Header list of 2bds.pdb file
Complete list - v 29 2 Bytes
HEADER ANTI-HYPERTENSIVE, ANTI-VIRAL PROTEIN 14-NOV-88 2BDS
TITLE DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE
TITLE 2 ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE
TITLE 3 ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID
TITLE 4 DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BDS-I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANEMONIA SULCATA;
SOURCE 3 ORGANISM_COMMON: SNAKE-LOCKS SEA ANEMONE;
SOURCE 4 ORGANISM_TAXID: 6108
KEYWDS ANTI-HYPERTENSIVE, ANTI-VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 42
AUTHOR G.M.CLORE,P.C.DRISCOLL,A.M.GRONENBORN
REVDAT 7 29-NOV-17 2BDS 1 REMARK HELIX
REVDAT 6 24-FEB-09 2BDS 1 VERSN
REVDAT 5 01-APR-03 2BDS 1 JRNL
REVDAT 4 15-APR-92 2BDS 1 EXPDTA
REVDAT 3 15-OCT-89 2BDS 1 AUTHOR EXPDTA
REVDAT 2 12-JUL-89 2BDS 1 REVDAT REMARK
REVDAT 1 19-APR-89 2BDS 0
JRNL AUTH P.C.DRISCOLL,A.M.GRONENBORN,L.BERESS,G.M.CLORE
JRNL TITL DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE
JRNL TITL 3 SEA ANEMONE ANEMONIA SULCATA: A STUDY USING NUCLEAR MAGNETIC
JRNL TITL 4 RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED
JRNL TITL 5 ANNEALING.
JRNL REF BIOCHEMISTRY V. 28 2188 1989
JRNL REFN ISSN 0006-2960
JRNL PMID 2566326
JRNL DOI 10.1021/BI00431A033
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.C.DRISCOLL,G.M.CLORE,L.BERESS,A.M.GRONENBORN
REMARK 1 TITL A PROTON NUCLEAR MAGNETIC RESONANCE STUDY OF THE
REMARK 1 TITL 2 ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA
REMARK 1 TITL 3 ANEMONE ANEMONIA SULCATA. SEQUENTIAL AND STEREOSPECIFIC
REMARK 1 TITL 4 RESONANCE ASSIGNMENT AND SECONDARY STRUCTURE
REMARK 1 REF BIOCHEMISTRY V. 28 2178 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.C.DRISCOLL,A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL THE INFLUENCE OF STEREOSPECIFIC ASSIGNMENTS ON THE
REMARK 1 TITL 2 DETERMINATION OF THREE-DIMENSIONAL STRUCTURES OF PROTEINS BY
REMARK 1 TITL 3 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY. APPLICATION TO THE
REMARK 1 TITL 4 SEA ANEMONE PROTEIN BDS-I
REMARK 1 REF FEBS LETT. V. 243 223 1989
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BDS 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_1000177825.
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 : 42
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: 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 H1 ALA A 1 HH22 ARG A 12 1.26
REMARK 500
REMARK 500 REMARK: NULL
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 1 TRP A 16 CG TRP A 16 CD2 -0.130
REMARK 500 1 TRP A 35 CG TRP A 35 CD2 -0.115
REMARK 500 1 HIS A 43 CG HIS A 43 ND1 -0.121
REMARK 500 2 TRP A 16 CG TRP A 16 CD2 -0.130
REMARK 500 2 TRP A 35 CG TRP A 35 CD2 -0.113
REMARK 500 2 HIS A 43 CG HIS A 43 ND1 -0.119
REMARK 500 3 TRP A 16 CG TRP A 16 CD2 -0.131
REMARK 500 3 TRP A 35 CG TRP A 35 CD2 -0.112
REMARK 500 3 HIS A 43 CG HIS A 43 ND1 -0.127
REMARK 500 4 TRP A 16 CG TRP A 16 CD2 -0.134
REMARK 500 4 TRP A 35 CG TRP A 35 CD2 -0.120
REMARK 500 4 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 5 TRP A 16 CG TRP A 16 CD2 -0.134
REMARK 500 5 TRP A 35 CG TRP A 35 CD2 -0.114
REMARK 500 5 HIS A 43 CG HIS A 43 ND1 -0.128
REMARK 500 6 TRP A 16 CG TRP A 16 CD2 -0.132
REMARK 500 6 TRP A 35 CG TRP A 35 CD2 -0.114
REMARK 500 6 HIS A 43 CG HIS A 43 ND1 -0.123
REMARK 500 7 TRP A 16 CG TRP A 16 CD2 -0.134
REMARK 500 7 TRP A 35 CG TRP A 35 CD2 -0.117
REMARK 500 7 HIS A 43 CG HIS A 43 ND1 -0.122
REMARK 500 8 TRP A 16 CG TRP A 16 CD2 -0.130
REMARK 500 8 TRP A 35 CG TRP A 35 CD2 -0.112
REMARK 500 8 HIS A 43 CG HIS A 43 ND1 -0.125
REMARK 500 9 TRP A 16 CG TRP A 16 CD2 -0.131
REMARK 500 9 TRP A 35 CG TRP A 35 CD2 -0.131
REMARK 500 9 TRP A 35 CG TRP A 35 CD1 -0.086
REMARK 500 9 HIS A 43 CG HIS A 43 ND1 -0.123
REMARK 500 10 TRP A 16 CG TRP A 16 CD2 -0.132
REMARK 500 10 TRP A 35 CG TRP A 35 CD2 -0.124
REMARK 500 10 HIS A 43 CG HIS A 43 ND1 -0.124
REMARK 500 11 TRP A 16 CG TRP A 16 CD2 -0.133
REMARK 500 11 TRP A 35 CG TRP A 35 CD2 -0.112
REMARK 500 11 HIS A 43 CG HIS A 43 ND1 -0.123
REMARK 500 12 TRP A 16 CG TRP A 16 CD2 -0.132
REMARK 500 12 TRP A 35 CG TRP A 35 CD2 -0.117
REMARK 500 12 HIS A 43 CG HIS A 43 ND1 -0.123
REMARK 500 13 TRP A 16 CG TRP A 16 CD2 -0.131
REMARK 500 13 TRP A 35 CG TRP A 35 CD2 -0.112
REMARK 500 13 HIS A 43 CG HIS A 43 ND1 -0.121
REMARK 500 14 TRP A 16 CG TRP A 16 CD2 -0.134
REMARK 500 14 TRP A 35 CG TRP A 35 CD2 -0.114
REMARK 500 14 HIS A 43 CG HIS A 43 ND1 -0.118
REMARK 500 15 TRP A 16 CG TRP A 16 CD2 -0.133
REMARK 500 15 TRP A 35 CG TRP A 35 CD2 -0.113
REMARK 500 15 HIS A 43 CG HIS A 43 ND1 -0.121
REMARK 500 16 TRP A 16 CG TRP A 16 CD2 -0.132
REMARK 500 16 TRP A 35 CG TRP A 35 CD2 -0.111
REMARK 500 16 HIS A 43 CG HIS A 43 ND1 -0.122
REMARK 500 17 TRP A 16 CG TRP A 16 CD2 -0.137
REMARK 500
REMARK 500 THIS ENTRY HAS 131 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 1 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 1 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 1 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 35 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 35 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 1 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 2 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 2 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 2 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TRP A 35 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 3 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 GLY A 25 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 3 TRP A 35 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 TRP A 35 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 4 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 4 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 4 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 4 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 35 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 4 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 4 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 5 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 5 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 5 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 35 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 35 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 5 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 6 GLY A 11 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 6 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 6 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 6 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 6 TRP A 16 CG - CD2 - CE3 ANGL. DEV. = -6.3 DEGREES
REMARK 500 6 TRP A 35 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 6 TRP A 35 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 6 TRP A 35 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 7 TRP A 16 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 7 TRP A 16 NE1 - CE2 - CZ2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 7 TRP A 16 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 347 ANGLE DEVIATIONS.
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 3 39.01 -78.95
REMARK 500 1 ILE A 17 -161.18 -104.32
REMARK 500 1 LEU A 18 70.89 -67.99
REMARK 500 1 PRO A 23 106.12 -56.69
REMARK 500 1 THR A 29 -46.05 -162.59
REMARK 500 1 TRP A 35 158.94 -44.81
REMARK 500 1 PRO A 36 35.25 -78.89
REMARK 500 2 PRO A 3 35.28 -77.96
REMARK 500 2 PRO A 10 -161.58 -73.09
REMARK 500 2 LEU A 18 67.36 -68.22
REMARK 500 2 TYR A 26 -75.97 -79.52
REMARK 500 2 THR A 29 -44.41 -161.93
REMARK 500 2 TRP A 35 156.02 -41.45
REMARK 500 2 PRO A 36 28.71 -78.56
REMARK 500 3 PRO A 3 40.63 -91.22
REMARK 500 3 PRO A 10 -167.70 -72.41
REMARK 500 3 ILE A 17 -162.39 -100.14
REMARK 500 3 LEU A 18 70.02 -68.87
REMARK 500 3 THR A 29 -43.00 -162.02
REMARK 500 3 TRP A 35 159.23 -46.47
REMARK 500 3 PRO A 36 28.23 -78.51
REMARK 500 4 CYS A 6 -162.66 -124.41
REMARK 500 4 PRO A 10 -166.19 -73.69
REMARK 500 4 ILE A 17 -158.32 -85.55
REMARK 500 4 LEU A 18 72.54 -67.67
REMARK 500 4 THR A 29 -43.00 -163.13
REMARK 500 4 TRP A 35 146.19 -38.82
REMARK 500 4 PRO A 36 38.44 -78.06
REMARK 500 5 PRO A 3 35.46 -86.26
REMARK 500 5 PRO A 10 -168.91 -74.87
REMARK 500 5 ILE A 17 -159.36 -90.61
REMARK 500 5 LEU A 18 73.87 -67.77
REMARK 500 5 PRO A 23 -164.98 -62.51
REMARK 500 5 TYR A 26 -70.71 -88.45
REMARK 500 5 THR A 29 -43.95 -161.42
REMARK 500 5 TRP A 35 155.35 -40.46
REMARK 500 5 PRO A 36 33.12 -78.45
REMARK 500 6 LEU A 18 59.63 -153.10
REMARK 500 6 THR A 29 -43.76 -162.32
REMARK 500 6 TRP A 35 153.57 -45.57
REMARK 500 7 ALA A 2 137.79 -39.12
REMARK 500 7 PRO A 3 36.09 -81.38
REMARK 500 7 PRO A 10 -166.34 -74.04
REMARK 500 7 LEU A 18 74.51 -151.89
REMARK 500 7 THR A 29 -44.07 -161.91
REMARK 500 7 LYS A 34 59.27 -142.27
REMARK 500 7 ASN A 37 -160.59 -101.23
REMARK 500 7 ILE A 38 141.22 171.34
REMARK 500 8 PRO A 3 38.55 -83.34
REMARK 500 8 PRO A 10 -164.21 -67.04
REMARK 500
REMARK 500 THIS ENTRY HAS 286 RAMACHANDRAN OUTLIERS.
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 12 0.29 SIDE CHAIN
REMARK 500 1 ARG A 19 0.20 SIDE CHAIN
REMARK 500 2 ARG A 12 0.30 SIDE CHAIN
REMARK 500 2 ARG A 19 0.21 SIDE CHAIN
REMARK 500 3 ARG A 12 0.28 SIDE CHAIN
REMARK 500 3 ARG A 19 0.15 SIDE CHAIN
REMARK 500 4 ARG A 12 0.19 SIDE CHAIN
REMARK 500 4 ARG A 19 0.21 SIDE CHAIN
REMARK 500 5 ARG A 12 0.08 SIDE CHAIN
REMARK 500 5 ARG A 19 0.32 SIDE CHAIN
REMARK 500 6 ARG A 19 0.32 SIDE CHAIN
REMARK 500 7 ARG A 12 0.15 SIDE CHAIN
REMARK 500 8 ARG A 12 0.28 SIDE CHAIN
REMARK 500 9 ARG A 12 0.23 SIDE CHAIN
REMARK 500 10 ARG A 12 0.14 SIDE CHAIN
REMARK 500 10 ARG A 19 0.17 SIDE CHAIN
REMARK 500 11 ARG A 12 0.24 SIDE CHAIN
REMARK 500 11 ARG A 19 0.26 SIDE CHAIN
REMARK 500 12 ARG A 12 0.24 SIDE CHAIN
REMARK 500 12 ARG A 19 0.25 SIDE CHAIN
REMARK 500 13 ARG A 12 0.24 SIDE CHAIN
REMARK 500 13 ARG A 19 0.32 SIDE CHAIN
REMARK 500 14 ARG A 12 0.30 SIDE CHAIN
REMARK 500 14 ARG A 19 0.14 SIDE CHAIN
REMARK 500 15 ARG A 12 0.30 SIDE CHAIN
REMARK 500 15 ARG A 19 0.13 SIDE CHAIN
REMARK 500 16 ARG A 12 0.30 SIDE CHAIN
REMARK 500 16 ARG A 19 0.29 SIDE CHAIN
REMARK 500 17 ARG A 12 0.29 SIDE CHAIN
REMARK 500 17 ARG A 19 0.20 SIDE CHAIN
REMARK 500 18 ARG A 12 0.32 SIDE CHAIN
REMARK 500 18 ARG A 19 0.27 SIDE CHAIN
REMARK 500 19 ARG A 12 0.24 SIDE CHAIN
REMARK 500 19 ARG A 19 0.32 SIDE CHAIN
REMARK 500 20 ARG A 12 0.15 SIDE CHAIN
REMARK 500 20 ARG A 19 0.32 SIDE CHAIN
REMARK 500 21 ARG A 12 0.31 SIDE CHAIN
REMARK 500 21 ARG A 19 0.23 SIDE CHAIN
REMARK 500 22 ARG A 12 0.20 SIDE CHAIN
REMARK 500 22 ARG A 19 0.13 SIDE CHAIN
REMARK 500 23 ARG A 12 0.31 SIDE CHAIN
REMARK 500 24 ARG A 12 0.31 SIDE CHAIN
REMARK 500 24 ARG A 19 0.31 SIDE CHAIN
REMARK 500 25 ARG A 12 0.13 SIDE CHAIN
REMARK 500 25 ARG A 19 0.09 SIDE CHAIN
REMARK 500 26 ARG A 12 0.24 SIDE CHAIN
REMARK 500 26 ARG A 19 0.30 SIDE CHAIN
REMARK 500 27 ARG A 12 0.30 SIDE CHAIN
REMARK 500 27 ARG A 19 0.32 SIDE CHAIN
REMARK 500 28 ARG A 12 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BDS RELATED DB: PDB
DBREF 2BDS A 1 43 UNP P11494 BDS1_ANESU 1 43
SEQRES 1 A 43 ALA ALA PRO CYS PHE CYS SER GLY LYS PRO GLY ARG GLY
SEQRES 2 A 43 ASP LEU TRP ILE LEU ARG GLY THR CYS PRO GLY GLY TYR
SEQRES 3 A 43 GLY TYR THR SER ASN CYS TYR LYS TRP PRO ASN ILE CYS
SEQRES 4 A 43 CYS TYR PRO HIS
SHEET 1 A 3 ASP A 14 ILE A 17 0
SHEET 2 A 3 ASN A 37 TYR A 41 -1
SHEET 3 A 3 SER A 30 LYS A 34 -1
SSBOND 1 CYS A 4 CYS A 39 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 32 1555 1555 2.01
SSBOND 3 CYS A 22 CYS A 40 1555 1555 2.02
CISPEP 1 TRP A 35 PRO A 36 1 -5.31
CISPEP 2 TYR A 41 PRO A 42 1 5.75
CISPEP 3 TRP A 35 PRO A 36 2 -3.32
CISPEP 4 TYR A 41 PRO A 42 2 3.89
CISPEP 5 TRP A 35 PRO A 36 3 -5.09
CISPEP 6 TYR A 41 PRO A 42 3 4.10
CISPEP 7 TRP A 35 PRO A 36 4 -5.26
CISPEP 8 TYR A 41 PRO A 42 4 5.49
CISPEP 9 TRP A 35 PRO A 36 5 -3.75
CISPEP 10 TYR A 41 PRO A 42 5 5.91
CISPEP 11 TRP A 35 PRO A 36 6 -5.10
CISPEP 12 TYR A 41 PRO A 42 6 3.03
CISPEP 13 TRP A 35 PRO A 36 7 -4.97
CISPEP 14 TYR A 41 PRO A 42 7 5.25
CISPEP 15 TRP A 35 PRO A 36 8 -6.55
CISPEP 16 TYR A 41 PRO A 42 8 -1.10
CISPEP 17 TRP A 35 PRO A 36 9 -5.71
CISPEP 18 TYR A 41 PRO A 42 9 6.31
CISPEP 19 TRP A 35 PRO A 36 10 -4.99
CISPEP 20 TYR A 41 PRO A 42 10 1.91
CISPEP 21 TRP A 35 PRO A 36 11 -2.89
CISPEP 22 TYR A 41 PRO A 42 11 5.83
CISPEP 23 TRP A 35 PRO A 36 12 -3.71
CISPEP 24 TYR A 41 PRO A 42 12 0.41
CISPEP 25 TRP A 35 PRO A 36 13 -1.60
CISPEP 26 TYR A 41 PRO A 42 13 0.64
CISPEP 27 TRP A 35 PRO A 36 14 -5.15
CISPEP 28 TYR A 41 PRO A 42 14 5.22
CISPEP 29 TRP A 35 PRO A 36 15 -5.75
CISPEP 30 TYR A 41 PRO A 42 15 4.89
CISPEP 31 TRP A 35 PRO A 36 16 -5.70
CISPEP 32 TYR A 41 PRO A 42 16 3.28
CISPEP 33 TRP A 35 PRO A 36 17 -5.27
CISPEP 34 TYR A 41 PRO A 42 17 6.17
CISPEP 35 TRP A 35 PRO A 36 18 -5.64
CISPEP 36 TYR A 41 PRO A 42 18 2.94
CISPEP 37 TRP A 35 PRO A 36 19 -1.35
CISPEP 38 TYR A 41 PRO A 42 19 5.93
CISPEP 39 TRP A 35 PRO A 36 20 -5.72
CISPEP 40 TYR A 41 PRO A 42 20 5.48
CISPEP 41 TRP A 35 PRO A 36 21 -2.71
CISPEP 42 TYR A 41 PRO A 42 21 2.50
CISPEP 43 TRP A 35 PRO A 36 22 -6.94
CISPEP 44 TYR A 41 PRO A 42 22 5.53
CISPEP 45 TRP A 35 PRO A 36 23 -5.30
CISPEP 46 TYR A 41 PRO A 42 23 5.74
CISPEP 47 TRP A 35 PRO A 36 24 -5.76
CISPEP 48 TYR A 41 PRO A 42 24 6.71
CISPEP 49 TRP A 35 PRO A 36 25 -5.32
CISPEP 50 TYR A 41 PRO A 42 25 6.32
CISPEP 51 TRP A 35 PRO A 36 26 -6.61
CISPEP 52 TYR A 41 PRO A 42 26 4.30
CISPEP 53 TRP A 35 PRO A 36 27 -3.53
CISPEP 54 TYR A 41 PRO A 42 27 4.66
CISPEP 55 TRP A 35 PRO A 36 28 -4.98
CISPEP 56 TYR A 41 PRO A 42 28 7.17
CISPEP 57 TRP A 35 PRO A 36 29 -5.94
CISPEP 58 TYR A 41 PRO A 42 29 6.20
CISPEP 59 TRP A 35 PRO A 36 30 -6.10
CISPEP 60 TYR A 41 PRO A 42 30 4.04
CISPEP 61 TRP A 35 PRO A 36 31 0.40
CISPEP 62 TYR A 41 PRO A 42 31 4.39
CISPEP 63 TRP A 35 PRO A 36 32 -4.51
CISPEP 64 TYR A 41 PRO A 42 32 4.82
CISPEP 65 TRP A 35 PRO A 36 33 -6.43
CISPEP 66 TYR A 41 PRO A 42 33 7.86
CISPEP 67 TRP A 35 PRO A 36 34 -5.52
CISPEP 68 TYR A 41 PRO A 42 34 4.25
CISPEP 69 TRP A 35 PRO A 36 35 -3.91
CISPEP 70 TYR A 41 PRO A 42 35 3.56
CISPEP 71 TRP A 35 PRO A 36 36 -5.56
CISPEP 72 TYR A 41 PRO A 42 36 6.07
CISPEP 73 TRP A 35 PRO A 36 37 -4.19
CISPEP 74 TYR A 41 PRO A 42 37 1.94
CISPEP 75 TRP A 35 PRO A 36 38 -4.66
CISPEP 76 TYR A 41 PRO A 42 38 5.33
CISPEP 77 TRP A 35 PRO A 36 39 -5.21
CISPEP 78 TYR A 41 PRO A 42 39 4.60
CISPEP 79 TRP A 35 PRO A 36 40 -3.73
CISPEP 80 TYR A 41 PRO A 42 40 3.96
CISPEP 81 TRP A 35 PRO A 36 41 -5.21
CISPEP 82 TYR A 41 PRO A 42 41 5.41
CISPEP 83 TRP A 35 PRO A 36 42 -5.32
CISPEP 84 TYR A 41 PRO A 42 42 5.98
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 - v 29 2 Bytes