Header list of 1s7a.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN, TRANSLATION 29-JAN-04 1S7A
TITLE NMR STRUCTURE OF THE LA MOTIF OF HUMAN LA PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LUPUS LA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LA MOTIF;
COMPND 5 SYNONYM: SJOGREN SYNDROME TYPE B ANTIGEN, SS-B, LA RIBONUCLEOPROTEIN,
COMPND 6 LA AUTOANTIGEN;
COMPND 7 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: SSB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30
KEYWDS LA MOTIF, ALPHA/BETA, WINGED HELIX DOMAIN, RNA BINDING PROTEIN,
KEYWDS 2 TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ALFANO,D.SANFELICE,J.BABON,G.KELLY,A.JACKS,S.CURRY,M.R.CONTE
REVDAT 3 02-MAR-22 1S7A 1 REMARK
REVDAT 2 24-FEB-09 1S7A 1 VERSN
REVDAT 1 06-APR-04 1S7A 0
JRNL AUTH C.ALFANO,D.SANFELICE,J.BABON,G.KELLY,A.JACKS,S.CURRY,
JRNL AUTH 2 M.R.CONTE
JRNL TITL STRUCTURAL ANALYSIS OF COOPERATIVE RNA BINDING BY THE LA
JRNL TITL 2 MOTIF AND CENTRAL RRM DOMAIN OF HUMAN LA PROTEIN.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 323 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15004549
JRNL DOI 10.1038/NSMB747
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.SANFELICE,J.BABON,G.KELLY,S.CURRY,M.R.CONTE
REMARK 1 TITL RESONANCE ASSIGNMENT AND SECONDARY STRUCTURE OF THE LA MOTIF
REMARK 1 REF J.BIOMOL.NMR V. 27 93
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S7A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021456.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM LA MOTIF U-15N,13C; 20 MM
REMARK 210 TRIS-HCL, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 1C, NMRPIPE 1, TALOS
REMARK 210 1999.019.15.47, MOLMOL 2.6,
REMARK 210 XEASY 6600
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 PHE A 25 H ASP A 27 1.22
REMARK 500 O GLU A 22 H GLY A 26 1.46
REMARK 500 O LEU A 49 H ILE A 53 1.50
REMARK 500 O ASP A 64 H ILE A 68 1.50
REMARK 500 O VAL A 47 H ILE A 89 1.58
REMARK 500 H VAL A 47 O ILE A 89 1.60
REMARK 500 O VAL A 69 H SER A 73 1.60
REMARK 500 O PHE A 25 N ASP A 27 2.15
REMARK 500 O GLU A 22 N GLY A 26 2.18
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 ALA A 2 -77.98 -172.23
REMARK 500 1 ASN A 4 -81.84 -69.44
REMARK 500 1 ASP A 27 -17.92 62.47
REMARK 500 1 ARG A 32 49.11 -145.37
REMARK 500 1 LEU A 42 -75.74 -33.12
REMARK 500 1 ASP A 43 114.41 -166.07
REMARK 500 1 GLU A 44 -24.18 81.14
REMARK 500 1 LEU A 61 -89.87 -124.89
REMARK 500 1 THR A 62 -72.70 -95.50
REMARK 500 1 THR A 63 -3.00 73.34
REMARK 500 1 LEU A 79 -70.25 -48.42
REMARK 500 1 SER A 83 -167.91 -67.98
REMARK 500 2 ALA A 2 -164.84 44.56
REMARK 500 2 GLU A 3 165.56 60.92
REMARK 500 2 ASP A 27 -26.49 64.18
REMARK 500 2 ARG A 32 44.80 -151.05
REMARK 500 2 LEU A 42 -75.44 -51.74
REMARK 500 2 ASP A 43 -118.88 -98.00
REMARK 500 2 LEU A 49 0.11 -60.70
REMARK 500 2 LEU A 61 -85.40 -142.33
REMARK 500 2 PHE A 65 -39.94 -36.72
REMARK 500 2 LYS A 76 53.53 179.90
REMARK 500 2 MET A 80 -161.75 -165.08
REMARK 500 3 ALA A 2 -176.46 59.69
REMARK 500 3 GLU A 3 -168.96 49.84
REMARK 500 3 ASN A 4 -171.32 -55.08
REMARK 500 3 ASP A 6 129.02 66.11
REMARK 500 3 ASN A 7 -66.27 -140.86
REMARK 500 3 ASP A 27 -17.12 164.67
REMARK 500 3 ARG A 32 54.42 -148.47
REMARK 500 3 LEU A 42 -76.90 -47.19
REMARK 500 3 ASP A 43 -116.96 -93.11
REMARK 500 3 LEU A 49 0.22 -60.07
REMARK 500 3 LEU A 61 -77.97 -130.43
REMARK 500 3 THR A 62 -74.05 -103.52
REMARK 500 3 LYS A 76 48.94 -156.25
REMARK 500 3 GLU A 78 83.75 34.28
REMARK 500 3 LEU A 79 -3.09 -153.73
REMARK 500 3 SER A 83 -178.47 -59.55
REMARK 500 3 THR A 87 34.51 -145.76
REMARK 500 4 ASN A 4 64.25 -105.62
REMARK 500 4 ASP A 6 -97.97 -62.47
REMARK 500 4 ASN A 7 -71.24 62.57
REMARK 500 4 ASP A 27 -18.54 161.51
REMARK 500 4 ARG A 32 50.07 -152.32
REMARK 500 4 LEU A 42 -91.62 -54.12
REMARK 500 4 ASP A 43 -131.22 -71.35
REMARK 500 4 LEU A 49 0.18 -61.45
REMARK 500 4 LEU A 61 -100.90 -124.71
REMARK 500 4 ASP A 64 98.19 -61.97
REMARK 500
REMARK 500 THIS ENTRY HAS 260 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6044 RELATED DB: BMRB
REMARK 900 NMR ASSIGNMENT OF THE SAME DOMAIN
REMARK 900 RELATED ID: 1S79 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ADJACENT RRM
REMARK 900 RELATED ID: 1OWX RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-TERMINAL RRM OF THE LA PROTEIN
DBREF 1S7A A 1 103 UNP P05455 LA_HUMAN 1 103
SEQRES 1 A 103 MET ALA GLU ASN GLY ASP ASN GLU LYS MET ALA ALA LEU
SEQRES 2 A 103 GLU ALA LYS ILE CYS HIS GLN ILE GLU TYR TYR PHE GLY
SEQRES 3 A 103 ASP PHE ASN LEU PRO ARG ASP LYS PHE LEU LYS GLU GLN
SEQRES 4 A 103 ILE LYS LEU ASP GLU GLY TRP VAL PRO LEU GLU ILE MET
SEQRES 5 A 103 ILE LYS PHE ASN ARG LEU ASN ARG LEU THR THR ASP PHE
SEQRES 6 A 103 ASN VAL ILE VAL GLU ALA LEU SER LYS SER LYS ALA GLU
SEQRES 7 A 103 LEU MET GLU ILE SER GLU ASP LYS THR LYS ILE ARG ARG
SEQRES 8 A 103 SER PRO SER LYS PRO LEU PRO GLU VAL THR ASP GLU
HELIX 1 1 ASN A 7 GLY A 26 1 20
HELIX 2 2 ASN A 29 ARG A 32 5 4
HELIX 3 3 ASP A 33 ASP A 43 1 11
HELIX 4 4 LEU A 49 PHE A 55 1 7
HELIX 5 5 PHE A 55 ARG A 60 1 6
HELIX 6 6 ASP A 64 SER A 75 1 12
SHEET 1 A 3 VAL A 47 PRO A 48 0
SHEET 2 A 3 LYS A 88 ARG A 90 -1 O ILE A 89 N VAL A 47
SHEET 3 A 3 GLU A 81 ILE A 82 -1 N GLU A 81 O ARG A 90
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