Header list of 1v92.pdb file
Complete list - 2 20 Bytes
HEADER RECOMBINATION 19-JAN-04 1V92
TITLE SOLUTION STRUCTURE OF THE UBA DOMAIN FROM P47, A MAJOR COFACTOR OF THE
TITLE 2 AAA ATPASE P97
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NSFL1 COFACTOR P47;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P47 UBA DOMAIN;
COMPND 5 SYNONYM: P97 COFACTOR P47, XY BODY-ASSOCIATED PROTEIN XY40;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPRO-EX HTB
KEYWDS 3-HELIX BUNDLE, RECOMBINATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR X.YUAN,P.SIMPSON,C.MCKEOWN,H.KONDO,K.UCHIYAMA,R.WALLIS,I.DREVENY,
AUTHOR 2 C.KEETCH,X.ZHANG,C.ROBINSON,P.FREEMONT,S.MATTHEWS
REVDAT 4 02-MAR-22 1V92 1 REMARK
REVDAT 3 24-FEB-09 1V92 1 VERSN
REVDAT 2 01-JUN-04 1V92 1 JRNL
REVDAT 1 06-APR-04 1V92 0
JRNL AUTH X.YUAN,P.SIMPSON,C.MCKEOWN,H.KONDO,K.UCHIYAMA,R.WALLIS,
JRNL AUTH 2 I.DREVENY,C.KEETCH,X.ZHANG,C.ROBINSON,P.FREEMONT,S.MATTHEWS
JRNL TITL STRUCTURE, DYNAMICS AND INTERACTIONS OF P47, A MAJOR ADAPTOR
JRNL TITL 2 OF THE AAA ATPASE, P97
JRNL REF EMBO J. V. 23 1463 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 15029246
JRNL DOI 10.1038/SJ.EMBOJ.7600152
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.0, ARIA 1.0
REMARK 3 AUTHORS : F.DELAGLIO (NMRPIPE), M.NILGES, J.P.LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V92 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000006359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : 20MM NAAC
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 15N, 13C DOUBLE LABELLED P47
REMARK 210 RESIDUES 1-174; 15N LABELLED P47
REMARK 210 RESIDUES 1-174
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.0, NMRVIEW 4.0.3, ARIA
REMARK 210 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 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 : 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: 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: 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 O ALA A 23 H LEU A 27 1.22
REMARK 500 O GLU A 28 H GLY A 31 1.47
REMARK 500 O GLU A 4 H ALA A 8 1.55
REMARK 500 O ALA A 23 N LEU A 27 2.11
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 TRP A 32 31.40 35.36
REMARK 500 2 TRP A 32 30.19 35.06
REMARK 500 3 ALA A 18 -173.52 -54.96
REMARK 500 3 TRP A 32 30.61 35.17
REMARK 500 4 ALA A 18 -158.92 -63.56
REMARK 500 4 TRP A 32 31.01 35.42
REMARK 500 4 PHE A 41 -39.51 -37.08
REMARK 500 5 TRP A 32 31.19 35.70
REMARK 500 5 ASP A 44 2.97 -61.31
REMARK 500 6 TRP A 32 27.63 37.76
REMARK 500 6 GLN A 35 -36.97 -35.07
REMARK 500 7 ALA A 18 -175.57 -57.33
REMARK 500 7 TRP A 32 31.31 35.57
REMARK 500 7 LEU A 34 -62.44 -92.56
REMARK 500 7 ILE A 36 -71.02 -81.51
REMARK 500 7 SER A 40 -70.68 -71.20
REMARK 500 8 TRP A 32 32.28 36.18
REMARK 500 8 LEU A 34 -62.81 -92.92
REMARK 500 8 ILE A 36 -71.12 -78.26
REMARK 500 9 ALA A 18 -165.27 -73.35
REMARK 500 9 TRP A 32 30.90 34.68
REMARK 500 9 ILE A 36 -70.22 -74.24
REMARK 500 9 GLU A 43 19.95 55.60
REMARK 500 9 ASP A 44 35.07 -81.22
REMARK 500 10 ALA A 18 -165.55 -102.37
REMARK 500 10 TRP A 32 27.44 38.37
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 ARG A 5 0.23 SIDE CHAIN
REMARK 500 1 ARG A 10 0.29 SIDE CHAIN
REMARK 500 1 ARG A 22 0.31 SIDE CHAIN
REMARK 500 1 ARG A 24 0.21 SIDE CHAIN
REMARK 500 2 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 24 0.31 SIDE CHAIN
REMARK 500 3 ARG A 5 0.10 SIDE CHAIN
REMARK 500 3 ARG A 10 0.30 SIDE CHAIN
REMARK 500 3 ARG A 22 0.32 SIDE CHAIN
REMARK 500 3 ARG A 24 0.31 SIDE CHAIN
REMARK 500 4 ARG A 5 0.28 SIDE CHAIN
REMARK 500 4 ARG A 10 0.30 SIDE CHAIN
REMARK 500 4 ARG A 22 0.30 SIDE CHAIN
REMARK 500 4 ARG A 24 0.19 SIDE CHAIN
REMARK 500 5 ARG A 5 0.15 SIDE CHAIN
REMARK 500 5 ARG A 10 0.31 SIDE CHAIN
REMARK 500 5 ARG A 22 0.20 SIDE CHAIN
REMARK 500 5 ARG A 24 0.11 SIDE CHAIN
REMARK 500 6 ARG A 5 0.20 SIDE CHAIN
REMARK 500 6 ARG A 22 0.32 SIDE CHAIN
REMARK 500 6 ARG A 24 0.26 SIDE CHAIN
REMARK 500 7 ARG A 5 0.26 SIDE CHAIN
REMARK 500 7 ARG A 22 0.31 SIDE CHAIN
REMARK 500 7 ARG A 24 0.21 SIDE CHAIN
REMARK 500 8 ARG A 5 0.22 SIDE CHAIN
REMARK 500 8 ARG A 10 0.18 SIDE CHAIN
REMARK 500 8 ARG A 22 0.31 SIDE CHAIN
REMARK 500 8 ARG A 24 0.09 SIDE CHAIN
REMARK 500 9 ARG A 5 0.21 SIDE CHAIN
REMARK 500 9 ARG A 10 0.29 SIDE CHAIN
REMARK 500 9 ARG A 22 0.19 SIDE CHAIN
REMARK 500 10 ARG A 5 0.17 SIDE CHAIN
REMARK 500 10 ARG A 10 0.15 SIDE CHAIN
REMARK 500 10 ARG A 22 0.31 SIDE CHAIN
REMARK 500 10 ARG A 24 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V92 A 1 46 UNP O35987 NSF1C_RAT 1 46
SEQRES 1 A 46 MET ALA GLU GLU ARG GLN ASP ALA LEU ARG GLU PHE VAL
SEQRES 2 A 46 ALA VAL THR GLY ALA GLU GLU ASP ARG ALA ARG PHE PHE
SEQRES 3 A 46 LEU GLU SER ALA GLY TRP ASP LEU GLN ILE ALA LEU ALA
SEQRES 4 A 46 SER PHE TYR GLU ASP GLY GLY
HELIX 1 1 GLU A 3 THR A 16 1 14
HELIX 2 2 GLU A 19 ALA A 30 1 12
HELIX 3 3 LEU A 34 ASP A 44 1 11
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 - 2 20 Bytes