Header list of 1ro3.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 01-DEC-03 1RO3
TITLE NEW STRUCTURAL INSIGHTS ON SHORT DISINTEGRIN ECHISTATIN BY NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISINTEGRIN ECHISTATIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PLATELET AGGREGATION ACTIVATION INHIBITOR, CARINATIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECHIS CARINATUS;
SOURCE 3 ORGANISM_COMMON: SAW-SCALED VIPER;
SOURCE 4 ORGANISM_TAXID: 40353
KEYWDS NO REGULAR SECONDARY STRUCTURE, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.MONLEON,V.ESTEVE,J.J.CALVETE,C.MARCINKIEWICZ,B.CELDA
REVDAT 4 02-MAR-22 1RO3 1 REMARK
REVDAT 3 24-FEB-09 1RO3 1 VERSN
REVDAT 2 29-MAR-05 1RO3 1 JRNL
REVDAT 1 09-DEC-03 1RO3 0
JRNL AUTH D.MONLEON,V.ESTEVE,H.KOVACS,J.J.CALVETE,B.CELDA
JRNL TITL CONFORMATION AND CONCERTED DYNAMICS OF THE INTEGRIN-BINDING
JRNL TITL 2 SITE AND THE C-TERMINAL REGION OF ECHISTATIN REVEALED BY
JRNL TITL 3 HOMONUCLEAR NMR
JRNL REF BIOCHEM.J. V. 387 57 2005
JRNL REFN ISSN 0264-6021
JRNL PMID 15535803
JRNL DOI 10.1042/BJ20041343
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, DYANA 1.5
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), GUNTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RO3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020906.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM ECHISTATIN, HCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY 100 MS; 2D NOESY 200 MS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.96, DYANA 1.5
REMARK 210 METHOD USED : INITIAL MANUAL ASSIGNMENT OF
REMARK 210 UNAMBIGUOUS NOES AND EXTENSION
REMARK 210 AND CONFIRMATION OF NOE
REMARK 210 ASSIGNMENTS BY 20 CYCLE SOF NOAH
REMARK 210 STANDARD ROUTINES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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 H ARG A 22 HA ASP A 27 0.68
REMARK 500 HB3 ASP A 30 H CYS A 39 1.03
REMARK 500 H LYS A 21 HB3 ASN A 42 1.06
REMARK 500 O ARG A 22 H ASP A 26 1.10
REMARK 500 HA ILE A 19 HB3 ARG A 41 1.11
REMARK 500 H GLY A 46 HD3 PRO A 47 1.14
REMARK 500 HA ARG A 22 CD2 HIS A 44 1.21
REMARK 500 HG13 ILE A 19 HE1 HIS A 44 1.25
REMARK 500 N ARG A 22 HA ASP A 27 1.27
REMARK 500 HA ARG A 22 HD2 HIS A 44 1.31
REMARK 500 H ALA A 23 HD2 HIS A 44 1.32
REMARK 500 HA ARG A 22 NE2 HIS A 44 1.42
REMARK 500 N ALA A 23 HD2 HIS A 44 1.43
REMARK 500 N CYS A 7 HB3 CYS A 32 1.44
REMARK 500 O CYS A 8 H CYS A 11 1.47
REMARK 500 OD1 ASN A 42 H ALA A 48 1.49
REMARK 500 HD1 TYR A 31 CB ARG A 41 1.50
REMARK 500 C ARG A 22 HD2 HIS A 44 1.51
REMARK 500 CA ARG A 22 HD2 HIS A 44 1.53
REMARK 500 O LYS A 21 H ALA A 23 1.54
REMARK 500 O ILE A 19 H ASP A 29 1.55
REMARK 500 H ARG A 22 CA ASP A 27 1.57
REMARK 500 CG ASN A 42 H ALA A 48 1.58
REMARK 500 CB CYS A 20 O CYS A 39 1.70
REMARK 500 O ARG A 22 N ASP A 26 1.85
REMARK 500 CB ILE A 19 O ARG A 41 2.03
REMARK 500 CA ILE A 19 O ARG A 41 2.07
REMARK 500 CA ARG A 22 CD2 HIS A 44 2.08
REMARK 500 C ARG A 22 O ASP A 26 2.10
REMARK 500 O ASN A 42 CG PRO A 47 2.11
REMARK 500 O THR A 18 N TYR A 31 2.12
REMARK 500 O ILE A 19 O ASP A 29 2.13
REMARK 500 CG1 ILE A 19 O ARG A 41 2.17
REMARK 500 N CYS A 7 CB CYS A 32 2.19
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 GLU A 3 -35.62 -134.66
REMARK 500 1 SER A 4 -14.00 147.12
REMARK 500 1 CYS A 7 54.85 78.70
REMARK 500 1 CYS A 8 43.73 -177.36
REMARK 500 1 ARG A 9 -72.77 -9.57
REMARK 500 1 CYS A 11 72.23 73.64
REMARK 500 1 LYS A 12 -26.69 172.35
REMARK 500 1 PHE A 13 138.47 62.10
REMARK 500 1 LEU A 14 -86.05 -94.10
REMARK 500 1 LYS A 15 78.33 -175.78
REMARK 500 1 GLU A 16 106.81 15.62
REMARK 500 1 THR A 18 78.28 -68.11
REMARK 500 1 CYS A 20 -91.07 -46.22
REMARK 500 1 ARG A 22 64.86 -62.06
REMARK 500 1 ARG A 24 -28.28 -36.25
REMARK 500 1 ASP A 26 -118.01 -166.70
REMARK 500 1 MET A 28 -88.85 -101.85
REMARK 500 1 ASP A 29 -136.96 -143.94
REMARK 500 1 LYS A 35 -52.18 -131.02
REMARK 500 1 CYS A 39 28.07 86.31
REMARK 500 1 ARG A 41 54.76 -177.77
REMARK 500 1 PRO A 43 47.86 -74.95
REMARK 500 1 HIS A 44 -140.80 -101.23
REMARK 500 1 LYS A 45 -77.85 -21.72
REMARK 500 1 PRO A 47 -151.22 -75.03
REMARK 500 1 ALA A 48 121.78 112.44
REMARK 500 2 GLU A 3 60.09 65.23
REMARK 500 2 SER A 4 27.47 -170.74
REMARK 500 2 CYS A 7 49.55 75.85
REMARK 500 2 CYS A 8 50.99 -170.94
REMARK 500 2 ARG A 9 -80.15 -3.91
REMARK 500 2 CYS A 11 72.31 157.13
REMARK 500 2 LYS A 12 -21.44 171.95
REMARK 500 2 PHE A 13 150.76 63.72
REMARK 500 2 LEU A 14 -84.44 -109.59
REMARK 500 2 LYS A 15 93.37 -175.73
REMARK 500 2 GLU A 16 107.29 -1.12
REMARK 500 2 CYS A 20 -89.43 -48.70
REMARK 500 2 ARG A 22 58.21 -63.51
REMARK 500 2 ARG A 24 -32.37 -28.27
REMARK 500 2 ASP A 26 -117.88 -168.71
REMARK 500 2 MET A 28 -84.31 -101.71
REMARK 500 2 ASP A 29 -138.68 -148.51
REMARK 500 2 CYS A 32 127.44 -32.96
REMARK 500 2 LYS A 35 -67.93 -109.45
REMARK 500 2 ASP A 38 58.13 -147.06
REMARK 500 2 CYS A 39 39.13 77.15
REMARK 500 2 ARG A 41 68.49 -178.17
REMARK 500 2 ASN A 42 51.29 -140.58
REMARK 500 2 HIS A 44 -137.46 -109.44
REMARK 500
REMARK 500 THIS ENTRY HAS 559 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ECH RELATED DB: PDB
REMARK 900 PREVIOUSLY REPORTED NMR STRUCTURE BY SAUDEK ET AL.
REMARK 900 RELATED ID: 2206 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS USED FOR THE NOESY ASSIGNMENT AND
REMARK 900 STRUCTURE CALCULATIONS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS INFORMED THAT RESIDUE 1 IS
REMARK 999 GLU AND NOT GLN, AS IN THE SWS SEQUENCE.
DBREF 1RO3 A 1 49 UNP P17347 DISI_ECHCA 1 49
SEQADV 1RO3 GLU A 1 UNP P17347 GLN 1 SEE REMARK 999
SEQRES 1 A 49 GLU CYS GLU SER GLY PRO CYS CYS ARG ASN CYS LYS PHE
SEQRES 2 A 49 LEU LYS GLU GLY THR ILE CYS LYS ARG ALA ARG GLY ASP
SEQRES 3 A 49 ASP MET ASP ASP TYR CYS ASN GLY LYS THR CYS ASP CYS
SEQRES 4 A 49 PRO ARG ASN PRO HIS LYS GLY PRO ALA THR
SSBOND 1 CYS A 2 CYS A 11 1555 1555 2.10
SSBOND 2 CYS A 7 CYS A 32 1555 1555 2.09
SSBOND 3 CYS A 8 CYS A 37 1555 1555 1.75
SSBOND 4 CYS A 20 CYS A 39 1555 1555 2.10
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