Header list of 2ech.pdb file
Complete list - 29 20 Bytes
HEADER BLOOD COAGULATION INHIBITOR 13-APR-93 2ECH
TITLE ECHISTATIN-THE REFINED STRUCTURE OF A DISINTEGRIN IN SOLUTION BY 1H
TITLE 2 NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECHISTATIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECHIS CARINATUS;
SOURCE 3 ORGANISM_COMMON: SAW-SCALED VIPER;
SOURCE 4 ORGANISM_TAXID: 40353
KEYWDS BLOOD COAGULATION INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR J.T.PELTON,R.A.ATKINSON,V.SAUDEK
REVDAT 3 29-NOV-17 2ECH 1 REMARK HELIX
REVDAT 2 24-FEB-09 2ECH 1 VERSN
REVDAT 1 31-OCT-93 2ECH 0
JRNL AUTH R.A.ATKINSON,V.SAUDEK,J.T.PELTON
JRNL TITL ECHISTATIN: THE REFINED STRUCTURE OF A DISINTEGRIN IN
JRNL TITL 2 SOLUTION BY 1H NMR AND RESTRAINED MOLECULAR DYNAMICS.
JRNL REF INT.J.PEPT.PROTEIN RES. V. 43 563 1994
JRNL REFN ISSN 0367-8377
JRNL PMID 7928087
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.SAUDEK,R.A.ATKINSON,P.LEPAGE,J.T.PELTON
REMARK 1 TITL THE SECONDARY STRUCTURE OF ECHISTATIN FROM 1H-NMR,
REMARK 1 TITL 2 CIRCULAR-DICHROISM AND RAMAN SPECTROSCOPY
REMARK 1 REF EUR.J.BIOCHEM. V. 202 329 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.SAUDEK,R.A.ATKINSON,J.T.PELTON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ECHISTATIN, THE SMALLEST
REMARK 1 TITL 2 ACTIVE RGD PROTEIN
REMARK 1 REF BIOCHEMISTRY V. 30 7369 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ECH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178023.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 2 PRO A 6 C - N - CA ANGL. DEV. = 11.0 DEGREES
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 PRO A 6 14.61 -57.11
REMARK 500 1 CYS A 7 -6.21 -58.64
REMARK 500 1 ARG A 9 -84.23 -77.67
REMARK 500 1 CYS A 11 -26.98 -150.78
REMARK 500 1 GLU A 16 91.26 0.16
REMARK 500 1 ASP A 29 -169.11 68.80
REMARK 500 1 ASP A 30 75.60 -156.44
REMARK 500 1 ASP A 38 40.19 -98.50
REMARK 500 1 PRO A 43 -80.59 -50.47
REMARK 500 1 HIS A 44 54.76 33.27
REMARK 500 2 PRO A 6 73.48 -28.58
REMARK 500 2 CYS A 7 -61.24 -171.28
REMARK 500 2 ARG A 9 -73.18 -22.35
REMARK 500 2 CYS A 11 -35.97 174.47
REMARK 500 2 PHE A 13 109.01 -52.47
REMARK 500 2 LEU A 14 -163.54 -73.80
REMARK 500 2 GLU A 16 113.33 0.10
REMARK 500 2 LYS A 21 -151.60 -146.93
REMARK 500 2 ARG A 22 -68.37 82.11
REMARK 500 2 ASP A 26 -86.17 -136.17
REMARK 500 2 ASP A 27 -124.64 -86.87
REMARK 500 2 ASP A 29 -165.75 -120.22
REMARK 500 2 CYS A 39 67.22 19.42
REMARK 500 3 ARG A 9 -72.85 -21.06
REMARK 500 3 CYS A 11 -43.33 152.28
REMARK 500 3 PHE A 13 107.00 -42.14
REMARK 500 3 LEU A 14 -157.67 -70.75
REMARK 500 3 LYS A 15 80.99 -69.81
REMARK 500 3 GLU A 16 111.96 -23.26
REMARK 500 3 ALA A 23 173.09 59.84
REMARK 500 3 ASP A 29 142.14 90.66
REMARK 500 3 ASP A 30 87.25 -158.79
REMARK 500 3 ASP A 38 49.15 -85.14
REMARK 500 3 CYS A 39 58.90 34.12
REMARK 500 3 PRO A 43 98.92 -60.02
REMARK 500 4 CYS A 7 17.77 -68.82
REMARK 500 4 ARG A 9 95.56 -65.10
REMARK 500 4 ASN A 10 64.85 25.62
REMARK 500 4 CYS A 11 -32.20 105.19
REMARK 500 4 PHE A 13 115.73 -21.61
REMARK 500 4 LYS A 15 41.25 -86.56
REMARK 500 4 GLU A 16 78.13 35.15
REMARK 500 4 LYS A 21 -104.97 -72.11
REMARK 500 4 ARG A 22 -52.72 -169.12
REMARK 500 4 ALA A 23 111.44 -36.42
REMARK 500 4 ASP A 26 -83.71 -71.48
REMARK 500 4 ASP A 27 59.27 -113.17
REMARK 500 4 MET A 28 -51.57 -122.08
REMARK 500 4 ASP A 30 96.38 -164.00
REMARK 500 4 ASP A 38 61.59 -109.57
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
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 PRO A 6 CYS A 7 1 132.51
REMARK 500 CYS A 7 CYS A 8 2 145.60
REMARK 500 MET A 28 ASP A 29 2 -147.60
REMARK 500 CYS A 32 ASN A 33 3 -149.33
REMARK 500 CYS A 8 ARG A 9 4 -149.18
REMARK 500 ASP A 29 ASP A 30 5 -144.91
REMARK 500 CYS A 8 ARG A 9 7 -149.46
REMARK 500 CYS A 8 ARG A 9 8 -130.26
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 4 HIS A 44 0.08 SIDE CHAIN
REMARK 500 5 HIS A 44 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RGD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 50
DBREF 2ECH A 1 49 UNP P17347 DISI_ECHCA 1 49
SEQRES 1 A 50 GLU CYS GLU SER GLY PRO CYS CYS ARG ASN CYS LYS PHE
SEQRES 2 A 50 LEU LYS GLU GLY THR ILE CYS LYS ARG ALA ARG GLY ASP
SEQRES 3 A 50 ASP MET ASP ASP TYR CYS ASN GLY LYS THR CYS ASP CYS
SEQRES 4 A 50 PRO ARG ASN PRO HIS LYS GLY PRO ALA THR NH2
HET NH2 A 50 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SHEET 1 A 2 THR A 18 ILE A 19 0
SHEET 2 A 2 TYR A 31 CYS A 32 -1 N CYS A 32 O THR A 18
SSBOND 1 CYS A 2 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 7 CYS A 32 1555 1555 2.01
SSBOND 3 CYS A 8 CYS A 37 1555 1555 2.03
SSBOND 4 CYS A 20 CYS A 39 1555 1555 2.04
LINK C THR A 49 N NH2 A 50 1555 1555 1.34
SITE 1 RGD 3 ARG A 24 GLY A 25 ASP A 26
SITE 1 AC1 1 THR A 49
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 - 29 20 Bytes