Header list of 1g5v.pdb file
Complete list - 5 20 Bytes
HEADER TRANSLATION 02-NOV-00 1G5V
TITLE SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF THE HUMAN SMN PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURVIVAL MOTOR NEURON PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TUDOR DOMAIN;
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: SMN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET9D;
SOURCE 11 EXPRESSION_SYSTEM_GENE: EXPRESSED AS FUSION PROTEIN WITH N-TERMINAL
SOURCE 12 HIS6-GST AND TEV CLEAVAGE SITE
KEYWDS MRNA PROCESSING, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.SELENKO,R.SPRANGERS,G.STIER,D.BUEHLER,U.FISCHER,M.SATTLER
REVDAT 4 05-FEB-20 1G5V 1 REMARK
REVDAT 3 24-FEB-09 1G5V 1 VERSN
REVDAT 2 01-APR-03 1G5V 1 JRNL
REVDAT 1 02-MAY-01 1G5V 0
JRNL AUTH P.SELENKO,R.SPRANGERS,G.STIER,D.BUHLER,U.FISCHER,M.SATTLER
JRNL TITL SMN TUDOR DOMAIN STRUCTURE AND ITS INTERACTION WITH THE SM
JRNL TITL 2 PROTEINS.
JRNL REF NAT.STRUCT.BIOL. V. 8 27 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11135666
JRNL DOI 10.1038/83014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 0.3
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUENGER ET AL. ACTA
REMARK 3 CRYSTALLOGR.D BIOL. CRYSTALLOGR. 54, 905-21 (1998)
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1402 UNAMBIGUOUS NOE DISTANCE
REMARK 3 RESTRAINTS 50 HYDROGEN BOND RESTRAINTS 44 HN-N DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1G5V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012271.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE 30MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM 15N; 20MM PHOSPHATE
REMARK 210 BUFFER PH 6.3; 30MM NACL; 5MM
REMARK 210 DTT; 1.0 MM 15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER PH 6.3; 30MM
REMARK 210 NACL; 5MM DTT; 1.0 MM 15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER PH 6.3;
REMARK 210 30MM NACL; 5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; IPAP
REMARK 210 (DIPOLAR COUPLINGS)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, XEASY
REMARK 210 METHOD USED : MIXED TORSION AND CARTESIAN
REMARK 210 ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 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 LYS A 82
REMARK 465 LYS A 83
REMARK 465 ASN A 84
REMARK 465 THR A 85
REMARK 465 ALA A 86
REMARK 465 ALA A 87
REMARK 465 SER A 88
REMARK 465 LEU A 89
REMARK 465 CYS A 146
REMARK 465 GLU A 147
REMARK 465 VAL A 148
REMARK 465 ALA A 149
REMARK 465 ASN A 150
REMARK 465 ASN A 151
REMARK 465 ILE A 152
REMARK 465 GLU A 153
REMARK 465 GLN A 154
REMARK 465 ASN A 155
REMARK 465 ALA A 156
REMARK 465 GLN A 157
REMARK 465 GLU A 158
REMARK 465 ASN A 159
REMARK 465 GLU A 160
REMARK 465 ASN A 161
REMARK 465 GLU A 162
REMARK 465 SER A 163
REMARK 465 GLN A 164
REMARK 465 VAL A 165
REMARK 465 SER A 166
REMARK 465 THR A 167
REMARK 465 ASP A 168
REMARK 465 GLU A 169
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 GLN A 91 97.53 59.28
REMARK 500 1 THR A 128 106.23 -57.48
REMARK 500 1 PRO A 144 -179.61 -64.57
REMARK 500 2 GLN A 91 -130.60 -75.60
REMARK 500 2 CYS A 98 -164.74 -125.75
REMARK 500 2 PHE A 118 -9.02 -57.49
REMARK 500 2 LYS A 119 -72.52 -51.74
REMARK 500 2 PRO A 144 93.37 -66.99
REMARK 500 3 LYS A 119 -72.15 -68.80
REMARK 500 3 THR A 128 98.42 -61.98
REMARK 500 3 PRO A 144 -79.10 -56.72
REMARK 500 4 CYS A 98 -162.54 -129.09
REMARK 500 5 GLN A 91 123.94 65.08
REMARK 500 5 CYS A 98 -155.91 -136.43
REMARK 500 5 ASP A 105 -76.97 -117.23
REMARK 500 5 LYS A 119 -60.62 -99.93
REMARK 500 5 GLU A 121 56.31 38.87
REMARK 500 5 TYR A 130 -95.08 -115.28
REMARK 500 6 CYS A 98 -154.79 -136.26
REMARK 500 6 SER A 103 36.54 -97.36
REMARK 500 6 LYS A 119 -75.40 -51.97
REMARK 500 7 CYS A 98 -165.13 -126.09
REMARK 500 7 ASP A 105 -1.88 -144.88
REMARK 500 7 ILE A 113 104.97 -58.55
REMARK 500 7 LYS A 119 -73.98 -81.79
REMARK 500 7 TYR A 130 -94.12 -114.72
REMARK 500 8 GLN A 91 133.03 65.68
REMARK 500 8 CYS A 98 -161.43 -124.99
REMARK 500 8 ASP A 105 -70.74 -126.94
REMARK 500 8 ILE A 113 101.10 -59.01
REMARK 500 8 ARG A 120 -90.74 -84.51
REMARK 500 8 GLU A 121 55.60 176.86
REMARK 500 8 CYS A 123 135.92 -172.03
REMARK 500 9 CYS A 98 -158.76 -135.48
REMARK 500 9 GLU A 104 -60.94 -90.51
REMARK 500 9 THR A 128 -88.38 -53.47
REMARK 500 10 GLN A 91 -151.75 50.63
REMARK 500 10 CYS A 98 -169.04 -121.90
REMARK 500 10 SER A 103 35.63 -84.55
REMARK 500 10 ILE A 113 109.72 -59.20
REMARK 500 10 LYS A 119 -71.75 -69.94
REMARK 500 10 GLU A 121 74.03 52.48
REMARK 500 10 THR A 128 95.70 -62.17
REMARK 500 10 PRO A 144 -162.59 -73.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4899 RELATED DB: BMRB
DBREF 1G5V A 82 169 UNP Q16637 SMN_HUMAN 82 169
SEQRES 1 A 88 LYS LYS ASN THR ALA ALA SER LEU GLN GLN TRP LYS VAL
SEQRES 2 A 88 GLY ASP LYS CYS SER ALA ILE TRP SER GLU ASP GLY CYS
SEQRES 3 A 88 ILE TYR PRO ALA THR ILE ALA SER ILE ASP PHE LYS ARG
SEQRES 4 A 88 GLU THR CYS VAL VAL VAL TYR THR GLY TYR GLY ASN ARG
SEQRES 5 A 88 GLU GLU GLN ASN LEU SER ASP LEU LEU SER PRO ILE CYS
SEQRES 6 A 88 GLU VAL ALA ASN ASN ILE GLU GLN ASN ALA GLN GLU ASN
SEQRES 7 A 88 GLU ASN GLU SER GLN VAL SER THR ASP GLU
HELIX 1 1 LEU A 138 ASP A 140 5 3
SHEET 1 B1 1 GLY A 95 ILE A 101 0
SHEET 1 B2 1 ILE A 108 PHE A 118 0
SHEET 1 B3 1 THR A 122 TYR A 127 0
SHEET 1 B4 1 ASN A 132 ASP A 140 0
SHEET 1 B5 1 LEU A 142 SER A 143 0
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 - 5 20 Bytes