Header list of 1vaz.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 20-FEB-04 1VAZ
TITLE SOLUTION STRUCTURES OF THE P47 SEP DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NSFL1 COFACTOR P47;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P47 SEP DOMAIN (RESIDUES 1-76);
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 TISSUE: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS BETA-BETA-BETA-ALPHA-ALPHA-BETA, NOVEL FOLD, LIPID BINDING PROTEIN
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 5 02-MAR-22 1VAZ 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1VAZ 1 VERSN
REVDAT 3 27-APR-04 1VAZ 1 JRNL
REVDAT 2 13-APR-04 1VAZ 1 AUTHOR
REVDAT 1 06-APR-04 1VAZ 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 2.1, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VAZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000006417.
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 : 13C, 15N-LABELLED P47(171-270)
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 : NMRVIEW 4.1.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
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 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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 H TRP A 17 O GLY A 20 1.40
REMARK 500 O LEU A 52 H HIS A 57 1.43
REMARK 500 O SER A 42 H GLY A 46 1.45
REMARK 500 O GLN A 38 H SER A 42 1.54
REMARK 500 O SER A 30 H ASP A 33 1.54
REMARK 500 O PHE A 39 HB ILE A 43 1.55
REMARK 500 O PRO A 34 H ALA A 37 1.60
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 ARG A 3 -155.84 -159.46
REMARK 500 1 GLN A 8 158.06 -42.48
REMARK 500 1 LEU A 23 108.36 -160.99
REMARK 500 1 ASP A 24 -175.09 58.60
REMARK 500 1 ASP A 33 -169.25 -63.00
REMARK 500 1 ALA A 50 -63.57 -101.08
REMARK 500 1 LEU A 55 -60.52 -100.77
REMARK 500 1 HIS A 57 45.07 73.29
REMARK 500 1 HIS A 68 61.48 -158.94
REMARK 500 1 PHE A 73 70.65 39.48
REMARK 500 2 SER A 6 -72.85 65.86
REMARK 500 2 LYS A 18 -26.12 -37.16
REMARK 500 2 THR A 19 28.91 -171.46
REMARK 500 2 LEU A 23 125.47 -171.82
REMARK 500 2 ASP A 24 173.22 58.57
REMARK 500 2 ASP A 33 -170.71 -64.58
REMARK 500 2 GLU A 47 89.30 -152.22
REMARK 500 2 PRO A 49 -156.74 -88.75
REMARK 500 2 HIS A 57 71.84 61.92
REMARK 500 2 HIS A 68 60.94 -156.50
REMARK 500 3 ARG A 3 -151.85 -76.97
REMARK 500 3 HIS A 5 42.61 -173.60
REMARK 500 3 GLN A 8 135.19 58.70
REMARK 500 3 LYS A 18 -33.93 -38.34
REMARK 500 3 THR A 19 27.09 -157.81
REMARK 500 3 ASP A 24 -139.18 67.64
REMARK 500 3 ASP A 27 -174.66 -65.82
REMARK 500 3 TYR A 31 -17.91 -49.09
REMARK 500 3 VAL A 48 89.92 -151.26
REMARK 500 3 PRO A 49 -159.75 -86.65
REMARK 500 3 HIS A 57 37.28 38.57
REMARK 500 3 HIS A 68 55.47 -147.35
REMARK 500 3 LYS A 75 101.97 48.34
REMARK 500 4 ASP A 9 157.48 57.87
REMARK 500 4 ASP A 24 -140.01 65.71
REMARK 500 4 ASP A 27 -177.97 -63.32
REMARK 500 4 ASP A 33 167.60 -41.73
REMARK 500 4 HIS A 57 66.41 70.50
REMARK 500 4 HIS A 68 27.29 178.07
REMARK 500 4 GLU A 71 70.38 -154.64
REMARK 500 4 VAL A 74 93.31 41.51
REMARK 500 4 LYS A 75 155.94 -47.77
REMARK 500 5 ARG A 2 121.67 59.54
REMARK 500 5 ARG A 3 -81.22 -108.28
REMARK 500 5 SER A 6 176.79 -48.84
REMARK 500 5 ASP A 9 -176.41 -65.05
REMARK 500 5 THR A 19 23.29 -141.52
REMARK 500 5 LEU A 23 113.31 -167.97
REMARK 500 5 ASP A 24 -174.03 61.49
REMARK 500 5 ASP A 33 156.88 -35.31
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 ARG A 2 0.32 SIDE CHAIN
REMARK 500 1 ARG A 3 0.13 SIDE CHAIN
REMARK 500 1 ARG A 4 0.32 SIDE CHAIN
REMARK 500 1 ARG A 29 0.28 SIDE CHAIN
REMARK 500 1 ARG A 44 0.31 SIDE CHAIN
REMARK 500 1 ARG A 45 0.19 SIDE CHAIN
REMARK 500 1 ARG A 53 0.24 SIDE CHAIN
REMARK 500 1 ARG A 54 0.25 SIDE CHAIN
REMARK 500 1 ARG A 69 0.19 SIDE CHAIN
REMARK 500 2 ARG A 2 0.20 SIDE CHAIN
REMARK 500 2 ARG A 3 0.10 SIDE CHAIN
REMARK 500 2 ARG A 4 0.22 SIDE CHAIN
REMARK 500 2 ARG A 29 0.30 SIDE CHAIN
REMARK 500 2 ARG A 44 0.31 SIDE CHAIN
REMARK 500 2 ARG A 45 0.26 SIDE CHAIN
REMARK 500 2 ARG A 53 0.23 SIDE CHAIN
REMARK 500 2 ARG A 54 0.25 SIDE CHAIN
REMARK 500 2 ARG A 69 0.23 SIDE CHAIN
REMARK 500 3 ARG A 2 0.31 SIDE CHAIN
REMARK 500 3 ARG A 3 0.32 SIDE CHAIN
REMARK 500 3 ARG A 29 0.22 SIDE CHAIN
REMARK 500 3 ARG A 44 0.28 SIDE CHAIN
REMARK 500 3 ARG A 45 0.21 SIDE CHAIN
REMARK 500 3 ARG A 53 0.31 SIDE CHAIN
REMARK 500 3 ARG A 54 0.27 SIDE CHAIN
REMARK 500 3 ARG A 69 0.26 SIDE CHAIN
REMARK 500 4 ARG A 2 0.32 SIDE CHAIN
REMARK 500 4 ARG A 3 0.29 SIDE CHAIN
REMARK 500 4 ARG A 4 0.30 SIDE CHAIN
REMARK 500 4 ARG A 29 0.23 SIDE CHAIN
REMARK 500 4 ARG A 44 0.22 SIDE CHAIN
REMARK 500 4 ARG A 45 0.24 SIDE CHAIN
REMARK 500 4 ARG A 53 0.23 SIDE CHAIN
REMARK 500 4 ARG A 54 0.29 SIDE CHAIN
REMARK 500 4 ARG A 69 0.25 SIDE CHAIN
REMARK 500 5 ARG A 2 0.27 SIDE CHAIN
REMARK 500 5 ARG A 3 0.31 SIDE CHAIN
REMARK 500 5 ARG A 29 0.32 SIDE CHAIN
REMARK 500 5 ARG A 44 0.23 SIDE CHAIN
REMARK 500 5 ARG A 45 0.28 SIDE CHAIN
REMARK 500 5 ARG A 54 0.08 SIDE CHAIN
REMARK 500 5 ARG A 69 0.30 SIDE CHAIN
REMARK 500 6 ARG A 3 0.31 SIDE CHAIN
REMARK 500 6 ARG A 4 0.32 SIDE CHAIN
REMARK 500 6 ARG A 29 0.28 SIDE CHAIN
REMARK 500 6 ARG A 44 0.14 SIDE CHAIN
REMARK 500 6 ARG A 45 0.28 SIDE CHAIN
REMARK 500 6 ARG A 53 0.32 SIDE CHAIN
REMARK 500 6 ARG A 54 0.27 SIDE CHAIN
REMARK 500 6 ARG A 69 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 85 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VAZ A 1 76 UNP O35987 NSF1C_RAT 171 246
SEQADV 1VAZ MET A -11 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ ARG A -10 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ GLY A -9 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ SER A -8 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -7 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -6 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -5 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -4 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -3 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ HIS A -2 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ GLY A -1 UNP O35987 EXPRESSION TAG
SEQADV 1VAZ SER A 0 UNP O35987 EXPRESSION TAG
SEQRES 1 A 88 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU
SEQRES 2 A 88 ARG ARG ARG HIS SER GLY GLN ASP VAL HIS VAL VAL LEU
SEQRES 3 A 88 LYS LEU TRP LYS THR GLY PHE SER LEU ASP ASN GLY ASP
SEQRES 4 A 88 LEU ARG SER TYR GLN ASP PRO SER ASN ALA GLN PHE LEU
SEQRES 5 A 88 GLU SER ILE ARG ARG GLY GLU VAL PRO ALA GLU LEU ARG
SEQRES 6 A 88 ARG LEU ALA HIS GLY GLY GLN VAL ASN LEU ASP MET GLU
SEQRES 7 A 88 ASP HIS ARG ASP GLU ASP PHE VAL LYS PRO
HELIX 1 1 SER A 35 GLY A 46 1 12
HELIX 2 2 ALA A 50 LEU A 55 1 6
SHEET 1 A 4 LEU A 28 SER A 30 0
SHEET 2 A 4 GLY A 20 SER A 22 -1 N PHE A 21 O ARG A 29
SHEET 3 A 4 HIS A 11 TRP A 17 -1 N TRP A 17 O GLY A 20
SHEET 4 A 4 ASN A 62 ASP A 67 1 O ASN A 62 N VAL A 12
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 2 2 Bytes