Header list of 2fin.pdb file
Complete list - t 20 2 Bytes
HEADER VIRUS/VIRAL PROTEIN/CYTOKINE 29-DEC-05 2FIN
TITLE SOLUTION STRUCTURE OF THE COMPLEX BETWEEN POXVIRUS-ENCODED CC
TITLE 2 CHEMOKINE INHIBITOR VCCI AND HUMAN MIP-1BETA, ENSEMBLE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RABBITPOX ENCODED CC CHEMOKINE INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VCCI, 35 KDA, P35;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SMALL INDUCIBLE CYTOKINE A4;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: MACROPHAGE INFLAMMATORY PROTEIN 1-BETA, MIP-1-BETA;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RABBITPOX VIRUS;
SOURCE 3 ORGANISM_TAXID: 32606;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SMD1168;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PPIC9K;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CCL4, LAG1, MIP1B, SCYA4;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-32 XA/LIC
KEYWDS PROTEIN-PROTEIN COMPLEX, CHEMOKINE, POX VIRUS, VIRAL CC CHEMOKINE
KEYWDS 2 INHIBITOR, VIRUS-VIRAL PROTEIN-CYTOKINE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR L.ZHANG
REVDAT 4 20-OCT-21 2FIN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2FIN 1 VERSN
REVDAT 2 03-OCT-06 2FIN 1 JRNL
REVDAT 1 22-AUG-06 2FIN 0
JRNL AUTH L.ZHANG,M.DERIDER,M.A.MCCORNACK,S.C.JAO,N.ISERN,T.NESS,
JRNL AUTH 2 R.MOYER,P.J.LIWANG
JRNL TITL SOLUTION STRUCTURE OF THE COMPLEX BETWEEN POXVIRUS-ENCODED
JRNL TITL 2 CC CHEMOKINE INHIBITOR VCCI AND HUMAN MIP-1BETA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 13985 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16963564
JRNL DOI 10.1073/PNAS.0602142103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYNAMO 3.1
REMARK 3 AUTHORS : FRANK DELAGLIO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FIN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035922.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5-2.0 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE LINUX9, DYNAMO 3.1
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 PRO A 2 -171.88 -51.77
REMARK 500 1 ALA A 3 175.18 53.49
REMARK 500 1 SER A 4 -8.87 -165.61
REMARK 500 1 GLN A 7 -143.11 -60.95
REMARK 500 1 SER A 8 -14.70 -158.11
REMARK 500 1 GLU A 19 -63.11 -27.60
REMARK 500 1 GLN A 37 -23.44 -172.09
REMARK 500 1 PRO A 39 159.17 -39.62
REMARK 500 1 ASN A 41 101.15 -174.08
REMARK 500 1 ILE A 44 176.09 -57.83
REMARK 500 1 SER A 47 165.52 178.71
REMARK 500 1 SER A 54 -46.09 74.15
REMARK 500 1 SER A 56 -105.76 39.71
REMARK 500 1 ASP A 57 -37.82 -160.31
REMARK 500 1 PRO A 58 -94.95 -80.92
REMARK 500 1 ASP A 59 51.67 -176.13
REMARK 500 1 GLU A 61 61.64 62.72
REMARK 500 1 VAL A 62 -25.42 72.54
REMARK 500 1 GLU A 63 63.04 63.35
REMARK 500 1 ASP A 66 90.89 -167.81
REMARK 500 1 SER A 68 -47.33 -173.56
REMARK 500 1 THR A 69 -39.96 -172.75
REMARK 500 1 VAL A 71 33.93 -158.28
REMARK 500 1 ASP A 73 -98.60 -34.35
REMARK 500 1 VAL A 74 -80.22 57.33
REMARK 500 1 PRO A 77 -147.51 -55.84
REMARK 500 1 SER A 82 66.18 -105.03
REMARK 500 1 PRO A 98 148.03 -39.10
REMARK 500 1 PRO A 121 162.25 -40.32
REMARK 500 1 GLN A 123 -46.13 -140.11
REMARK 500 1 SER A 127 61.89 -163.21
REMARK 500 1 ASP A 147 77.07 -158.29
REMARK 500 1 ARG A 149 -149.11 -134.70
REMARK 500 1 GLU A 152 10.79 -147.50
REMARK 500 1 THR A 161 -2.33 -57.95
REMARK 500 1 PRO A 163 160.46 -40.49
REMARK 500 1 ASN A 168 -0.65 58.75
REMARK 500 1 LYS A 172 -166.90 -58.26
REMARK 500 1 LYS A 188 -16.98 -44.93
REMARK 500 1 CYS A 189 24.55 -143.71
REMARK 500 1 VAL A 190 104.27 -163.98
REMARK 500 1 ARG A 198 113.87 -171.79
REMARK 500 1 LYS A 204 117.56 -161.69
REMARK 500 1 GLU A 205 156.40 -43.98
REMARK 500 1 SER A 206 17.80 -141.11
REMARK 500 1 SER A 207 -74.22 56.28
REMARK 500 1 ASP A 228 95.52 -67.09
REMARK 500 1 SER B 5 -91.81 -54.75
REMARK 500 1 PRO B 8 -99.34 -34.33
REMARK 500 1 THR B 9 165.20 163.50
REMARK 500
REMARK 500 THIS ENTRY HAS 897 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 80 0.07 SIDE CHAIN
REMARK 500 1 ARG A 89 0.10 SIDE CHAIN
REMARK 500 1 ARG A 115 0.32 SIDE CHAIN
REMARK 500 1 ARG A 149 0.29 SIDE CHAIN
REMARK 500 1 ARG B 18 0.31 SIDE CHAIN
REMARK 500 1 ARG B 22 0.19 SIDE CHAIN
REMARK 500 2 ARG A 89 0.09 SIDE CHAIN
REMARK 500 2 ARG A 149 0.31 SIDE CHAIN
REMARK 500 2 ARG A 198 0.10 SIDE CHAIN
REMARK 500 2 ARG B 18 0.24 SIDE CHAIN
REMARK 500 2 ARG B 22 0.20 SIDE CHAIN
REMARK 500 3 ARG A 89 0.08 SIDE CHAIN
REMARK 500 3 ARG A 115 0.15 SIDE CHAIN
REMARK 500 3 ARG A 149 0.14 SIDE CHAIN
REMARK 500 3 ARG A 198 0.29 SIDE CHAIN
REMARK 500 3 ARG B 18 0.32 SIDE CHAIN
REMARK 500 3 ARG B 22 0.25 SIDE CHAIN
REMARK 500 4 ARG A 89 0.20 SIDE CHAIN
REMARK 500 4 ARG A 115 0.25 SIDE CHAIN
REMARK 500 4 ARG A 149 0.26 SIDE CHAIN
REMARK 500 4 ARG A 198 0.31 SIDE CHAIN
REMARK 500 4 ARG B 22 0.25 SIDE CHAIN
REMARK 500 5 ARG A 89 0.16 SIDE CHAIN
REMARK 500 5 ARG A 115 0.31 SIDE CHAIN
REMARK 500 5 ARG A 149 0.21 SIDE CHAIN
REMARK 500 5 ARG A 198 0.23 SIDE CHAIN
REMARK 500 5 ARG B 18 0.30 SIDE CHAIN
REMARK 500 6 ARG A 89 0.22 SIDE CHAIN
REMARK 500 6 ARG A 115 0.32 SIDE CHAIN
REMARK 500 6 ARG A 149 0.29 SIDE CHAIN
REMARK 500 6 ARG B 18 0.32 SIDE CHAIN
REMARK 500 6 ARG B 22 0.27 SIDE CHAIN
REMARK 500 7 ARG A 89 0.31 SIDE CHAIN
REMARK 500 7 ARG A 115 0.14 SIDE CHAIN
REMARK 500 7 ARG A 149 0.20 SIDE CHAIN
REMARK 500 7 ARG A 198 0.29 SIDE CHAIN
REMARK 500 7 ARG B 18 0.28 SIDE CHAIN
REMARK 500 7 ARG B 22 0.25 SIDE CHAIN
REMARK 500 8 TYR A 80 0.09 SIDE CHAIN
REMARK 500 8 ARG A 89 0.14 SIDE CHAIN
REMARK 500 8 ARG A 149 0.27 SIDE CHAIN
REMARK 500 8 ARG A 198 0.22 SIDE CHAIN
REMARK 500 8 ARG B 18 0.27 SIDE CHAIN
REMARK 500 9 ARG A 89 0.18 SIDE CHAIN
REMARK 500 9 ARG A 149 0.32 SIDE CHAIN
REMARK 500 9 ARG A 198 0.25 SIDE CHAIN
REMARK 500 9 ARG B 18 0.11 SIDE CHAIN
REMARK 500 9 ARG B 22 0.22 SIDE CHAIN
REMARK 500 10 TYR A 80 0.07 SIDE CHAIN
REMARK 500 10 ARG A 89 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 84 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FFK RELATED DB: PDB
DBREF 2FIN A 1 242 GB 44971547 AAS49897 17 258
DBREF 2FIN B 1 69 UNP P13236 CCL4_HUMAN 24 92
SEQADV 2FIN ALA B 45 UNP P13236 LYS 68 ENGINEERED MUTATION
SEQADV 2FIN ALA B 46 UNP P13236 ARG 69 ENGINEERED MUTATION
SEQADV 2FIN ALA B 48 UNP P13236 LYS 71 ENGINEERED MUTATION
SEQRES 1 A 242 MET PRO ALA SER LEU GLN GLN SER SER SER SER SER SER
SEQRES 2 A 242 SER CYS THR GLU GLU GLU ASN LYS HIS HIS MET GLY ILE
SEQRES 3 A 242 ASP VAL ILE ILE LYS VAL THR LYS GLN ASP GLN THR PRO
SEQRES 4 A 242 THR ASN ASP LYS ILE CYS GLN SER VAL THR GLU ILE THR
SEQRES 5 A 242 GLU SER GLU SER ASP PRO ASP PRO GLU VAL GLU SER GLU
SEQRES 6 A 242 ASP ASP SER THR SER VAL GLU ASP VAL ASP PRO PRO THR
SEQRES 7 A 242 THR TYR TYR SER ILE ILE GLY GLY GLY LEU ARG MET ASN
SEQRES 8 A 242 PHE GLY PHE THR LYS CYS PRO GLN ILE LYS SER ILE SER
SEQRES 9 A 242 GLU SER ALA ASP GLY ASN THR VAL ASN ALA ARG LEU SER
SEQRES 10 A 242 SER VAL SER PRO GLY GLN GLY LYS ASP SER PRO ALA ILE
SEQRES 11 A 242 THR HIS GLU GLU ALA LEU ALA MET ILE LYS ASP CYS GLU
SEQRES 12 A 242 VAL SER ILE ASP ILE ARG CYS SER GLU GLU GLU LYS ASP
SEQRES 13 A 242 SER ASP ILE LYS THR HIS PRO VAL LEU GLY SER ASN ILE
SEQRES 14 A 242 SER HIS LYS LYS VAL SER TYR GLU ASP ILE ILE GLY SER
SEQRES 15 A 242 THR ILE VAL ASP THR LYS CYS VAL LYS ASN LEU GLU PHE
SEQRES 16 A 242 SER VAL ARG ILE GLY ASP MET CYS LYS GLU SER SER GLU
SEQRES 17 A 242 LEU GLU VAL LYS ASP GLY PHE LYS TYR VAL ASP GLY SER
SEQRES 18 A 242 ALA SER LYS GLY ALA THR ASP ASP THR SER LEU ILE ASP
SEQRES 19 A 242 SER THR LYS LEU LYS ALA CYS VAL
SEQRES 1 B 69 ALA PRO MET GLY SER ASP PRO PRO THR ALA CYS CYS PHE
SEQRES 2 B 69 SER TYR THR ALA ARG LYS LEU PRO ARG ASN PHE VAL VAL
SEQRES 3 B 69 ASP TYR TYR GLU THR SER SER LEU CYS SER GLN PRO ALA
SEQRES 4 B 69 VAL VAL PHE GLN THR ALA ALA SER ALA GLN VAL CYS ALA
SEQRES 5 B 69 ASP PRO SER GLU SER TRP VAL GLN GLU TYR VAL TYR ASP
SEQRES 6 B 69 LEU GLU LEU ASN
HELIX 1 1 HIS A 132 ASP A 141 1 10
HELIX 2 2 SER B 57 LEU B 68 1 12
SHEET 1 1 1 MET A 24 THR A 33 0
SHEET 1 2 1 SER A 47 THR A 52 0
SHEET 1 3 1 THR A 79 GLY A 85 0
SHEET 1 4 1 LEU A 88 THR A 95 0
SHEET 1 5 1 SER A 102 ASP A 108 0
SHEET 1 6 1 THR A 111 SER A 117 0
SHEET 1 7 1 GLU A 143 ARG A 149 0
SHEET 1 8 1 GLY A 181 ASP A 186 0
SHEET 1 9 1 ASN A 192 ASP A 201 0
SHEET 1 10 1 VAL A 211 VAL A 218 0
SHEET 1 11 1 SER A 221 SER A 223 0
SHEET 1 12 1 ASP B 27 GLU B 30 0
SHEET 1 13 1 VAL B 40 GLN B 43 0
SHEET 1 14 1 GLN B 49 ALA B 52 0
SSBOND 1 CYS A 15 CYS A 203 1555 1555 2.02
SSBOND 2 CYS A 45 CYS A 241 1555 1555 2.02
SSBOND 3 CYS A 97 CYS A 142 1555 1555 2.02
SSBOND 4 CYS A 150 CYS A 189 1555 1555 2.02
SSBOND 5 CYS B 11 CYS B 35 1555 1555 2.03
SSBOND 6 CYS B 12 CYS B 51 1555 1555 2.02
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
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