Header list of 1nxn.pdb file
Complete list - 24 20 Bytes
HEADER TOXIN 11-FEB-03 1NXN
TITLE SOLUTION STRUCTURE OF CONTRYPHAN-VN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONTRYPHAN-VN, MAJOR FORM (CIS CONFORMER);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 6 OF THE PEPTIDE IS NATURALLY FOUND IN THE VENOM DUCT OF CONUS
SOURCE 7 VENTRICOSUS (MARINE CONE SNAIL).
KEYWDS D-TRYPTOPHAN, CYCLIC PEPTIDE, DISULFIDE BRIDGE, CIS-TRANS ISOMERISM,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.ELISEO,D.O.CICERO,F.POLTICELLI,M.E.SCHININA,G.R.MASSILIA,M.PACI,
AUTHOR 2 P.ASCENZI
REVDAT 4 24-JUN-20 1NXN 1 SOURCE REMARK DBREF LINK
REVDAT 3 24-FEB-09 1NXN 1 VERSN
REVDAT 2 11-JAN-05 1NXN 1 JRNL
REVDAT 1 04-MAR-03 1NXN 0
SPRSDE 04-MAR-03 1NXN 1N3V
JRNL AUTH T.ELISEO,D.O.CICERO,C.ROMEO,M.E.SCHININA,G.R.MASSILIA,
JRNL AUTH 2 F.POLTICELLI,P.ASCENZI,M.PACI
JRNL TITL SOLUTION STRUCTURE OF THE CYCLIC PEPTIDE CONTRYPHAN-VN, A
JRNL TITL 2 CA2+-DEPENDENT K+ CHANNEL MODULATOR
JRNL REF BIOPOLYMERS V. 74 189 2004
JRNL REFN ISSN 0006-3525
JRNL PMID 15150794
JRNL DOI 10.1002/BIP.20025
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, XPLOR 1.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NXN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018323.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5 MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D ROESY; COSY; 1H-
REMARK 210 15N HSQC; 1H-13C HMQC; 1H-13C
REMARK 210 HSQC-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, XPLOR 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : FEWEST RESTRAINTS VIOLATIONS,
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HETERONUCLEAR EXPERIMENTS WERE PERFORMED AT NATURAL
REMARK 210 ABUNDANCE
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 C DTR A 5 H LYS A 6 1.38
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 GLY A 1 C ASP A 2 N 0.142
REMARK 500 1 ASP A 2 N ASP A 2 CA -0.353
REMARK 500 1 ASP A 2 CA ASP A 2 CB -0.437
REMARK 500 1 CYS A 3 CB CYS A 3 SG -0.255
REMARK 500 1 DTR A 5 C DTR A 5 O -0.347
REMARK 500 1 DTR A 5 C LYS A 6 N -0.277
REMARK 500 1 LYS A 6 CG LYS A 6 CD -0.591
REMARK 500 1 LYS A 6 CD LYS A 6 CE -0.253
REMARK 500 1 LYS A 6 CE LYS A 6 NZ -0.459
REMARK 500 1 PRO A 7 CD PRO A 7 N -0.117
REMARK 500 1 TRP A 8 NE1 TRP A 8 CE2 -0.089
REMARK 500 1 TRP A 8 C TRP A 8 O -0.177
REMARK 500 1 TRP A 8 C CYS A 9 N -0.177
REMARK 500 1 CYS A 9 CA CYS A 9 CB -0.533
REMARK 500 1 CYS A 9 CB CYS A 9 SG -0.283
REMARK 500 1 CYS A 9 C NH2 A 10 N 0.143
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 ASP A 2 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 1 DTR A 5 CA - C - N ANGL. DEV. = 13.8 DEGREES
REMARK 500 1 DTR A 5 O - C - N ANGL. DEV. = -19.8 DEGREES
REMARK 500 1 LYS A 6 CB - CG - CD ANGL. DEV. = 55.9 DEGREES
REMARK 500 1 LYS A 6 CG - CD - CE ANGL. DEV. = 62.9 DEGREES
REMARK 500 1 LYS A 6 CD - CE - NZ ANGL. DEV. = 25.0 DEGREES
REMARK 500 1 CYS A 9 N - CA - CB ANGL. DEV. = 18.1 DEGREES
REMARK 500 1 CYS A 9 CA - CB - SG ANGL. DEV. = 17.2 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 2 PRO A 4 -159.84 -86.71
REMARK 500 3 PRO A 4 -163.84 -79.85
REMARK 500 4 ASP A 2 83.60 -162.76
REMARK 500 4 PRO A 4 -163.83 -76.05
REMARK 500 6 ASP A 2 41.94 -162.82
REMARK 500 6 PRO A 4 -167.05 -74.28
REMARK 500 6 LYS A 6 136.44 62.03
REMARK 500 7 ASP A 2 71.50 -162.50
REMARK 500 8 ASP A 2 -64.62 -162.69
REMARK 500 8 PRO A 4 -163.29 -78.49
REMARK 500 10 ASP A 2 -40.67 -163.07
REMARK 500 10 PRO A 4 -162.90 -75.02
REMARK 500 11 ASP A 2 88.49 -162.90
REMARK 500 13 ASP A 2 -71.66 -162.63
REMARK 500 13 PRO A 4 -164.78 -77.12
REMARK 500 14 ASP A 2 40.63 -162.75
REMARK 500 14 PRO A 4 -164.52 -74.61
REMARK 500 14 LYS A 6 119.87 58.99
REMARK 500 16 PRO A 4 -163.00 -75.99
REMARK 500 17 ASP A 2 25.26 25.46
REMARK 500 17 PRO A 4 -164.52 -74.71
REMARK 500 17 LYS A 6 142.62 62.62
REMARK 500 18 ASP A 2 28.46 -162.41
REMARK 500 18 PRO A 4 -160.73 -77.90
REMARK 500 18 TRP A 8 31.79 -92.38
REMARK 500 19 PRO A 4 -163.46 -79.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 10
DBREF 1NXN A 1 10 PDB 1NXN 1NXN 1 10
SEQRES 1 A 10 GLY ASP CYS PRO DTR LYS PRO TRP CYS NH2
MODRES 1NXN DTR A 5 TRP D-TRYPTOPHAN
HET DTR A 5 24
HET NH2 A 10 3
HETNAM DTR D-TRYPTOPHAN
HETNAM NH2 AMINO GROUP
FORMUL 1 DTR C11 H12 N2 O2
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 3 CYS A 9 1555 1555 1.25
LINK C PRO A 4 N DTR A 5 1555 1555 1.29
LINK C DTR A 5 N LYS A 6 1555 1555 1.06
LINK O DTR A 5 N LYS A 6 1555 1555 1.52
LINK C CYS A 9 N NH2 A 10 1555 1555 1.48
CISPEP 1 CYS A 3 PRO A 4 1 -0.43
CISPEP 2 CYS A 3 PRO A 4 2 -0.39
CISPEP 3 CYS A 3 PRO A 4 3 -0.34
CISPEP 4 CYS A 3 PRO A 4 4 -0.22
CISPEP 5 CYS A 3 PRO A 4 5 -0.59
CISPEP 6 CYS A 3 PRO A 4 6 -0.08
CISPEP 7 CYS A 3 PRO A 4 7 -0.26
CISPEP 8 CYS A 3 PRO A 4 8 -0.13
CISPEP 9 CYS A 3 PRO A 4 9 -0.25
CISPEP 10 CYS A 3 PRO A 4 10 0.01
CISPEP 11 CYS A 3 PRO A 4 11 -0.76
CISPEP 12 CYS A 3 PRO A 4 12 -1.12
CISPEP 13 CYS A 3 PRO A 4 13 -0.09
CISPEP 14 CYS A 3 PRO A 4 14 0.06
CISPEP 15 CYS A 3 PRO A 4 15 -0.31
CISPEP 16 CYS A 3 PRO A 4 16 -0.10
CISPEP 17 CYS A 3 PRO A 4 17 0.08
CISPEP 18 CYS A 3 PRO A 4 18 -0.17
CISPEP 19 CYS A 3 PRO A 4 19 -0.32
CISPEP 20 CYS A 3 PRO A 4 20 -0.48
SITE 1 AC1 2 TRP A 8 CYS A 9
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 - 24 20 Bytes