Header list of 1p1p.pdb file
Complete list - 23 20 Bytes
HEADER NEUROTOXIN 06-DEC-96 1P1P
TITLE [PRO7,13] AA-CONOTOXIN PIVA, NMR, 12 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AA-CONOTOXIN PIVA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS PURPURASCENS;
SOURCE 3 ORGANISM_TAXID: 41690
KEYWDS NEUROTOXIN, CONOTOXIN, ACETYLCHOLINE RECEPTOR BINDING, TRANSCRIPTION
KEYWDS 2 REGULATION
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR K.-H.HAN,K.-J.HWANG,S.-M.KIM,S.-K.KIM,W.R.GRAY,B.M.OLIVERA,J.RIVIER,
AUTHOR 2 K.J.SHON
REVDAT 3 23-FEB-22 1P1P 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1P1P 1 VERSN
REVDAT 1 07-JUL-97 1P1P 0
JRNL AUTH K.H.HAN,K.J.HWANG,S.M.KIM,S.K.KIM,W.R.GRAY,B.M.OLIVERA,
JRNL AUTH 2 J.RIVIER,K.J.SHON
JRNL TITL NMR STRUCTURE DETERMINATION OF A NOVEL CONOTOXIN, [PRO 7,13]
JRNL TITL 2 ALPHA A-CONOTOXIN PIVA.
JRNL REF BIOCHEMISTRY V. 36 1669 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9048550
JRNL DOI 10.1021/BI962301K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII, DISCOVER DISCOVER
REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE TOTAL OF 324 NOE-DERIVED
REMARK 3 INTERPROTON DISTANCE RESTRAINTS INCLUDING 33 LONG-RANGE NOE
REMARK 3 RESTRAINTS AS WELL AS 11 PHI AND 7 CHI1 TORSION ANGLE RESTRAINTS
REMARK 3 WERE USED FOR STRUCTURE DETERMINATION. BACK CALCULATION OF
REMARK 3 EXPERIMENTAL NOE SPECTRUM YIELDED THE FINAL R-FACTORS OF RA=
REMARK 3 0.641 AND RB=0.157. THE FINAL RMSD VALUES ARE 0.90A AND 1.16A
REMARK 3 FOR THE BACKBONE AND THE HEAVY ATOMS, RESPECTIVELY. RESIDUES 12 -
REMARK 3 24 ARE EXTREMELY WELL-DEFINED WITH A BACKBONE RMSD OF 0.56 A
REMARK 3 WHEREAS THE N-TERMINAL 3 - 11 DISULFIDE LOOP IS FLEXIBLE
REMARK 3 POSSESSING A BACKBONE RMSD OF 1.09 A.
REMARK 4
REMARK 4 1P1P 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_1000175552.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 287
REMARK 210 PH : 3.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; P.E.COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR, FELIX, DGII, DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : RMSD
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 CYS A 14 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 4 CYS A 14 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 6 PRO A 13 C - N - CA ANGL. DEV. = 9.0 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 CYS A 2 -57.35 -146.75
REMARK 500 1 ASN A 8 11.45 -142.41
REMARK 500 1 CYS A 11 132.18 -20.27
REMARK 500 1 PRO A 13 45.51 -67.45
REMARK 500 1 CYS A 14 -53.42 -164.54
REMARK 500 2 CYS A 2 -88.51 -151.95
REMARK 500 2 ASN A 8 45.07 -77.14
REMARK 500 2 CYS A 11 87.66 -18.56
REMARK 500 2 PRO A 13 44.48 -68.03
REMARK 500 2 CYS A 14 -49.78 -152.10
REMARK 500 3 CYS A 2 -59.88 -150.83
REMARK 500 3 ALA A 10 53.76 -155.83
REMARK 500 3 PRO A 13 46.92 -64.83
REMARK 500 3 CYS A 14 -50.58 -165.39
REMARK 500 4 CYS A 2 -60.41 -145.54
REMARK 500 4 PRO A 7 102.77 -40.91
REMARK 500 4 ASN A 8 -104.90 -65.98
REMARK 500 4 ALA A 9 79.67 -19.29
REMARK 500 4 ALA A 10 -54.59 145.51
REMARK 500 4 PRO A 13 44.93 -68.05
REMARK 500 4 CYS A 14 -51.11 -150.55
REMARK 500 5 CYS A 2 -49.10 -156.60
REMARK 500 5 CYS A 3 30.71 -87.66
REMARK 500 5 PRO A 13 42.79 -68.40
REMARK 500 5 CYS A 14 -49.66 -167.19
REMARK 500 6 CYS A 2 -96.96 -142.56
REMARK 500 6 ALA A 10 47.12 -156.66
REMARK 500 6 PRO A 13 45.41 -68.39
REMARK 500 6 CYS A 14 -42.78 -166.64
REMARK 500 6 CYS A 23 48.42 -100.41
REMARK 500 7 CYS A 2 -69.84 -153.23
REMARK 500 7 ALA A 10 53.25 -154.34
REMARK 500 7 PRO A 13 49.84 -63.68
REMARK 500 7 CYS A 14 -44.34 -163.85
REMARK 500 8 CYS A 2 -58.93 -149.15
REMARK 500 8 SER A 5 40.06 -87.88
REMARK 500 8 PRO A 7 171.69 -53.83
REMARK 500 8 PRO A 13 46.34 -65.63
REMARK 500 8 CYS A 14 -43.39 -164.27
REMARK 500 8 ASP A 18 78.07 -105.34
REMARK 500 8 CYS A 23 59.47 -94.22
REMARK 500 9 CYS A 2 -48.55 -149.00
REMARK 500 9 PRO A 13 45.46 -67.03
REMARK 500 9 CYS A 14 -49.67 -166.40
REMARK 500 10 CYS A 2 -67.47 -154.28
REMARK 500 10 ASN A 8 49.17 -80.84
REMARK 500 10 ALA A 10 55.57 -152.31
REMARK 500 10 PRO A 13 51.60 -62.97
REMARK 500 10 CYS A 14 -48.61 -164.70
REMARK 500 11 CYS A 2 -58.71 -147.61
REMARK 500
REMARK 500 THIS ENTRY HAS 61 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 TYR A 22 0.12 SIDE CHAIN
REMARK 500 2 TYR A 22 0.13 SIDE CHAIN
REMARK 500 3 TYR A 22 0.08 SIDE CHAIN
REMARK 500 4 TYR A 22 0.13 SIDE CHAIN
REMARK 500 7 TYR A 22 0.07 SIDE CHAIN
REMARK 500 8 TYR A 22 0.09 SIDE CHAIN
REMARK 500 9 TYR A 22 0.09 SIDE CHAIN
REMARK 500 10 TYR A 22 0.10 SIDE CHAIN
REMARK 500 11 TYR A 22 0.09 SIDE CHAIN
REMARK 500 12 TYR A 22 0.09 SIDE CHAIN
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 26
DBREF 1P1P A 1 25 UNP P55963 CXA4_CONPU 1 25
SEQADV 1P1P HYP A 20 UNP P55963 PRO 20 CONFLICT
SEQRES 1 A 26 GLY CYS CYS GLY SER TYR PRO ASN ALA ALA CYS HIS PRO
SEQRES 2 A 26 CYS SER CYS LYS ASP ARG HYP SER TYR CYS GLY GLN NH2
MODRES 1P1P HYP A 20 PRO 4-HYDROXYPROLINE
HET HYP A 20 15
HET NH2 A 26 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP C5 H9 N O3
FORMUL 1 NH2 H2 N
HELIX 1 H1 SER A 21 GLY A 24 5 4
SSBOND 1 CYS A 2 CYS A 16 1555 1555 2.05
SSBOND 2 CYS A 3 CYS A 11 1555 1555 2.05
SSBOND 3 CYS A 14 CYS A 23 1555 1555 2.02
LINK C ARG A 19 N HYP A 20 1555 1555 1.34
LINK C HYP A 20 N SER A 21 1555 1555 1.33
LINK C GLN A 25 N NH2 A 26 1555 1555 1.33
SITE 1 AC1 2 SER A 21 GLN A 25
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 - 23 20 Bytes