Header list of 1nbl.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 03-DEC-02 1NBL
TITLE NMR STRUCTURE OF HELLETHIONIN D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HELLETHIONIN D;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELLEBORUS PURPURASCENS;
SOURCE 3 ORGANISM_TAXID: 171899
KEYWDS GAMMA THIONINS HELLEBORUS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.G.MILBRADT,F.KEREK,L.MORODER,C.RENNER
REVDAT 3 23-FEB-22 1NBL 1 REMARK
REVDAT 2 24-FEB-09 1NBL 1 VERSN
REVDAT 1 11-MAR-03 1NBL 0
JRNL AUTH A.G.MILBRADT,F.KEREK,L.MORODER,C.RENNER
JRNL TITL STRUCTURAL CHARACTERIZATION OF HELLETHIONINS FROM HELLEBORUS
JRNL TITL 2 PURPURASCENS
JRNL REF BIOCHEMISTRY V. 42 2404 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12600207
JRNL DOI 10.1021/BI020628H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, DISCOVER 2.98
REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE IS BASED ON 577 NOE-DERIVED
REMARK 3 CONSTRAINTS AND 17 DISTANCE CONSTRAINTS FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1NBL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017744.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 283; 303
REMARK 210 PH : 2.5; 2.5; 2.5
REMARK 210 IONIC STRENGTH : PH 2.5; PH 2.5; PH 2.5
REMARK 210 PRESSURE : 1 BAR; 1 BAR; 1 BAR
REMARK 210 SAMPLE CONTENTS : 4MM HELLETHIONIN D; WATER PH
REMARK 210 2.5; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ; 400 MHZ; 600
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, SPARKY 3.98, DGII,
REMARK 210 DISCOVER 2.98
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 1 SER A 46 C SER A 46 OXT 0.135
REMARK 500 2 SER A 46 C SER A 46 OXT 0.133
REMARK 500 3 SER A 46 C SER A 46 OXT 0.135
REMARK 500 4 SER A 46 C SER A 46 OXT 0.134
REMARK 500 5 SER A 46 C SER A 46 OXT 0.134
REMARK 500 6 SER A 46 C SER A 46 OXT 0.136
REMARK 500 7 SER A 46 C SER A 46 OXT 0.134
REMARK 500 8 SER A 46 C SER A 46 OXT 0.134
REMARK 500 9 SER A 46 C SER A 46 OXT 0.135
REMARK 500 10 SER A 46 C SER A 46 OXT 0.134
REMARK 500 11 SER A 46 C SER A 46 OXT 0.134
REMARK 500 12 SER A 46 C SER A 46 OXT 0.135
REMARK 500 13 SER A 46 C SER A 46 OXT 0.136
REMARK 500 14 SER A 46 C SER A 46 OXT 0.135
REMARK 500 15 SER A 46 C SER A 46 OXT 0.137
REMARK 500 16 SER A 46 C SER A 46 OXT 0.135
REMARK 500 17 SER A 46 C SER A 46 OXT 0.135
REMARK 500 18 SER A 46 C SER A 46 OXT 0.135
REMARK 500 19 SER A 46 C SER A 46 OXT 0.137
REMARK 500 20 SER A 46 C SER A 46 OXT 0.134
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 6 VAL A 35 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 13 CYS A 32 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 15 CYS A 32 CA - CB - SG ANGL. DEV. = 7.1 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 THR A 37 -177.24 -65.25
REMARK 500 2 THR A 36 55.15 -111.43
REMARK 500 2 THR A 37 -174.37 -63.35
REMARK 500 3 ILE A 33 -156.19 -101.61
REMARK 500 3 THR A 36 50.72 -109.11
REMARK 500 5 THR A 19 -178.93 -65.10
REMARK 500 5 SER A 22 -140.00 -62.04
REMARK 500 5 ILE A 33 -162.39 -123.21
REMARK 500 7 ILE A 28 -61.43 -92.00
REMARK 500 8 SER A 22 170.29 -59.64
REMARK 500 8 ILE A 28 -60.71 -94.24
REMARK 500 8 THR A 36 50.53 -109.92
REMARK 500 9 SER A 22 -134.69 -68.11
REMARK 500 9 ILE A 33 -163.91 -127.17
REMARK 500 9 THR A 37 -179.97 -66.53
REMARK 500 10 THR A 19 0.70 -64.03
REMARK 500 10 ILE A 33 -159.51 -118.44
REMARK 500 10 THR A 37 -179.53 -67.21
REMARK 500 11 ILE A 28 -61.01 -91.70
REMARK 500 11 ILE A 33 -160.46 -118.27
REMARK 500 12 THR A 37 -178.67 -65.97
REMARK 500 13 THR A 19 1.28 -63.16
REMARK 500 13 THR A 36 50.10 -117.70
REMARK 500 13 THR A 37 -179.16 -65.89
REMARK 500 14 THR A 36 50.14 -111.80
REMARK 500 15 THR A 19 0.51 -63.50
REMARK 500 15 THR A 37 -177.73 -66.67
REMARK 500 16 SER A 22 171.43 -58.86
REMARK 500 16 THR A 36 50.81 -108.55
REMARK 500 17 THR A 19 2.38 -63.99
REMARK 500 17 ILE A 28 -61.98 -91.59
REMARK 500 17 ILE A 33 -159.08 -114.73
REMARK 500 18 THR A 39 -153.03 -125.53
REMARK 500 19 ILE A 33 -164.10 -128.64
REMARK 500 19 THR A 37 -176.23 -66.06
REMARK 500 20 THR A 19 -179.04 -64.08
REMARK 500 20 ILE A 33 -158.15 -113.80
REMARK 500 20 THR A 37 152.96 59.06
REMARK 500 20 THR A 39 -179.60 -175.39
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 VAL A 35 THR A 36 1 148.22
REMARK 500 VAL A 35 THR A 36 2 145.28
REMARK 500 THR A 37 THR A 38 2 140.95
REMARK 500 VAL A 35 THR A 36 3 145.65
REMARK 500 VAL A 35 THR A 36 4 145.43
REMARK 500 VAL A 35 THR A 36 5 145.82
REMARK 500 VAL A 35 THR A 36 6 147.25
REMARK 500 VAL A 35 THR A 36 7 146.31
REMARK 500 VAL A 35 THR A 36 8 146.12
REMARK 500 VAL A 35 THR A 36 9 147.10
REMARK 500 THR A 37 THR A 38 9 148.69
REMARK 500 VAL A 35 THR A 36 10 148.40
REMARK 500 THR A 37 THR A 38 10 145.50
REMARK 500 VAL A 35 THR A 36 11 145.79
REMARK 500 VAL A 35 THR A 36 12 148.76
REMARK 500 THR A 37 THR A 38 12 144.26
REMARK 500 VAL A 35 THR A 36 13 147.36
REMARK 500 THR A 37 THR A 38 13 146.85
REMARK 500 VAL A 35 THR A 36 14 146.76
REMARK 500 VAL A 35 THR A 36 15 147.25
REMARK 500 VAL A 35 THR A 36 16 145.41
REMARK 500 VAL A 35 THR A 36 17 145.74
REMARK 500 VAL A 35 THR A 36 18 147.00
REMARK 500 VAL A 35 THR A 36 19 147.75
REMARK 500 THR A 37 THR A 38 19 148.01
REMARK 500 THR A 37 THR A 38 20 132.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE WAS NO SUITABLE SEQUENCE DATABASE REFERENCE
REMARK 999 AT THE TIME OF PROCESSING.
DBREF 1NBL A 1 46 PDB 1NBL 1NBL 1 46
SEQRES 1 A 46 LYS SER CYS CYS ARG ASN THR LEU ALA ARG ASN CYS TYR
SEQRES 2 A 46 ASN ALA CYS ARG PHE THR GLY GLY SER GLN PRO THR CYS
SEQRES 3 A 46 GLY ILE LEU CYS ASP CYS ILE HIS VAL THR THR THR THR
SEQRES 4 A 46 CYS PRO SER SER HIS PRO SER
HELIX 1 1 ASN A 6 THR A 19 1 14
HELIX 2 2 SER A 22 CYS A 30 1 9
SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.05
SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.05
SSBOND 3 CYS A 12 CYS A 30 1555 1555 2.05
SSBOND 4 CYS A 16 CYS A 26 1555 1555 2.04
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 - b 23 2 Bytes