Header list of 1gjj.pdb file
Complete list - 23 20 Bytes
HEADER MEMBRANE PROTEIN 25-JUN-01 1GJJ
TITLE N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAP2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL CONSTANT REGION (RESIDUES 1-168);
COMPND 5 SYNONYM: LAMIN-ASSOCIATED POLYPEPTIDE 2, THYMOPOIETIN, ISOFORM ALPHA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: NUCLEUS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INNER NUCLEAR MEMBRANE PROTEIN, LAMIN-ASSOCIATED POLYPEPTIDE, LEM
KEYWDS 2 DOMAIN, MULTIDIMENSIONAL NMR DIPOLAR COUPLINGS, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,M.CAI
REVDAT 4 23-FEB-22 1GJJ 1 REMARK
REVDAT 3 24-FEB-09 1GJJ 1 VERSN
REVDAT 2 28-DEC-04 1GJJ 1 JRNL
REVDAT 1 24-JUN-03 1GJJ 0
JRNL AUTH M.CAI,Y.HUANG,R.GHIRLANDO,K.L.WILSON,R.CRAIGIE,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE CONSTANT REGION OF NUCLEAR
JRNL TITL 2 ENVELOPE PROTEIN LAP2 REVEALS TWO LEM-DOMAIN STRUCTURES: ONE
JRNL TITL 3 BINDS BAF AND THE OTHER BINDS DNA.
JRNL REF EMBO J. V. 20 4399 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11500367
JRNL DOI 10.1093/EMBOJ/20.16.4399
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH VERSION (AVAILABLE TO ACADEMIC USERS BY
REMARK 3 ANONYMOUS FTP AT PORTAL.NIDDK.NIH.GOV IN PUB/CLORE/
REMARK 3 XPLOR_NIH OR AT HTTP://NMR.CIT.NIH.GOV)
REMARK 3 AUTHORS : CLORE, KUSZEWSKI AND SCHWIETERS. ADAPTED FROM
REMARK 3 BRUNGER (GENERAL XPLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED BY SIMULATED ANNEALING IN TORSION
REMARK 3 ANGLE SPACE (C. SCHWIETERS AND G.M. CLORE. IN PRESS). THE TARGET
REMARK 3 FUNCTION COMPRISES TERMS FOR THE NOE RESTRAINTS, TORSION ANGLE
REMARK 3 RESTRAINTS, CARBON CHEMICAL SHIFT RESTRAINTS (KUSZEWSKI ET AL. J.
REMARK 3 MAGN. RESON. SERIES B 106, 92-96 (1995)), THE DIPOLAR COUPLING
REMARK 3 RESTRAINTS (CLORE ET AL. J.MAGN.RESON. 131, 159-162 (1998);
REMARK 3 J.MAGN.RESON. 133, 216-221(1998)), THE RADIUS OF GYRATION
REMARK 3 (KUSZEWSKI ET AL. (1999), AND A QUARTIC VAN DER WAALS REPULSION
REMARK 3 TERM (NILGES ET AL. (1988) FEBS LETT. 229, 129-136).
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE
REMARK 3 RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED
REMARK 3 ANNEALING STRUCTURES AND THE MEAN COORDINATE
REMARK 3 POSITIONS. ONLY COORDINATES FOR RESIDUES 1-50 (LAP2-N)
REMARK 3 AND 111-153 (LAP2-C) ARE PROVIDED. THE LINKER CONNECTING
REMARK 3 THESE TWO DOMAINS IS COMPLETELY DISORDERED.
REMARK 3 LIKEWISE THE C-TERMINAL RESIDUES (154-168) ARE DISORDERED.
REMARK 3 SINCE THE TWO DOMAINS, LAP2-N AND LAP2-C, REORIENT
REMARK 3 ESSENTIALLY INDEPENDENTLY IN SOLUTION, THE COORDINATES
REMARK 3 OF THE TWO DOMAINS HAVE BEEN BEST-FITTED TO EACH OTHER
REMARK 3 SINCE THEY ARE STRUCTURALY VERY SIMILAR. THE LAP2-N
REMARK 3 DOMAIN BINDS DNA. THE LAP2-C DOMAIN BINDS THE
REMARK 3 BARRIER-TO-AUTOINTEGRATION FACTOR BAF.
REMARK 3
REMARK 3
REMARK 3 STRUCTURAL STATISTICS:
REMARK 3 ---------------------------------------------------------
REMARK 3 LAP2-N LAP2-C
REMARK 3 ---------------------------------------------------------
REMARK 3 DEVIATIONS FROM IDEALIZED GEOMETRY:
REMARK 3 BONDS 0.003 A 0.003 A
REMARK 3 ANGLES 0.48 DEG 0.54 DEG
REMARK 3 IMPROPERS 0.49 DEG 0.39 DEG
REMARK 3 DEVIATIONS FROM EXPT RESTRAINTS (LAP2-N/LAP2-C)
REMARK 3 NOES (395/401) 0.024 A 0.012 A
REMARK 3 TORSION ANGLES (151/121) 0.49 DEG 0.13 DEG
REMARK 3 13C CHEMICAL SHIFTS (105/91) 0.92 PPM 0.81 PPM
REMARK 3
REMARK 3 DIPOLAR COUPLING R-FACTORS (CLORE AND GARRETT (1999)
REMARK 3 J. AM. CHEM. SOC. 121, 9008-9012):
REMARK 3 1DNH (39/34) 6.4% 2.9%
REMARK 3 1DCH (36/29) 6.4% 1.9%
REMARK 3 1DNC' (24/19) 28.2% 26.2%
REMARK 3 2DHNC' (24/20) 30.1% 25.3%
REMARK 3 % RESIDUES IN MOST FAVORABLE
REMARK 3 REGION OF RAMACHADRAN MAP 84.1% 89.0%
REMARK 3
REMARK 3 NOTE: THE ALIGNMENT TENSOR FOR LAP2-N AND LAP2-C ARE
REMARK 3 DIFFERENT DUE TO THE FACT THAT THE TWO DOMAINS ARE
REMARK 3 ORIENTED INDEPENDENTLY BY THE PHAGE LIQUID
REMARK 3 CRYSTALLINE MEDIUM.
REMARK 4
REMARK 4 1GJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000001585.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DRX600; DRX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED SIMULATED IN TORSION
REMARK 210 ANGLE SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINED REGULARIZED MEAN
REMARK 210 STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE FOLLOWING EXPERIMENTS WERE CONDUCTED: (1) DOUBLE AND
REMARK 210 TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN; (2) QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING CONSTANTS; (3) 3D SEPARATED NOE
REMARK 210 EXPERIMENTS; (4) 2D AND 3D DOUBLE AND TRIPLE RESONANCE
REMARK 210 EXPERIMENTS FOR DIPOLAR COUPLING MEASUREMENTS IN LIQUID
REMARK 210 CRYSTALLINE MEDIUM OF PHAGE PF1.
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 RES C SSSEQI
REMARK 465 PRO A 51
REMARK 465 PRO A 52
REMARK 465 LEU A 53
REMARK 465 PRO A 54
REMARK 465 ALA A 55
REMARK 465 GLY A 56
REMARK 465 THR A 57
REMARK 465 ASN A 58
REMARK 465 SER A 59
REMARK 465 LYS A 60
REMARK 465 GLY A 61
REMARK 465 PRO A 62
REMARK 465 PRO A 63
REMARK 465 ASP A 64
REMARK 465 PHE A 65
REMARK 465 SER A 66
REMARK 465 SER A 67
REMARK 465 ASP A 68
REMARK 465 GLU A 69
REMARK 465 GLU A 70
REMARK 465 ARG A 71
REMARK 465 GLU A 72
REMARK 465 PRO A 73
REMARK 465 THR A 74
REMARK 465 PRO A 75
REMARK 465 VAL A 76
REMARK 465 LEU A 77
REMARK 465 GLY A 78
REMARK 465 SER A 79
REMARK 465 GLY A 80
REMARK 465 ALA A 81
REMARK 465 ALA A 82
REMARK 465 ALA A 83
REMARK 465 ALA A 84
REMARK 465 GLY A 85
REMARK 465 ARG A 86
REMARK 465 SER A 87
REMARK 465 ARG A 88
REMARK 465 ALA A 89
REMARK 465 ALA A 90
REMARK 465 VAL A 91
REMARK 465 GLY A 92
REMARK 465 ARG A 93
REMARK 465 LYS A 94
REMARK 465 ALA A 95
REMARK 465 THR A 96
REMARK 465 LYS A 97
REMARK 465 LYS A 98
REMARK 465 THR A 99
REMARK 465 ASP A 100
REMARK 465 LYS A 101
REMARK 465 PRO A 102
REMARK 465 ARG A 103
REMARK 465 GLN A 104
REMARK 465 GLU A 105
REMARK 465 ASP A 106
REMARK 465 LYS A 107
REMARK 465 ASP A 108
REMARK 465 ASP A 109
REMARK 465 LEU A 110
REMARK 465 THR A 154
REMARK 465 GLU A 155
REMARK 465 SER A 156
REMARK 465 ARG A 157
REMARK 465 SER A 158
REMARK 465 SER A 159
REMARK 465 THR A 160
REMARK 465 PRO A 161
REMARK 465 LEU A 162
REMARK 465 PRO A 163
REMARK 465 THR A 164
REMARK 465 ILE A 165
REMARK 465 SER A 166
REMARK 465 SER A 167
REMARK 465 SER A 168
DBREF 1GJJ A 1 168 UNP P42166 LAP2A_HUMAN 1 168
SEQRES 1 A 168 MET PRO GLU PHE LEU GLU ASP PRO SER VAL LEU THR LYS
SEQRES 2 A 168 ASP LYS LEU LYS SER GLU LEU VAL ALA ASN ASN VAL THR
SEQRES 3 A 168 LEU PRO ALA GLY GLU GLN ARG LYS ASP VAL TYR VAL GLN
SEQRES 4 A 168 LEU TYR LEU GLN HIS LEU THR ALA ARG ASN ARG PRO PRO
SEQRES 5 A 168 LEU PRO ALA GLY THR ASN SER LYS GLY PRO PRO ASP PHE
SEQRES 6 A 168 SER SER ASP GLU GLU ARG GLU PRO THR PRO VAL LEU GLY
SEQRES 7 A 168 SER GLY ALA ALA ALA ALA GLY ARG SER ARG ALA ALA VAL
SEQRES 8 A 168 GLY ARG LYS ALA THR LYS LYS THR ASP LYS PRO ARG GLN
SEQRES 9 A 168 GLU ASP LYS ASP ASP LEU ASP VAL THR GLU LEU THR ASN
SEQRES 10 A 168 GLU ASP LEU LEU ASP GLN LEU VAL LYS TYR GLY VAL ASN
SEQRES 11 A 168 PRO GLY PRO ILE VAL GLY THR THR ARG LYS LEU TYR GLU
SEQRES 12 A 168 LYS LYS LEU LEU LYS LEU ARG GLU GLN GLY THR GLU SER
SEQRES 13 A 168 ARG SER SER THR PRO LEU PRO THR ILE SER SER SER
HELIX 1 1 PRO A 8 VAL A 10 3 3
HELIX 2 2 LYS A 13 ALA A 22 1 10
HELIX 3 3 LYS A 34 LEU A 45 1 12
HELIX 4 4 VAL A 112 GLU A 114 3 3
HELIX 5 5 ASN A 117 LYS A 126 1 10
HELIX 6 6 ARG A 139 GLN A 152 1 14
CRYST1 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 - 23 20 Bytes