Header list of 1jmn.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 19-JUL-01 1JMN TITLE SOLUTION STRUCTURE OF THE VISCOTOXIN A2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VISCOTOXIN A2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM; SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE; SOURCE 4 ORGANISM_TAXID: 3972; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS THIONIN, VISCOTOXIN, VISCUM ALBUM, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.MOSBAH,A.COULON,C.BERNARD,K.URECH,P.ROUGE,H.DARBON REVDAT 3 23-FEB-22 1JMN 1 REMARK REVDAT 2 24-FEB-09 1JMN 1 VERSN REVDAT 1 24-JUN-03 1JMN 0 JRNL AUTH A.MOSBAH,A.COULON,C.BERNARD,K.URECH,P.ROUGE,H.DARBON JRNL TITL SOLUTION STRUCTURE OF THE VISCOTOXIN A2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JMN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-01. REMARK 100 THE DEPOSITION ID IS D_1000013942. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM, REMARK 210 STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY, STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND 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: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 3 TYR A 13 CE2 TYR A 13 CD2 -0.097 REMARK 500 4 TYR A 13 CE2 TYR A 13 CD2 -0.093 REMARK 500 5 TYR A 13 CE2 TYR A 13 CD2 -0.120 REMARK 500 8 TYR A 13 CG TYR A 13 CD1 -0.081 REMARK 500 14 TYR A 13 CG TYR A 13 CD1 -0.081 REMARK 500 14 TYR A 13 CE1 TYR A 13 CZ -0.086 REMARK 500 18 TYR A 13 CE2 TYR A 13 CD2 -0.099 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 SER A 22 -148.74 -138.37 REMARK 500 1 SER A 36 32.96 -97.07 REMARK 500 1 ALA A 37 -167.69 -166.93 REMARK 500 1 PRO A 41 -165.65 -72.47 REMARK 500 1 SER A 42 45.91 -83.15 REMARK 500 1 TYR A 44 87.56 48.03 REMARK 500 2 SER A 22 -148.83 -62.95 REMARK 500 2 ALA A 37 -156.09 -178.87 REMARK 500 2 CYS A 40 108.30 51.40 REMARK 500 2 PRO A 41 -157.95 -56.59 REMARK 500 2 SER A 42 42.36 -80.12 REMARK 500 2 ASP A 43 44.59 -106.32 REMARK 500 2 TYR A 44 88.98 47.60 REMARK 500 3 SER A 22 -149.31 -139.68 REMARK 500 3 SER A 36 33.85 -97.20 REMARK 500 3 PRO A 41 -164.80 -73.88 REMARK 500 3 SER A 42 42.23 -79.56 REMARK 500 3 TYR A 44 88.00 48.57 REMARK 500 4 SER A 22 -149.02 -62.62 REMARK 500 4 ALA A 37 -171.27 179.46 REMARK 500 4 PRO A 41 -162.06 -62.25 REMARK 500 4 SER A 42 42.61 -79.52 REMARK 500 4 TYR A 44 88.18 46.00 REMARK 500 5 PRO A 5 -72.99 -41.39 REMARK 500 5 SER A 22 -128.90 -176.13 REMARK 500 5 SER A 36 33.33 -96.44 REMARK 500 5 PRO A 41 -161.54 -68.97 REMARK 500 5 SER A 42 44.13 -81.97 REMARK 500 5 ASP A 43 47.48 -109.92 REMARK 500 5 TYR A 44 77.26 46.41 REMARK 500 6 SER A 22 -146.80 -132.87 REMARK 500 6 SER A 36 33.45 -97.78 REMARK 500 6 ALA A 37 -170.46 -178.49 REMARK 500 6 SER A 42 15.64 39.14 REMARK 500 6 ASP A 43 37.35 -97.51 REMARK 500 6 TYR A 44 82.87 46.98 REMARK 500 7 ASN A 6 -175.87 -177.43 REMARK 500 7 SER A 22 -148.36 -63.24 REMARK 500 7 SER A 36 33.22 -97.73 REMARK 500 7 PRO A 41 -163.47 -68.06 REMARK 500 7 SER A 42 45.11 -81.98 REMARK 500 7 TYR A 44 82.85 47.70 REMARK 500 8 SER A 22 -148.97 -62.98 REMARK 500 8 ALA A 37 -164.59 -177.75 REMARK 500 8 PRO A 41 -167.02 -71.19 REMARK 500 8 SER A 42 45.41 -83.04 REMARK 500 8 TYR A 44 94.44 49.25 REMARK 500 9 SER A 2 121.08 -175.54 REMARK 500 9 CYS A 3 86.71 -62.59 REMARK 500 9 SER A 22 -148.36 -63.27 REMARK 500 REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1JMN A 1 46 UNP P32880 THN2_VISAL 1 46 SEQADV 1JMN GLN A 24 UNP P32880 GLU 24 SEE REMARK 999 SEQADV 1JMN ASP A 43 UNP P32880 TYR 43 SEE REMARK 999 SEQADV 1JMN TYR A 44 UNP P32880 PRO 44 SEE REMARK 999 SEQADV 1JMN PRO A 45 UNP P32880 ASP 45 SEE REMARK 999 SEQRES 1 A 46 LYS SER CYS CYS PRO ASN THR THR GLY ARG ASN ILE TYR SEQRES 2 A 46 ASN THR CYS ARG PHE GLY GLY GLY SER ARG GLN VAL CYS SEQRES 3 A 46 ALA SER LEU SER GLY CYS LYS ILE ILE SER ALA SER THR SEQRES 4 A 46 CYS PRO SER ASP TYR PRO LYS HELIX 1 1 ASN A 6 PHE A 18 1 13 HELIX 2 2 ARG A 23 GLY A 31 1 9 SHEET 1 A 2 SER A 2 CYS A 3 0 SHEET 2 A 2 LYS A 33 ILE A 34 -1 O LYS A 33 N CYS A 3 SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.03 SSBOND 2 CYS A 4 CYS A 32 1555 1555 1.95 SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.02 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 MODEL 1
Complete list - b 23 2 Bytes