Header list of 2fv4.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN, PROTEIN BINDING 29-JAN-06 2FV4
TITLE NMR SOLUTION STRUCTURE OF THE YEAST KINETOCHORE SPC24/SPC25 GLOBULAR
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL 25.2 KDA PROTEIN IN AFG3-SEB2 INTERGENIC
COMPND 3 REGION;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SPC25P GLOBULAR DOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HYPOTHETICAL 24.6 KDA PROTEIN IN ILV2-ADE17 INTERGENIC
COMPND 9 REGION;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SPC24P GLOBULAR DOMAIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YER018C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3ATR;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: YMR117C, YM9718.16C;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: ROSETTA;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3ATR
KEYWDS ALPHA-BETA, COMPLEX, COILED-COIL, STRUCTURAL PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.SCHNELL,J.J.CHOU
REVDAT 4 09-MAR-22 2FV4 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2FV4 1 VERSN
REVDAT 2 20-JUN-06 2FV4 1 JRNL
REVDAT 1 13-JUN-06 2FV4 0
JRNL AUTH R.R.WEI,J.R.SCHNELL,N.A.LARSEN,P.K.SORGER,J.J.CHOU,
JRNL AUTH 2 S.C.HARRISON
JRNL TITL STRUCTURE OF A CENTRAL COMPONENT OF THE YEAST KINETOCHORE:
JRNL TITL 2 THE SPC24P/SPC25P GLOBULAR DOMAIN.
JRNL REF STRUCTURE V. 6 1003 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16765893
JRNL DOI 10.1016/J.STR.2006.04.007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.0, XPLOR-NIH 2.11
REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), CHARLES SCHWIETERS
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FV4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036348.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM SPC25G U-15N,13C,85%-2H,
REMARK 210 1.5 MM SPC24G NATURAL ABUNDANCE
REMARK 210 ISOTOPES, 95% H2O, 5% D2O; 1.5
REMARK 210 MM SPC25G NATURAL ABUNDANCE
REMARK 210 ISOTOPES, 1.5 MM SPC24G U-15N,
REMARK 210 13C,85%-2H, 95% H2O, 5% D2O; 1.5
REMARK 210 MM SPC25G U-15N,13C, 1.5 MM
REMARK 210 SPC24G NATURAL ABUNDANCE
REMARK 210 ISOTOPES, 95% H2O, 5% D2O; 1.5
REMARK 210 MM SPC25G NATURAL ABUNDANCE
REMARK 210 ISOTOPES, 1.5 MM SPC24G U-15N,
REMARK 210 13C, 95% H2O, 5% D2O; 1.5 MM
REMARK 210 SPC25G U-15N,13C, 85%-2H, 1.5 MM
REMARK 210 SPC24G NATURAL ABUNDANCE
REMARK 210 ISOTOPES, 50 MG/ML PF1 PHAGE, 95%
REMARK 210 H2O, 5% D2O; 1.5 MM SPC25G
REMARK 210 NATURAL ABUNDANCE ISOTOPES, 1.5
REMARK 210 MM SPC24G U-15N,13C, 50 MG/ML
REMARK 210 PF1 PHAGE, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY VERSIONS OF HNCA, HNCACB
REMARK 210 AND HNCO; 3D 15N-TOCSY-HSQC.; 3D
REMARK 210 15N-NOESY, 3D 13C-NOESY, AND 3D
REMARK 210 15N-EDITED 13C-FILTERED NOESY;
REMARK 210 2D SPIN ECHO DIFFERENCE
REMARK 210 EXPERIMENTS FOR MEASURING THREE-
REMARK 210 BOND J(C'C) AND J(NC); STANDARD
REMARK 210 HNCO-BASED 3D EXPERIMENTS FOR
REMARK 210 MEASURING ONE-BOND J(NH) AND J(C'
REMARK 210 CA).; 3D 15N-NOESY, 3D 13C-NOESY,
REMARK 210 AND 3D 15N-EDITED 13C-FILTERED
REMARK 210 NOESY; 2D SPIN ECHO DIFFERENCE
REMARK 210 EXPERIMENTS FOR MEASURING THREE-
REMARK 210 BOND J(C'C), J(NC) AND J(CC);
REMARK 210 STANDARD HNCO-BASED 3D
REMARK 210 EXPERIMENTS FOR MEASURING ONE-
REMARK 210 BOND J(NH).; STANDARD HNCO-BASED
REMARK 210 3D EXPERIMENTS FOR MEASURING
REMARK 210 RESIDUAL ONE-BOND D(NH) AND D(C'
REMARK 210 CA).; STANDARD HNCO-BASED 3D
REMARK 210 EXPERIMENTS FOR MEASURING
REMARK 210 RESIDUAL ONE-BOND D(NH).
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CARA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 124
REMARK 465 SER A 125
REMARK 465 HIS A 126
REMARK 465 MET A 127
REMARK 465 ALA A 128
REMARK 465 ALA A 129
REMARK 465 GLN A 130
REMARK 465 SER A 131
REMARK 465 GLY A 132
REMARK 465 MET B 137
REMARK 465 ALA B 138
REMARK 465 LYS B 139
REMARK 465 VAL B 140
REMARK 465 ILE B 141
REMARK 465 GLU B 142
REMARK 465 PRO B 143
REMARK 465 GLU B 144
REMARK 465 LEU B 145
REMARK 465 GLU B 146
REMARK 465 GLU B 147
REMARK 465 GLN B 148
REMARK 465 SER B 149
REMARK 465 ALA B 150
REMARK 465 VAL B 151
REMARK 465 THR B 152
REMARK 465 PRO B 153
REMARK 465 GLU B 154
REMARK 465 ALA B 155
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 SER A 154 -72.13 176.19
REMARK 500 1 ASP A 155 -10.56 -165.08
REMARK 500 1 ASP A 165 89.72 -152.33
REMARK 500 1 ASP A 166 -76.59 27.90
REMARK 500 1 ARG A 168 102.77 57.56
REMARK 500 1 HIS A 176 -102.51 -85.40
REMARK 500 1 VAL A 180 -5.25 -58.44
REMARK 500 1 ILE A 181 85.87 -53.85
REMARK 500 1 PRO A 186 -100.30 -83.94
REMARK 500 1 ALA A 187 30.32 161.90
REMARK 500 1 LEU A 188 -76.86 -156.78
REMARK 500 1 LEU A 206 -13.36 -47.50
REMARK 500 1 GLU B 157 -4.77 -53.39
REMARK 500 1 ASN B 176 26.61 -174.14
REMARK 500 1 ASP B 186 -168.27 44.54
REMARK 500 1 ASN B 188 -99.92 -135.62
REMARK 500 1 ASN B 197 -167.72 43.89
REMARK 500 2 SER A 154 -118.22 -60.78
REMARK 500 2 ASP A 155 -91.46 50.05
REMARK 500 2 HIS A 157 102.14 -54.80
REMARK 500 2 ASP A 165 -159.76 -102.99
REMARK 500 2 SER A 167 -5.45 70.38
REMARK 500 2 ARG A 168 112.46 64.84
REMARK 500 2 MET A 175 -83.78 54.07
REMARK 500 2 HIS A 179 -144.32 -151.45
REMARK 500 2 ILE A 181 102.02 -49.41
REMARK 500 2 PRO A 186 -90.07 -85.44
REMARK 500 2 ALA A 187 35.42 160.72
REMARK 500 2 LEU A 188 -134.60 -151.86
REMARK 500 2 GLU B 157 -6.18 -52.63
REMARK 500 2 LEU B 164 -70.88 -66.06
REMARK 500 2 ASN B 176 26.64 -174.57
REMARK 500 2 ASN B 185 -168.46 -55.10
REMARK 500 2 ASP B 186 85.09 -55.35
REMARK 500 2 ASN B 188 -46.52 -136.54
REMARK 500 2 ASN B 197 -175.72 49.19
REMARK 500 3 ASP A 165 -94.69 60.76
REMARK 500 3 ASP A 166 83.11 -32.13
REMARK 500 3 SER A 167 46.74 24.07
REMARK 500 3 ARG A 168 90.70 51.53
REMARK 500 3 MET A 175 12.42 51.58
REMARK 500 3 HIS A 176 9.15 -168.23
REMARK 500 3 PRO A 186 -99.66 -87.69
REMARK 500 3 ALA A 187 31.77 161.55
REMARK 500 3 LEU A 188 -156.67 -150.62
REMARK 500 3 SER A 192 -70.56 -70.76
REMARK 500 3 ASN B 176 26.69 -176.21
REMARK 500 3 ASN B 185 -113.18 -140.97
REMARK 500 3 ASN B 188 -68.82 74.98
REMARK 500 3 ASP B 195 -70.90 -146.80
REMARK 500
REMARK 500 THIS ENTRY HAS 335 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FTX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YEAST KINETOCHORE SPC24/SPC25 GLOBULAR
REMARK 900 DOMAIN
DBREF 2FV4 A 128 221 UNP P40014 YEK8_YEAST 128 221
DBREF 2FV4 B 138 213 UNP Q04477 YM06_YEAST 138 213
SEQADV 2FV4 GLY A 124 UNP P40014 CLONING ARTIFACT
SEQADV 2FV4 SER A 125 UNP P40014 CLONING ARTIFACT
SEQADV 2FV4 HIS A 126 UNP P40014 CLONING ARTIFACT
SEQADV 2FV4 MET A 127 UNP P40014 CLONING ARTIFACT
SEQADV 2FV4 MET B 137 UNP Q04477 CLONING ARTIFACT
SEQRES 1 A 98 GLY SER HIS MET ALA ALA GLN SER GLY ASN ASP ALA ALA
SEQRES 2 A 98 GLU VAL ALA LEU TYR GLU ARG LEU LEU GLN LEU ARG VAL
SEQRES 3 A 98 LEU PRO GLY ALA SER ASP VAL HIS ASP VAL ARG PHE VAL
SEQRES 4 A 98 PHE GLY ASP ASP SER ARG CYS TRP ILE GLU VAL ALA MET
SEQRES 5 A 98 HIS GLY ASP HIS VAL ILE GLY ASN SER HIS PRO ALA LEU
SEQRES 6 A 98 ASP PRO LYS SER ARG ALA THR LEU GLU HIS VAL LEU THR
SEQRES 7 A 98 VAL GLN GLY ASP LEU ALA ALA PHE LEU VAL VAL ALA ARG
SEQRES 8 A 98 ASP MET LEU LEU ALA SER LEU
SEQRES 1 B 77 MET ALA LYS VAL ILE GLU PRO GLU LEU GLU GLU GLN SER
SEQRES 2 B 77 ALA VAL THR PRO GLU ALA ASN GLU ASN ILE LEU LYS LEU
SEQRES 3 B 77 LYS LEU TYR ARG SER LEU GLY VAL ILE LEU ASP LEU GLU
SEQRES 4 B 77 ASN ASP GLN VAL LEU ILE ASN ARG LYS ASN ASP GLY ASN
SEQRES 5 B 77 ILE ASP ILE LEU PRO LEU ASP ASN ASN LEU SER ASP PHE
SEQRES 6 B 77 TYR LYS THR LYS TYR ILE TRP GLU ARG LEU GLY LYS
HELIX 1 1 ASN A 133 GLN A 146 1 14
HELIX 2 2 PRO A 190 GLY A 204 1 15
HELIX 3 3 ASP A 205 LEU A 221 1 17
HELIX 4 4 GLU B 157 LEU B 168 1 12
HELIX 5 5 SER B 199 GLY B 212 1 14
SHEET 1 A 4 LEU A 147 GLY A 152 0
SHEET 2 A 4 ASP A 158 PHE A 163 -1 O ASP A 158 N GLY A 152
SHEET 3 A 4 CYS A 169 GLU A 172 -1 O CYS A 169 N PHE A 163
SHEET 4 A 4 SER A 184 HIS A 185 -1 O HIS A 185 N TRP A 170
SHEET 1 B 3 VAL B 170 ASP B 173 0
SHEET 2 B 3 GLN B 178 ASN B 182 -1 O LEU B 180 N ILE B 171
SHEET 3 B 3 ILE B 189 PRO B 193 -1 O LEU B 192 N VAL B 179
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
Complete list - r 9 2 Bytes