Header list of 2gvp.pdb file
Complete list - 9 20 Bytes
HEADER TRANSPORT PROTEIN 03-MAY-06 2GVP
TITLE SOLUTION STRUCTURE OF HUMAN APO SCO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCO1 PROTEIN HOMOLOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 132-301);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SCO1, SCOD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETG-30A
KEYWDS THIOREDOXIN-LIKE FOLD, METALLOPROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,V.CALDERONE,S.CIOFI-BAFFONI,S.MANGANI,P.PAULMAA,
AUTHOR 2 M.MARTINELLI,S.WANG,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 09-MAR-22 2GVP 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GVP 1 VERSN
REVDAT 2 20-JUN-06 2GVP 1 JRNL
REVDAT 1 06-JUN-06 2GVP 0
JRNL AUTH L.BANCI,I.BERTINI,V.CALDERONE,S.CIOFI-BAFFONI,S.MANGANI,
JRNL AUTH 2 M.MARTINELLI,P.PALUMAA,S.WANG
JRNL TITL A HINT FOR THE FUNCTION OF HUMAN SCO1 FROM DIFFERENT
JRNL TITL 2 STRUCTURES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 8595 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16735468
JRNL DOI 10.1073/PNAS.0601375103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 8.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037605.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUMAN SCO1 U-15N,13C, 50MM
REMARK 210 PHOSPHATE BUFFER NA, 90% H2O, 10%
REMARK 210 D2O; 1MM HUMAN SCO1 U-15N, 50MM
REMARK 210 PHOSPHATE BUFFER NA, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; CBCA(CO)NH;
REMARK 210 HNCA; HN(CO)CA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, CARA 2.1, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ILE A 257 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 VAL A 258 C - N - CA ANGL. DEV. = 15.8 DEGREES
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 PHE A 130 98.78 43.69
REMARK 500 THR A 131 164.22 69.42
REMARK 500 PRO A 134 -114.25 -76.02
REMARK 500 LEU A 135 -173.66 63.04
REMARK 500 SER A 141 26.03 -140.99
REMARK 500 ASP A 171 -144.00 -152.63
REMARK 500 ILE A 187 -61.35 -128.16
REMARK 500 THR A 191 -42.25 76.36
REMARK 500 ARG A 207 -11.63 -169.13
REMARK 500 TYR A 244 -95.57 -171.83
REMARK 500 PRO A 249 41.20 20.39
REMARK 500 ASP A 251 -118.75 80.83
REMARK 500 GLU A 252 -94.49 -155.02
REMARK 500 ASP A 255 98.29 151.47
REMARK 500 TYR A 256 -38.35 178.09
REMARK 500 ILE A 257 125.48 104.25
REMARK 500 VAL A 258 -19.82 72.33
REMARK 500 ASP A 259 138.32 82.58
REMARK 500 GLU A 272 -151.36 -110.69
REMARK 500 LEU A 274 -43.46 -141.04
REMARK 500 GLN A 279 -58.77 72.59
REMARK 500 LYS A 283 -60.11 -24.66
REMARK 500 LYS A 299 -177.19 -67.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 133 PRO A 134 143.75
REMARK 500 LEU A 136 GLY A 137 65.24
REMARK 500 ASP A 270 GLY A 271 -144.26
REMARK 500 ASN A 280 LYS A 281 146.99
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 ARG A 149 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GQK RELATED DB: PDB
REMARK 900 THE FAMILY OF 30 STRUCTURES OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 NI(II) IONS.
REMARK 900 RELATED ID: 2GQL RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 NI(II) IONS.
REMARK 900 RELATED ID: 2GQM RELATED DB: PDB
REMARK 900 THE FAMILY OF 30 STRUCTURES OF THE SAME PROTEIN COMPLEXED WITH CU(I)
REMARK 900 IONS.
REMARK 900 RELATED ID: 2GT6 RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH CU(I)
REMARK 900 IONS.
REMARK 900 RELATED ID: 2GT5 RELATED DB: PDB
REMARK 900 THE FAMILY OF 30 STRUCTURES OF THE SAME PROTEIN, APO FORM.
REMARK 900 RELATED ID: CIRMMP13 RELATED DB: TARGETDB
DBREF 2GVP A 132 301 UNP O75880 SCO1_HUMAN 132 301
SEQADV 2GVP SER A 129 UNP O75880 CLONING ARTIFACT
SEQADV 2GVP PHE A 130 UNP O75880 CLONING ARTIFACT
SEQADV 2GVP THR A 131 UNP O75880 CLONING ARTIFACT
SEQRES 1 A 173 SER PHE THR GLY LYS PRO LEU LEU GLY GLY PRO PHE SER
SEQRES 2 A 173 LEU THR THR HIS THR GLY GLU ARG LYS THR ASP LYS ASP
SEQRES 3 A 173 TYR LEU GLY GLN TRP LEU LEU ILE TYR PHE GLY PHE THR
SEQRES 4 A 173 HIS CYS PRO ASP VAL CYS PRO GLU GLU LEU GLU LYS MET
SEQRES 5 A 173 ILE GLN VAL VAL ASP GLU ILE ASP SER ILE THR THR LEU
SEQRES 6 A 173 PRO ASP LEU THR PRO LEU PHE ILE SER ILE ASP PRO GLU
SEQRES 7 A 173 ARG ASP THR LYS GLU ALA ILE ALA ASN TYR VAL LYS GLU
SEQRES 8 A 173 PHE SER PRO LYS LEU VAL GLY LEU THR GLY THR ARG GLU
SEQRES 9 A 173 GLU VAL ASP GLN VAL ALA ARG ALA TYR ARG VAL TYR TYR
SEQRES 10 A 173 SER PRO GLY PRO LYS ASP GLU ASP GLU ASP TYR ILE VAL
SEQRES 11 A 173 ASP HIS THR ILE ILE MET TYR LEU ILE GLY PRO ASP GLY
SEQRES 12 A 173 GLU PHE LEU ASP TYR PHE GLY GLN ASN LYS ARG LYS GLY
SEQRES 13 A 173 GLU ILE ALA ALA SER ILE ALA THR HIS MET ARG PRO TYR
SEQRES 14 A 173 ARG LYS LYS SER
HELIX 1 1 PRO A 174 SER A 189 1 16
HELIX 2 2 THR A 209 SER A 221 1 13
HELIX 3 3 THR A 230 TYR A 241 1 12
HELIX 4 4 LYS A 283 ARG A 295 1 13
SHEET 1 A 6 THR A 143 THR A 144 0
SHEET 2 A 6 VAL A 225 THR A 228 -1 O THR A 228 N THR A 143
SHEET 3 A 6 LEU A 196 SER A 202 1 N PRO A 198 O VAL A 225
SHEET 4 A 6 TRP A 159 GLY A 165 1 N LEU A 161 O LEU A 199
SHEET 5 A 6 ILE A 263 ILE A 267 -1 O ILE A 267 N LEU A 160
SHEET 6 A 6 PHE A 273 GLY A 278 -1 O PHE A 277 N MET A 264
CISPEP 1 SER A 129 PHE A 130 0 8.88
CISPEP 2 PRO A 170 ASP A 171 0 -2.30
CISPEP 3 PRO A 247 GLY A 248 0 14.86
CISPEP 4 LYS A 250 ASP A 251 0 -3.46
CISPEP 5 ASP A 255 TYR A 256 0 -25.00
CISPEP 6 TYR A 256 ILE A 257 0 -14.09
CISPEP 7 ILE A 257 VAL A 258 0 -27.09
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
Complete list - 9 20 Bytes