HEADER IMMUNE SYSTEM 06-JAN-09 3FPU
TITLE THE CRYSTALLOGRAPHIC STRUCTURE OF THE COMPLEX BETWEEN EVASIN-1 AND
TITLE 2 CCL3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EVASIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: C-C MOTIF CHEMOKINE 3;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: SMALL-INDUCIBLE CYTOKINE A3, MACROPHAGE INFLAMMATORY PROTEIN
COMPND 9 1-ALPHA, MIP-1-ALPHA, TONSILLAR LYMPHOCYTE LD78 ALPHA PROTEIN, G0/G1
COMPND 10 SWITCH REGULATORY PROTEIN 19-1, G0S19-1 PROTEIN, SIS-BETA, PAT 464.1,
COMPND 11 MIP-1-ALPHA(4-69), LD78-ALPHA(4-69);
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIPICEPHALUS SANGUINEUS;
SOURCE 3 ORGANISM_COMMON: BROWN DOG TICK;
SOURCE 4 ORGANISM_TAXID: 34632;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS PROTEIN:PROTEIN COMPLEX, CHEMOKINE, GLYCOPROTEIN, SECRETED,
KEYWDS 2 CHEMOTAXIS, CYTOKINE, INFLAMMATORY RESPONSE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.SHAW,J.M.DIAS
REVDAT 4 01-NOV-23 3FPU 1 REMARK
REVDAT 3 10-NOV-21 3FPU 1 REMARK SEQADV
REVDAT 2 16-OCT-13 3FPU 1 REMARK VERSN
REVDAT 1 12-JAN-10 3FPU 0
JRNL AUTH J.M.DIAS,C.LOSBERGER,M.DERUAZ,C.A.POWER,A.E.I.PROUDFOOT,
JRNL AUTH 2 J.P.SHAW
JRNL TITL STRUCTURAL BASIS OF CHEMOKINE SEQUESTRATION BY A TICK
JRNL TITL 2 CHEMOKINE BINDING PROTEIN: THE CRYSTAL STRUCTURE OF THE
JRNL TITL 3 COMPLEX BETWEEN EVASIN-1 AND CCL3
JRNL REF PLOS ONE V. 4 2009
JRNL REFN ESSN 1932-6203
JRNL PMID 20041127
JRNL DOI 10.1371/JOURNAL.PONE.0008514
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.FRAUENSCHUH,C.A.POWER,M.DERUAZ,B.R.FERREIRA,J.S.SILVA,
REMARK 1 AUTH 2 M.M.TEIXEIRA,J.M.DIAS,T.MARTIN,T.N.C.WELLS,A.E.I.PROUDFOOT
REMARK 1 TITL MOLECULAR CLONING AND CHARACTERIZATION OF A HIGHLY SELECTIVE
REMARK 1 TITL 2 CHEMOKINE-BINDING PROTEIN FROM THE TICK RHIPICEPHALUS
REMARK 1 TITL 3 SANGUINEUS.
REMARK 1 REF J.BIOL.CHEM. V. 282 27250 2007
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 17640866
REMARK 1 DOI 10.1074/JBC.M704706200
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.DERUAZ,A.FRAUENSCHUH,A.L.ALESSANDRI,J.M.DIAS,F.M.COELHO,
REMARK 1 AUTH 2 R.C.RUSSO,B.R.FERREIRA,G.J.GRAHAM,J.P.SHAW,T.N.C.WELLS,
REMARK 1 AUTH 3 M.M.TEIXEIRA,C.A.POWER,A.E.I.PROUDFOOT
REMARK 1 TITL TICKS PRODUCE HIGHLY SELECTIVE CHEMOKINE BINDING PROTEINS
REMARK 1 TITL 2 WITH ANTIINFLAMMATORY ACTIVITY
REMARK 1 REF J.EXP.MED. V. 205 2019 2008
REMARK 1 REFN ISSN 0022-1007
REMARK 1 PMID 18678732
REMARK 1 DOI 10.1084/JEM.20072689
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 18797
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1015
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1371
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1308
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.868
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1347 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1832 ; 1.639 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 164 ; 6.566 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 69 ;32.481 ;24.203
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 212 ;14.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.595 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 190 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1063 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 570 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 906 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 116 ; 0.153 ; 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): 94 ; 0.256 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.189 ; 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): 845 ; 1.318 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1341 ; 2.275 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 565 ; 2.981 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 491 ; 4.290 ; 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 : 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
REMARK 4
REMARK 4 3FPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050892.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19881
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
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 : 40.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.82800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3FPR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG 3350, 200MM AMMONIUM
REMARK 280 SULFATE, 100MM HEPES, PH 8.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 52.19200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.19200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.19200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.19200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.19200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 52.19200
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 52.19200
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 52.19200
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 52.19200
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 52.19200
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 52.19200
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 52.19200
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 52.19200
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 52.19200
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 52.19200
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 52.19200
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 52.19200
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 26.09600
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 78.28800
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 26.09600
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 26.09600
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 26.09600
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 78.28800
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 26.09600
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 78.28800
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 26.09600
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 78.28800
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 26.09600
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 78.28800
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 78.28800
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 26.09600
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 78.28800
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 26.09600
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 26.09600
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 26.09600
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 78.28800
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 26.09600
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 26.09600
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 78.28800
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 78.28800
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 78.28800
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 26.09600
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 78.28800
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 26.09600
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 78.28800
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 26.09600
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 26.09600
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 26.09600
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: 2690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NI NI A 101 LIES ON A SPECIAL POSITION.
REMARK 375 NI NI A 102 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 71 LIES ON A SPECIAL POSITION.
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 MET B 1
REMARK 465 LEU B 68
REMARK 465 SER B 69
REMARK 465 ALA B 70
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 ASP A 2 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 163 O HOH A 187 5555 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 65 CB CYS A 65 SG 0.135
REMARK 500 CYS A 84 CB CYS A 84 SG -0.125
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 ASP A 2 123.14 69.20
REMARK 500 ASN A 34 -130.00 53.24
REMARK 500 LYS A 78 -164.02 -104.08
REMARK 500 ASN A 94 -175.85 55.23
REMARK 500 LEU B 66 38.92 -78.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 102 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 98 NE2
REMARK 620 2 HIS A 100 NE2 89.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FPR RELATED DB: PDB
REMARK 900 UNCOMPLEXED NON-GLYCOSYLATED EVASIN-1
REMARK 900 RELATED ID: 3FPT RELATED DB: PDB
REMARK 900 UNCOMPLEXED GLYCOSYLATED EVASIN-1
DBREF 3FPU A 1 94 UNP P0C8E7 EVA1_RHISA 21 114
DBREF 3FPU B 2 70 UNP P10147 CCL3_HUMAN 24 92
SEQADV 3FPU HIS A 95 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU HIS A 96 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU HIS A 97 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU HIS A 98 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU HIS A 99 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU HIS A 100 UNP P0C8E7 EXPRESSION TAG
SEQADV 3FPU MET B 1 UNP P10147 EXPRESSION TAG
SEQADV 3FPU THR B 10 UNP P10147 ALA 32 ENGINEERED MUTATION
SEQRES 1 A 100 GLU ASP ASP GLU ASP TYR GLY ASP LEU GLY GLY CYS PRO
SEQRES 2 A 100 PHE LEU VAL ALA GLU ASN LYS THR GLY TYR PRO THR ILE
SEQRES 3 A 100 VAL ALA CYS LYS GLN ASP CYS ASN GLY THR THR GLU THR
SEQRES 4 A 100 ALA PRO ASN GLY THR ARG CYS PHE SER ILE GLY ASP GLU
SEQRES 5 A 100 GLY LEU ARG ARG MET THR ALA ASN LEU PRO TYR ASP CYS
SEQRES 6 A 100 PRO LEU GLY GLN CYS SER ASN GLY ASP CYS ILE PRO LYS
SEQRES 7 A 100 GLU THR TYR GLU VAL CYS TYR ARG ARG ASN TRP ARG ASP
SEQRES 8 A 100 LYS LYS ASN HIS HIS HIS HIS HIS HIS
SEQRES 1 B 70 MET SER LEU ALA ALA ASP THR PRO THR THR CYS CYS PHE
SEQRES 2 B 70 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 B 70 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 B 70 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 B 70 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 B 70 LEU GLU LEU SER ALA
HET NI A 101 1
HET NI A 102 1
HETNAM NI NICKEL (II) ION
FORMUL 3 NI 2(NI 2+)
FORMUL 5 HOH *160(H2 O)
HELIX 1 1 ILE A 49 MET A 57 1 9
HELIX 2 2 ASN A 88 LYS A 93 5 6
HELIX 3 3 LEU B 3 THR B 7 5 5
HELIX 4 4 PRO B 21 ASN B 23 5 3
HELIX 5 5 GLU B 56 LEU B 66 1 11
SHEET 1 A 3 PRO A 24 ILE A 26 0
SHEET 2 A 3 PHE A 14 GLU A 18 -1 N ALA A 17 O THR A 25
SHEET 3 A 3 THR B 10 CYS B 11 -1 O CYS B 11 N PHE A 14
SHEET 1 B 2 LYS A 30 CYS A 33 0
SHEET 2 B 2 THR A 36 THR A 39 -1 O THR A 36 N CYS A 33
SHEET 1 C 3 ARG A 45 PHE A 47 0
SHEET 2 C 3 TYR A 63 SER A 71 -1 O GLY A 68 N CYS A 46
SHEET 3 C 3 ASP A 74 CYS A 84 -1 O GLU A 82 N CYS A 65
SHEET 1 D 3 ILE B 25 GLU B 30 0
SHEET 2 D 3 VAL B 40 THR B 44 -1 O LEU B 43 N ALA B 26
SHEET 3 D 3 GLN B 49 ALA B 52 -1 O ALA B 52 N VAL B 40
SSBOND 1 CYS A 12 CYS A 33 1555 1555 2.04
SSBOND 2 CYS A 29 CYS A 70 1555 1555 2.02
SSBOND 3 CYS A 46 CYS A 75 1555 1555 2.00
SSBOND 4 CYS A 65 CYS A 84 1555 1555 1.99
SSBOND 5 CYS B 11 CYS B 35 1555 1555 2.00
SSBOND 6 CYS B 12 CYS B 51 1555 1555 2.08
LINK NE2 HIS A 97 NI NI A 101 1555 1555 2.22
LINK NE2 HIS A 98 NI NI A 102 1555 1555 2.18
LINK NE2 HIS A 100 NI NI A 102 1555 1555 2.12
CISPEP 1 ASP A 2 ASP A 3 0 -2.30
CISPEP 2 SER B 2 LEU B 3 0 -17.08
SITE 1 AC1 1 HIS A 97
SITE 1 AC2 2 HIS A 98 HIS A 100
CRYST1 104.384 104.384 104.384 90.00 90.00 90.00 P 43 3 2 24
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 0.009580 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009580 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
