Header list of 1j1h.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 04-DEC-02 1J1H
TITLE SOLUTION STRUCTURE OF A TMRNA-BINDING PROTEIN, SMPB, FROM THERMUS
TITLE 2 THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-11B
KEYWDS SMPB, SSRA ASSOCIATED PROTEIN, OB FOLD, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, RNA
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
MDLTYP MINIMIZED AVERAGE
AUTHOR T.SOMEYA,N.NAMEKI,H.HOSOI,S.SUZUKI,H.HATANAKA,M.FUJII,T.TERADA,
AUTHOR 2 M.SHIROUZU,Y.INOUE,T.SHIBATA,S.KURAMITSU,S.YOKOYAMA,G.KAWAI,RIKEN
AUTHOR 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 23-FEB-22 1J1H 1 REMARK
REVDAT 2 24-FEB-09 1J1H 1 VERSN
REVDAT 1 11-FEB-03 1J1H 0
JRNL AUTH T.SOMEYA,N.NAMEKI,H.HOSOI,S.SUZUKI,H.HATANAKA,M.FUJII,
JRNL AUTH 2 T.TERADA,M.SHIROUZU,Y.INOUE,T.SHIBATA,S.KURAMITSU,
JRNL AUTH 3 S.YOKOYAMA,G.KAWAI
JRNL TITL SOLUTION STRUCTURE OF A TMRNA-BINDING PROTEIN, SMPB, FROM
JRNL TITL 2 THERMUS THERMOPHILUS
JRNL REF FEBS LETT. V. 535 94 2003
JRNL REFN ISSN 0014-5793
JRNL PMID 12560085
JRNL DOI 10.1016/S0014-5793(02)03880-2
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 1J1H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000005511.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM SMPB U-15N; 1MM HCL AND
REMARK 210 100MM NACL; 0.6MM SMPB U-15N,13C;
REMARK 210 1MM HCL AND 100MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : ON THE BASIS OF AGREEMENT WITH
REMARK 210 THE EXPERIMENTAL DATA AND VAN
REMARK 210 DER WAALS 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 1-11
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 124
REMARK 465 ALA A 125
REMARK 465 TYR A 126
REMARK 465 GLU A 127
REMARK 465 LYS A 128
REMARK 465 ARG A 129
REMARK 465 ARG A 130
REMARK 465 GLU A 131
REMARK 465 ASP A 132
REMARK 465 LYS A 133
REMARK 465 LYS A 134
REMARK 465 GLU A 135
REMARK 465 ALA A 136
REMARK 465 VAL A 137
REMARK 465 ARG A 138
REMARK 465 ARG A 139
REMARK 465 ALA A 140
REMARK 465 LEU A 141
REMARK 465 GLU A 142
REMARK 465 GLU A 143
REMARK 465 LEU A 144
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 TYR A 20 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 TYR A 20 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 TYR A 20 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 TYR A 20 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 8 TYR A 20 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 20 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 10 TYR A 20 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
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 VAL A 4 107.93 -49.59
REMARK 500 1 LEU A 5 158.32 57.56
REMARK 500 1 LEU A 17 -71.71 -68.67
REMARK 500 1 THR A 42 154.76 137.68
REMARK 500 1 GLU A 49 30.08 -98.60
REMARK 500 1 GLU A 56 -50.11 -129.14
REMARK 500 1 TYR A 63 39.68 178.29
REMARK 500 1 GLU A 64 47.69 -90.78
REMARK 500 1 TYR A 68 -148.35 -123.29
REMARK 500 1 ASN A 70 92.54 -172.85
REMARK 500 1 PRO A 73 -89.84 -76.18
REMARK 500 1 ARG A 74 -37.84 -175.45
REMARK 500 1 LYS A 76 -44.18 82.09
REMARK 500 1 ARG A 77 176.98 101.34
REMARK 500 1 LYS A 78 52.59 90.22
REMARK 500 1 GLN A 95 -84.02 -47.30
REMARK 500 1 LYS A 96 111.34 178.11
REMARK 500 1 LEU A 103 -46.19 -20.42
REMARK 500 2 ALA A 2 176.11 176.32
REMARK 500 2 LEU A 5 142.29 60.53
REMARK 500 2 LEU A 17 -73.31 -71.21
REMARK 500 2 THR A 42 154.20 128.80
REMARK 500 2 GLU A 56 -63.80 -128.01
REMARK 500 2 TYR A 63 54.18 -146.41
REMARK 500 2 LYS A 65 17.53 -141.39
REMARK 500 2 TYR A 68 -156.33 -120.60
REMARK 500 2 ALA A 69 87.79 44.19
REMARK 500 2 ASN A 70 -168.77 -162.69
REMARK 500 2 ARG A 74 -7.19 144.03
REMARK 500 2 ARG A 75 77.77 63.03
REMARK 500 2 LYS A 76 123.65 66.23
REMARK 500 2 ARG A 77 -139.51 -111.93
REMARK 500 2 GLN A 95 -95.18 -51.70
REMARK 500 2 LYS A 96 110.22 -172.79
REMARK 500 3 ALA A 2 147.12 175.70
REMARK 500 3 LEU A 5 150.07 57.21
REMARK 500 3 THR A 42 154.29 130.92
REMARK 500 3 PRO A 62 -159.46 -74.76
REMARK 500 3 LYS A 65 83.84 -166.58
REMARK 500 3 ALA A 69 -45.62 -146.71
REMARK 500 3 ASN A 70 32.45 -177.75
REMARK 500 3 PRO A 73 -163.62 -71.11
REMARK 500 3 LYS A 76 -95.72 53.69
REMARK 500 3 ARG A 77 114.46 -178.36
REMARK 500 3 LYS A 78 50.84 171.09
REMARK 500 3 GLN A 95 -76.66 -46.04
REMARK 500 3 LYS A 96 102.96 167.06
REMARK 500 3 PRO A 102 91.35 -69.79
REMARK 500 4 LEU A 5 148.96 53.76
REMARK 500 4 LEU A 17 -71.64 -73.51
REMARK 500
REMARK 500 THIS ENTRY HAS 149 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 8 0.25 SIDE CHAIN
REMARK 500 1 ARG A 9 0.28 SIDE CHAIN
REMARK 500 1 ARG A 35 0.32 SIDE CHAIN
REMARK 500 1 ARG A 47 0.19 SIDE CHAIN
REMARK 500 1 ARG A 74 0.30 SIDE CHAIN
REMARK 500 1 ARG A 75 0.19 SIDE CHAIN
REMARK 500 1 ARG A 77 0.13 SIDE CHAIN
REMARK 500 1 ARG A 87 0.08 SIDE CHAIN
REMARK 500 1 ARG A 110 0.20 SIDE CHAIN
REMARK 500 1 ARG A 121 0.18 SIDE CHAIN
REMARK 500 2 ARG A 8 0.32 SIDE CHAIN
REMARK 500 2 ARG A 9 0.31 SIDE CHAIN
REMARK 500 2 ARG A 11 0.22 SIDE CHAIN
REMARK 500 2 ARG A 35 0.32 SIDE CHAIN
REMARK 500 2 ARG A 47 0.10 SIDE CHAIN
REMARK 500 2 ARG A 75 0.32 SIDE CHAIN
REMARK 500 2 ARG A 77 0.20 SIDE CHAIN
REMARK 500 2 ARG A 87 0.26 SIDE CHAIN
REMARK 500 2 ARG A 88 0.31 SIDE CHAIN
REMARK 500 2 ARG A 110 0.28 SIDE CHAIN
REMARK 500 2 ARG A 121 0.18 SIDE CHAIN
REMARK 500 3 ARG A 8 0.25 SIDE CHAIN
REMARK 500 3 ARG A 9 0.10 SIDE CHAIN
REMARK 500 3 ARG A 11 0.23 SIDE CHAIN
REMARK 500 3 ARG A 35 0.26 SIDE CHAIN
REMARK 500 3 ARG A 47 0.32 SIDE CHAIN
REMARK 500 3 ARG A 74 0.32 SIDE CHAIN
REMARK 500 3 ARG A 75 0.22 SIDE CHAIN
REMARK 500 3 ARG A 77 0.09 SIDE CHAIN
REMARK 500 3 ARG A 87 0.28 SIDE CHAIN
REMARK 500 3 ARG A 88 0.28 SIDE CHAIN
REMARK 500 3 ARG A 110 0.28 SIDE CHAIN
REMARK 500 3 ARG A 121 0.32 SIDE CHAIN
REMARK 500 4 ARG A 8 0.20 SIDE CHAIN
REMARK 500 4 ARG A 11 0.29 SIDE CHAIN
REMARK 500 4 ARG A 35 0.27 SIDE CHAIN
REMARK 500 4 ARG A 47 0.30 SIDE CHAIN
REMARK 500 4 ARG A 74 0.32 SIDE CHAIN
REMARK 500 4 ARG A 75 0.32 SIDE CHAIN
REMARK 500 4 ARG A 77 0.27 SIDE CHAIN
REMARK 500 4 ARG A 87 0.26 SIDE CHAIN
REMARK 500 4 ARG A 110 0.31 SIDE CHAIN
REMARK 500 4 ARG A 121 0.24 SIDE CHAIN
REMARK 500 5 ARG A 8 0.16 SIDE CHAIN
REMARK 500 5 ARG A 9 0.12 SIDE CHAIN
REMARK 500 5 ARG A 11 0.32 SIDE CHAIN
REMARK 500 5 ARG A 35 0.13 SIDE CHAIN
REMARK 500 5 ARG A 74 0.16 SIDE CHAIN
REMARK 500 5 ARG A 75 0.29 SIDE CHAIN
REMARK 500 5 ARG A 77 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 123 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000801.1 RELATED DB: TARGETDB
DBREF 1J1H A 1 144 UNP Q8RR57 SSRP_THET8 1 144
SEQRES 1 A 144 MET ALA PRO VAL LEU GLU ASN ARG ARG ALA ARG HIS ASP
SEQRES 2 A 144 TYR GLU ILE LEU GLU THR TYR GLU ALA GLY ILE ALA LEU
SEQRES 3 A 144 LYS GLY THR GLU VAL LYS SER LEU ARG ALA GLY LYS VAL
SEQRES 4 A 144 ASP PHE THR GLY SER PHE ALA ARG PHE GLU ASP GLY GLU
SEQRES 5 A 144 LEU TYR LEU GLU ASN LEU TYR ILE ALA PRO TYR GLU LYS
SEQRES 6 A 144 GLY SER TYR ALA ASN VAL ASP PRO ARG ARG LYS ARG LYS
SEQRES 7 A 144 LEU LEU LEU HIS LYS HIS GLU LEU ARG ARG LEU LEU GLY
SEQRES 8 A 144 LYS VAL GLU GLN LYS GLY LEU THR LEU VAL PRO LEU LYS
SEQRES 9 A 144 ILE TYR PHE ASN GLU ARG GLY TYR ALA LYS VAL LEU LEU
SEQRES 10 A 144 GLY LEU ALA ARG GLY LYS LYS ALA TYR GLU LYS ARG ARG
SEQRES 11 A 144 GLU ASP LYS LYS GLU ALA VAL ARG ARG ALA LEU GLU GLU
SEQRES 12 A 144 LEU
HELIX 1 1 ASN A 7 ASP A 13 1 7
HELIX 2 2 THR A 29 ALA A 36 1 8
HELIX 3 3 HIS A 82 GLU A 94 1 13
SHEET 1 A 3 GLU A 21 GLY A 23 0
SHEET 2 A 3 LYS A 114 LEU A 116 -1 O VAL A 115 N ALA A 22
SHEET 3 A 3 LYS A 104 TYR A 106 -1 N TYR A 106 O LYS A 114
SHEET 1 B 2 LYS A 38 VAL A 39 0
SHEET 2 B 2 ILE A 60 ALA A 61 -1 O ALA A 61 N LYS A 38
SHEET 1 C 2 ALA A 46 PHE A 48 0
SHEET 2 C 2 LEU A 53 LEU A 55 -1 O TYR A 54 N ARG A 47
SHEET 1 D 2 LEU A 98 THR A 99 0
SHEET 2 D 2 ALA A 120 ARG A 121 -1 O ALA A 120 N THR A 99
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 - b 23 2 Bytes