Header list of 1kg1.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 26-NOV-01 1KG1 TITLE NMR STRUCTURE OF THE NIP1 ELICITOR PROTEIN FROM RHYNCHOSPORIUM SECALIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: NECROSIS INDUCING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NIP1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHYNCHOSPORIUM SECALIS; SOURCE 3 ORGANISM_COMMON: LEAF BLOTCH OF BARLEY; SOURCE 4 ORGANISM_TAXID: 38038; SOURCE 5 GENE: NIP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AD494; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30 KEYWDS ANTIPARALEL BETA SHEETS, TOXIN EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR K.A.VAN'T SLOT,H.A.VAN DEN BURG,C.P.KLOKS,C.W.HILBERS,W.KNOGGE, AUTHOR 2 C.H.PAPAVOINE REVDAT 4 23-FEB-22 1KG1 1 REMARK REVDAT 3 24-FEB-09 1KG1 1 VERSN REVDAT 2 18-NOV-03 1KG1 1 JRNL REVDAT 1 11-NOV-03 1KG1 0 JRNL AUTH K.A.VAN'T SLOT,H.A.VAN DEN BURG,C.P.KLOKS,C.W.HILBERS, JRNL AUTH 2 W.KNOGGE,C.H.PAPAVOINE JRNL TITL SOLUTION STRUCTURE OF THE PLANT DISEASE JRNL TITL 2 RESISTANCE-TRIGGERING PROTEIN NIP1 FROM THE FUNGUS JRNL TITL 3 RHYNCHOSPORIUM SECALIS SHOWS A NOVEL BETA-SHEET FOLD. JRNL REF J.BIOL.CHEM. V. 278 45730 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12944393 JRNL DOI 10.1074/JBC.M308304200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUNTERT (DYANA), GUNTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BESED ON A TOTAL OF REMARK 3 785 RESTRAINTS: 740 NOE RESTRAINTS AND 45, 40 TORSION ANGLE REMARK 3 RESTRAINTS AND 5 DISULFIDE BONDS REMARK 4 REMARK 4 1KG1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-01. REMARK 100 THE DEPOSITION ID IS D_1000014918. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.0MM NIP1, 97% 15N REMARK 210 INCORPORATION; 2.0MM NIP1, REMARK 210 UNLABELED; 2.0MM NIP1, UNLABELED REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; REMARK 210 HNHB; 2D NOESY; DQF-COSY; HMQC- REMARK 210 NOESY-HMQC; 2D HMQC-J REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE VERSION 1.8 REV REMARK 210 2001.030.21.27, XEASY 1.3.13 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: DISULFIDE BOND PATTERN WAS DETERMINED INDEPENDENTLY 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 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 TYR A 5 109.95 -48.20 REMARK 500 1 ALA A 12 79.01 -150.77 REMARK 500 1 LEU A 13 -84.02 173.19 REMARK 500 1 LYS A 14 132.58 174.59 REMARK 500 1 LEU A 27 93.07 -67.12 REMARK 500 1 GLU A 46 125.68 -38.68 REMARK 500 2 CYS A 3 158.70 59.69 REMARK 500 2 TYR A 5 99.98 -38.84 REMARK 500 2 ALA A 12 81.10 -151.77 REMARK 500 2 LEU A 13 -94.11 176.34 REMARK 500 2 LYS A 14 121.97 -175.40 REMARK 500 2 LEU A 27 77.36 -64.81 REMARK 500 2 PRO A 29 -168.09 -75.05 REMARK 500 2 LYS A 36 29.19 -148.42 REMARK 500 2 GLU A 46 151.05 59.64 REMARK 500 2 GLN A 59 125.18 -35.14 REMARK 500 3 CYS A 3 137.55 86.76 REMARK 500 3 TYR A 5 98.10 -36.08 REMARK 500 3 ALA A 12 74.28 -150.54 REMARK 500 3 LEU A 13 -92.72 177.56 REMARK 500 3 LYS A 14 117.17 179.50 REMARK 500 3 ALA A 15 125.66 -36.46 REMARK 500 3 PRO A 29 -169.53 -75.10 REMARK 500 3 GLN A 52 -169.39 -119.58 REMARK 500 4 CYS A 3 161.40 -43.84 REMARK 500 4 ARG A 4 79.55 -101.77 REMARK 500 4 ALA A 12 72.85 -150.78 REMARK 500 4 LEU A 13 -89.58 175.02 REMARK 500 4 LYS A 14 133.07 177.70 REMARK 500 4 ALA A 15 129.68 -39.32 REMARK 500 4 LEU A 27 89.85 -60.46 REMARK 500 4 LYS A 36 27.89 -145.01 REMARK 500 4 ASN A 49 87.96 -150.32 REMARK 500 4 GLN A 59 126.83 -37.62 REMARK 500 5 CYS A 3 153.32 178.82 REMARK 500 5 ALA A 12 72.32 -152.90 REMARK 500 5 LEU A 13 -99.53 -178.86 REMARK 500 5 LEU A 27 87.58 -60.84 REMARK 500 5 PRO A 29 -169.15 -75.02 REMARK 500 5 GLU A 46 139.59 -36.63 REMARK 500 5 GLN A 59 140.56 -35.78 REMARK 500 6 CYS A 3 157.83 76.72 REMARK 500 6 ALA A 12 44.72 -89.74 REMARK 500 6 LEU A 13 54.28 31.90 REMARK 500 6 LYS A 14 78.90 -152.12 REMARK 500 6 LEU A 27 90.54 -60.28 REMARK 500 6 SER A 43 116.01 -160.50 REMARK 500 6 ASN A 49 79.85 -113.40 REMARK 500 6 GLN A 59 143.62 -38.69 REMARK 500 7 ALA A 12 76.74 -152.73 REMARK 500 REMARK 500 THIS ENTRY HAS 202 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5199 RELATED DB: BMRB REMARK 900 5199 CONTAINS NIP1 WITH CHEMICAL SHIFT VALUES AND TORSION ANGLES. DBREF 1KG1 A 1 60 UNP Q02039 Q02039_RHYSE 23 82 SEQRES 1 A 60 ASP ARG CYS ARG TYR THR LEU CYS CYS ASP GLY ALA LEU SEQRES 2 A 60 LYS ALA VAL SER ALA CYS LEU HIS GLU SER GLU SER CYS SEQRES 3 A 60 LEU VAL PRO GLY ASP CYS CYS ARG GLY LYS SER ARG LEU SEQRES 4 A 60 THR LEU CYS SER TYR GLY GLU GLY GLY ASN GLY PHE GLN SEQRES 5 A 60 CYS PRO THR GLY TYR ARG GLN CYS SHEET 1 A 2 ARG A 4 CYS A 8 0 SHEET 2 A 2 VAL A 16 LEU A 20 -1 O ALA A 18 N THR A 6 SHEET 1 B 3 SER A 37 LEU A 41 0 SHEET 2 B 3 GLY A 30 ARG A 34 -1 N ARG A 34 O SER A 37 SHEET 3 B 3 ARG A 58 GLN A 59 -1 O ARG A 58 N CYS A 33 SSBOND 1 CYS A 3 CYS A 19 1555 1555 1.98 SSBOND 2 CYS A 8 CYS A 26 1555 1555 1.96 SSBOND 3 CYS A 9 CYS A 42 1555 1555 1.96 SSBOND 4 CYS A 32 CYS A 53 1555 1555 2.11 SSBOND 5 CYS A 33 CYS A 60 1555 1555 1.98 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