NAG D 1 NAG -D
MODRES 4ZKB NAG D 2 NAG -D
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
HELIX 1 AA1 SER A 11 HIS A 21 1 11
HELIX 2 AA2 SER A 128 GLU A 142 1 15
HELIX 3 AA3 CYS A 227 LYS A 231 5 5
HELIX 4 AA4 ASP A 244 ILE A 252 1 9
HELIX 5 AA5 LYS A 253 VAL A 255 5 3
HELIX 6 AA6 GLU B 56 VAL B 62 1 7
SHEET 1 AA1 6 SER A 237 TYR A 242 0
SHEET 2 AA1 6 VAL A 214 ASP A 225 -1 N VAL A 221 O GLY A 240
SHEET 3 AA1 6 ALA A 27 VAL A 37 -1 N ARG A 34 O ASP A 218
SHEET 4 AA1 6 SER A 108 SER A 116 -1 O SER A 108 N VAL A 37
SHEET 5 AA1 6 PHE A 94 PHE A 101 -1 N SER A 95 O SER A 115
SHEET 6 AA1 6 ASN A 260 ASN A 265 -1 O CYS A 262 N LEU A 99
SHEET 1 AA2 6 CYS A 49 ASP A 59 0
SHEET 2 AA2 6 LYS A 66 ALA A 76 -1 O GLU A 67 N GLU A 58
SHEET 3 AA2 6 VAL A 79 GLU A 88 -1 O VAL A 81 N GLY A 74
SHEET 4 AA2 6 LEU A 143 GLY A 149 -1 O ALA A 145 N ALA A 84
SHEET 5 AA2 6 PHE A 205 VAL A 209 1 O SER A 206 N ILE A 146
SHEET 6 AA2 6 CYS B 10 SER B 13 -1 O PHE B 12 N LEU A 207
SHEET 1 AA3 2 ILE B 40 PHE B 41 0
SHEET 2 AA3 2 VAL B 49 CYS B 50 -1 O VAL B 49 N PHE B 41
SSBOND 1 CYS A 18 CYS A 227 1555 1555 2.04
SSBOND 2 CYS A 49 CYS A 262 1555 1555 2.04
SSBOND 3 CYS A 150 CYS A 213 1555 1555 2.02
SSBOND 4 CYS B 10 CYS B 34 1555 1555 2.03
SSBOND 5 CYS B 11 CYS B 50 1555 1555 2.01
LINK ND2 ASN A 80 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 113 C1 NAG D 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
CISPEP 1 ILE B 19 PRO B 20 0 7.77
CRYST1 78.000 78.000 186.020 90.00 90.00 90.00 P 43 21 2 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 0.012821 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005376 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
