Header list of 1n4y.pdb file
Complete list - p 12 2 Bytes
HEADER BLOOD CLOTTING 02-NOV-02 1N4Y TITLE REFINED STRUCTURE OF KISTRIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: KISTRIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RHODOSTOMIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CALLOSELASMA RHODOSTOMA; SOURCE 3 ORGANISM_COMMON: MALAYAN PIT VIPER; SOURCE 4 ORGANISM_TAXID: 8717; SOURCE 5 GENE: RHOD; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PZKIS KEYWDS BETA, VENOM, BLOOD COAGULATION, RGD, BLOOD CLOTTING EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR A.M.KREZEL,J.KRANE,M.S.DENNIS,R.A.LAZARUS,G.WAGNER REVDAT 2 24-FEB-09 1N4Y 1 VERSN REVDAT 1 28-JAN-03 1N4Y 0 SPRSDE 28-JAN-03 1N4Y 1KST JRNL AUTH R.A.ADLER,R.A.LAZARUS,M.S.DENNIS,G.WAGNER JRNL TITL SOLUTION STRUCTURE OF KISTRIN, A POTENT PLATELET JRNL TITL 2 AGGREGATION INHIBITOR AND GP IIB-IIIA ANTAGONIST. JRNL REF SCIENCE V. 253 445 1991 JRNL REFN ISSN 0036-8075 JRNL PMID 1862345 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPAL REMARK 3 AUTHORS : JONES,ZOU,COWAN,KJELDGAARD REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1N4Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-02. REMARK 100 THE RCSB ID CODE IS RCSB017524. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.7 REMARK 210 IONIC STRENGTH : 5 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM KISTRIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 750 MHZ REMARK 210 SPECTROMETER MODEL : AMX, INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER, VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 1.1, FELIX 1995 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 18 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 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 GLN A 60 23.49 -140.60 REMARK 500 1 PRO A 65 -77.88 -75.06 REMARK 500 1 ARG A 66 -55.12 -155.05 REMARK 500 1 TYR A 67 4.69 -151.49 REMARK 500 2 PRO A 65 -70.66 -74.96 REMARK 500 2 ARG A 66 -50.64 -172.74 REMARK 500 3 ARG A 49 30.01 -147.42 REMARK 500 3 PRO A 65 -80.24 -74.94 REMARK 500 3 ARG A 66 -55.86 -161.68 REMARK 500 4 ARG A 49 27.42 -146.54 REMARK 500 4 GLN A 60 -53.26 -163.27 REMARK 500 4 ARG A 66 -52.91 -169.75 REMARK 500 5 ASP A 51 28.66 -140.21 REMARK 500 5 PRO A 65 -74.43 -75.05 REMARK 500 5 ARG A 66 -49.83 -170.65 REMARK 500 6 PRO A 65 -70.12 -75.04 REMARK 500 6 ARG A 66 -54.35 -168.82 REMARK 500 7 LYS A 2 -155.66 58.87 REMARK 500 7 ARG A 49 28.79 -146.43 REMARK 500 7 PRO A 65 -83.09 -75.01 REMARK 500 7 ARG A 66 -53.96 -155.47 REMARK 500 8 ASP A 51 28.46 -144.15 REMARK 500 8 GLN A 60 -46.44 -174.51 REMARK 500 8 PRO A 65 -76.96 -74.93 REMARK 500 8 ARG A 66 -47.21 -168.91 REMARK 500 9 PRO A 23 -168.42 -75.03 REMARK 500 9 PRO A 65 -81.24 -74.94 REMARK 500 9 ARG A 66 -63.97 -168.11 REMARK 500 9 TYR A 67 8.79 -151.79 REMARK 500 10 PRO A 65 -82.38 -74.95 REMARK 500 10 ARG A 66 -52.91 -171.27 REMARK 500 11 PRO A 65 -80.09 -74.98 REMARK 500 11 ARG A 66 -57.68 -162.02 REMARK 500 12 GLN A 60 -45.76 -166.33 REMARK 500 12 ARG A 66 -57.23 -168.66 REMARK 500 13 PRO A 65 -82.03 -74.97 REMARK 500 13 ARG A 66 -59.31 -162.51 REMARK 500 13 TYR A 67 10.53 -158.03 REMARK 500 14 GLN A 60 26.66 -142.42 REMARK 500 14 ARG A 66 -55.24 -170.64 REMARK 500 15 GLN A 60 -49.62 -169.25 REMARK 500 15 PRO A 65 -76.58 -74.88 REMARK 500 15 ARG A 66 -60.43 -165.16 REMARK 500 16 PRO A 23 -168.83 -74.95 REMARK 500 16 ASP A 51 26.18 -140.44 REMARK 500 16 GLN A 60 -49.51 -166.79 REMARK 500 16 PRO A 65 -79.03 -75.05 REMARK 500 16 ARG A 66 -50.93 -163.12 REMARK 500 17 PRO A 65 -73.58 -74.92 REMARK 500 17 ARG A 66 -53.41 -169.41 REMARK 500 18 PRO A 65 -76.67 -74.86 REMARK 500 18 ARG A 66 -49.61 -165.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR A 67 HIS A 68 1 -126.97 REMARK 500 ARG A 22 PRO A 23 2 -144.98 REMARK 500 GLN A 60 SER A 61 4 -145.19 REMARK 500 ARG A 22 PRO A 23 5 -145.26 REMARK 500 GLY A 50 ASP A 51 11 -149.32 REMARK 500 ARG A 22 PRO A 23 16 -146.50 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 46 0.10 SIDE_CHAIN REMARK 500 2 ARG A 22 0.08 SIDE_CHAIN REMARK 500 3 ARG A 46 0.11 SIDE_CHAIN REMARK 500 4 ARG A 46 0.13 SIDE_CHAIN REMARK 500 5 ARG A 22 0.08 SIDE_CHAIN REMARK 500 5 ARG A 46 0.10 SIDE_CHAIN REMARK 500 6 ARG A 46 0.09 SIDE_CHAIN REMARK 500 8 ARG A 46 0.09 SIDE_CHAIN REMARK 500 9 ARG A 40 0.12 SIDE_CHAIN REMARK 500 9 ARG A 46 0.11 SIDE_CHAIN REMARK 500 10 ARG A 46 0.09 SIDE_CHAIN REMARK 500 11 ARG A 46 0.11 SIDE_CHAIN REMARK 500 12 ARG A 40 0.09 SIDE_CHAIN REMARK 500 12 ARG A 46 0.09 SIDE_CHAIN REMARK 500 14 ARG A 46 0.09 SIDE_CHAIN REMARK 500 15 ARG A 46 0.12 SIDE_CHAIN REMARK 500 16 ARG A 22 0.08 SIDE_CHAIN REMARK 500 17 ARG A 46 0.10 SIDE_CHAIN REMARK 500 18 ARG A 46 0.09 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KST RELATED DB: PDB DBREF 1N4Y A 1 68 UNP P30403 DISR_AGKRH 408 475 SEQRES 1 A 68 GLY LYS GLU CYS ASP CYS SER SER PRO GLU ASN PRO CYS SEQRES 2 A 68 CYS ASP ALA ALA THR CYS LYS LEU ARG PRO GLY ALA GLN SEQRES 3 A 68 CYS GLY GLU GLY LEU CYS CYS GLU GLN CYS LYS PHE SER SEQRES 4 A 68 ARG ALA GLY LYS ILE CYS ARG ILE PRO ARG GLY ASP MET SEQRES 5 A 68 PRO ASP ASP ARG CYS THR GLY GLN SER ALA ASP CYS PRO SEQRES 6 A 68 ARG TYR HIS SHEET 1 A 2 CYS A 33 GLU A 34 0 SHEET 2 A 2 LYS A 37 PHE A 38 -1 O LYS A 37 N GLU A 34 SHEET 1 B 2 ILE A 44 ARG A 46 0 SHEET 2 B 2 ASP A 55 ARG A 56 -1 O ASP A 55 N ARG A 46 SSBOND 1 CYS A 4 CYS A 19 1555 1555 2.08 SSBOND 2 CYS A 6 CYS A 14 1555 1555 2.00 SSBOND 3 CYS A 13 CYS A 36 1555 1555 1.99 SSBOND 4 CYS A 27 CYS A 33 1555 1555 2.05 SSBOND 5 CYS A 32 CYS A 57 1555 1555 2.09 SSBOND 6 CYS A 45 CYS A 64 1555 1555 2.01 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 - p 12 2 Bytes