Header list of 1sjr.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 04-MAR-04 1SJR
TITLE NMR STRUCTURE OF RRM2 FROM HUMAN POLYPYRIMIDINE TRACT BINDING PROTEIN
TITLE 2 ISOFORM 1 (PTB1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYPYRIMIDINE TRACT-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PTB, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN I, HNRNP I, 57
COMPND 5 KDA RNA-BINDING PROTEIN PPTB-1;
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 GENE: PTBP1, PTB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009 (QIAGEN);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE9
KEYWDS EXTENDED BABBAB MOTIF, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR P.J.SIMPSON,T.P.MONIE,A.SZENDROI,N.DAVYDOVA,J.K.TYZACK,M.R.CONTE,
AUTHOR 2 C.M.READ,P.D.CARY,D.I.SVERGUN,P.V.KONAREV,M.V.PETOUKHOV,S.CURRY,
AUTHOR 3 S.J.MATTHEWS
REVDAT 3 02-MAR-22 1SJR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SJR 1 VERSN
REVDAT 1 14-SEP-04 1SJR 0
JRNL AUTH P.J.SIMPSON,T.P.MONIE,A.SZENDROI,N.DAVYDOVA,J.K.TYZACK,
JRNL AUTH 2 M.R.CONTE,C.M.READ,P.D.CARY,D.I.SVERGUN,P.V.KONAREV,S.CURRY,
JRNL AUTH 3 S.J.MATTHEWS
JRNL TITL STRUCTURE AND RNA INTERACTIONS OF THE N-TERMINAL RRM DOMAINS
JRNL TITL 2 OF PTB
JRNL REF STRUCTURE V. 12 1631 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15341728
JRNL DOI 10.1016/J.STR.2004.07.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SJR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021770.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.3 M
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.25 MM PTB1-2, U-15N, 13C, 50
REMARK 210 MM NA PHOSPHATE BUFFER, 100 MM
REMARK 210 NACL, 10 MM DTT, 2 MM NAN3,10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
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 : NMRPIPE 1, NMRVIEW 4.1.3, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : HYBRID DISTANCE
REMARK 210 GEOMETRY/SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 1-16
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 ALA A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 GLN A 15
REMARK 465 ALA A 16
REMARK 465 VAL A 17
REMARK 465 ASN A 18
REMARK 465 SER A 19
REMARK 465 VAL A 20
REMARK 465 GLN A 21
REMARK 465 SER A 22
REMARK 465 GLY A 23
REMARK 465 ASN A 24
REMARK 465 LEU A 25
REMARK 465 ALA A 26
REMARK 465 LEU A 27
REMARK 465 ALA A 28
REMARK 465 ALA A 29
REMARK 465 SER A 30
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 VAL A 34
REMARK 465 ASP A 35
REMARK 465 ALA A 36
REMARK 465 GLY A 37
REMARK 465 MET A 38
REMARK 465 ALA A 39
REMARK 465 SER A 148
REMARK 465 GLN A 149
REMARK 465 PRO A 150
REMARK 465 SER A 151
REMARK 465 LEU A 152
REMARK 465 ASP A 153
REMARK 465 GLN A 154
REMARK 465 THR A 155
REMARK 465 MET A 156
REMARK 465 ALA A 157
REMARK 465 ALA A 158
REMARK 465 ALA A 159
REMARK 465 PHE A 160
REMARK 465 GLY A 161
REMARK 465 LEU A 162
REMARK 465 SER A 163
REMARK 465 VAL A 164
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 67 HH TYR A 91 1.38
REMARK 500 H ASN A 131 O PRO A 144 1.50
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 41 65.10 -68.39
REMARK 500 1 GLN A 43 57.03 36.38
REMARK 500 1 ASN A 53 77.26 70.95
REMARK 500 1 PHE A 55 -75.08 -142.21
REMARK 500 1 ASN A 83 40.87 85.62
REMARK 500 1 TYR A 110 -64.82 -129.39
REMARK 500 1 ASN A 111 -66.20 -147.15
REMARK 500 1 ALA A 112 41.59 -148.24
REMARK 500 1 CYS A 114 33.12 73.40
REMARK 500 1 THR A 115 124.26 -36.20
REMARK 500 1 SER A 121 171.14 -50.96
REMARK 500 1 THR A 124 19.11 55.74
REMARK 500 1 LYS A 129 24.94 -143.48
REMARK 500 1 ASN A 132 -91.21 -146.02
REMARK 500 1 ASP A 133 -41.34 -140.81
REMARK 500 1 ARG A 136 108.58 -165.54
REMARK 500 1 ASP A 142 30.32 -89.02
REMARK 500 2 ALA A 41 91.47 -179.86
REMARK 500 2 GLN A 43 77.10 81.49
REMARK 500 2 ASN A 53 75.05 37.16
REMARK 500 2 PHE A 55 -48.91 -155.06
REMARK 500 2 ASN A 82 -19.03 86.94
REMARK 500 2 ASN A 83 41.00 158.93
REMARK 500 2 ASN A 111 -65.20 66.69
REMARK 500 2 ALA A 112 48.79 -165.14
REMARK 500 2 CYS A 114 33.68 72.60
REMARK 500 2 THR A 115 107.72 -36.24
REMARK 500 2 THR A 124 19.36 55.16
REMARK 500 2 SER A 125 167.66 158.86
REMARK 500 2 ASN A 127 109.40 -59.35
REMARK 500 2 LYS A 129 40.19 -143.25
REMARK 500 2 ASN A 132 -90.97 -170.46
REMARK 500 2 ASP A 133 -40.68 -138.80
REMARK 500 2 TYR A 138 70.98 -110.78
REMARK 500 2 THR A 139 -35.58 -176.97
REMARK 500 3 ALA A 41 44.85 -165.98
REMARK 500 3 ASN A 53 80.50 64.96
REMARK 500 3 PHE A 55 -59.00 -148.50
REMARK 500 3 LYS A 81 -95.16 -72.08
REMARK 500 3 ASN A 82 38.97 -91.64
REMARK 500 3 ASN A 83 44.24 86.61
REMARK 500 3 TYR A 110 -77.68 -112.52
REMARK 500 3 ASN A 111 87.72 -152.13
REMARK 500 3 THR A 115 136.61 -38.96
REMARK 500 3 SER A 121 170.49 -50.75
REMARK 500 3 THR A 124 18.24 56.84
REMARK 500 3 ASN A 127 60.64 -102.79
REMARK 500 3 LYS A 129 15.44 -142.19
REMARK 500 3 ASN A 132 -28.31 86.75
REMARK 500 3 ASP A 142 30.98 -89.79
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SJQ RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF RRM1 FROM HUMAN POLYPYRIMIDINE TRACT BINDING
REMARK 900 PROTEIN ISOFORM 1 (PTB1)
DBREF 1SJR A 10 164 UNP P26599 PTBP1_HUMAN 147 301
SEQADV 1SJR MET A 1 UNP P26599 INITIATING METHIONINE
SEQADV 1SJR HIS A 2 UNP P26599 EXPRESSION TAG
SEQADV 1SJR HIS A 3 UNP P26599 EXPRESSION TAG
SEQADV 1SJR HIS A 4 UNP P26599 EXPRESSION TAG
SEQADV 1SJR HIS A 5 UNP P26599 EXPRESSION TAG
SEQADV 1SJR HIS A 6 UNP P26599 EXPRESSION TAG
SEQADV 1SJR HIS A 7 UNP P26599 EXPRESSION TAG
SEQADV 1SJR GLY A 8 UNP P26599 EXPRESSION TAG
SEQADV 1SJR SER A 9 UNP P26599 EXPRESSION TAG
SEQRES 1 A 164 MET HIS HIS HIS HIS HIS HIS GLY SER ALA GLN ALA ALA
SEQRES 2 A 164 LEU GLN ALA VAL ASN SER VAL GLN SER GLY ASN LEU ALA
SEQRES 3 A 164 LEU ALA ALA SER ALA ALA ALA VAL ASP ALA GLY MET ALA
SEQRES 4 A 164 MET ALA GLY GLN SER PRO VAL LEU ARG ILE ILE VAL GLU
SEQRES 5 A 164 ASN LEU PHE TYR PRO VAL THR LEU ASP VAL LEU HIS GLN
SEQRES 6 A 164 ILE PHE SER LYS PHE GLY THR VAL LEU LYS ILE ILE THR
SEQRES 7 A 164 PHE THR LYS ASN ASN GLN PHE GLN ALA LEU LEU GLN TYR
SEQRES 8 A 164 ALA ASP PRO VAL SER ALA GLN HIS ALA LYS LEU SER LEU
SEQRES 9 A 164 ASP GLY GLN ASN ILE TYR ASN ALA CYS CYS THR LEU ARG
SEQRES 10 A 164 ILE ASP PHE SER LYS LEU THR SER LEU ASN VAL LYS TYR
SEQRES 11 A 164 ASN ASN ASP LYS SER ARG ASP TYR THR ARG PRO ASP LEU
SEQRES 12 A 164 PRO SER GLY ASP SER GLN PRO SER LEU ASP GLN THR MET
SEQRES 13 A 164 ALA ALA ALA PHE GLY LEU SER VAL
HELIX 1 1 THR A 59 GLY A 71 1 13
HELIX 2 2 ASP A 93 LEU A 104 1 12
SHEET 1 A 5 LEU A 116 PHE A 120 0
SHEET 2 A 5 VAL A 46 VAL A 51 -1 N ARG A 48 O ASP A 119
SHEET 3 A 5 PHE A 85 TYR A 91 -1 O ALA A 87 N ILE A 49
SHEET 4 A 5 VAL A 73 THR A 80 -1 N ILE A 77 O LEU A 88
SHEET 5 A 5 SER A 135 ASP A 137 -1 O ARG A 136 N ILE A 76
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