Header list of 1hth.pdb file
Complete list - 3 20 Bytes
HEADER HORMONE 09-APR-97 1HTH
TITLE THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-
TITLE 2 34, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIC PARATHYROID HORMONE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-34;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN
KEYWDS HUMAN PARATHYROID HORMONE, CYCLIC, ORNITHINE, NORLEUCINE, HORMONE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.ROESCH,G.SEIDEL,W.SCHAEFER,A.ESSWEIN,E.HOFMANN
REVDAT 4 03-NOV-21 1HTH 1 SEQADV LINK
REVDAT 3 13-JUL-11 1HTH 1 VERSN
REVDAT 2 24-FEB-09 1HTH 1 VERSN
REVDAT 1 15-OCT-97 1HTH 0
JRNL AUTH M.WEIDLER,U.C.MARX,G.SEIDEL,W.SCHAEFER,E.HOFFMANN,A.ESSWEIN,
JRNL AUTH 2 P.ROESCH
JRNL TITL THE STRUCTURE OF HUMAN PARATHYROID HORMONE-RELATED
JRNL TITL 2 PROTEIN(1-34) IN NEAR-PHYSIOLOGICAL SOLUTION.
JRNL REF FEBS LETT. V. 444 239 1999
JRNL REFN ISSN 0014-5793
JRNL PMID 10050767
JRNL DOI 10.1016/S0014-5793(98)01658-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HTH 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_1000174014.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
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: 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 ILE A 5 32.51 -89.16
REMARK 500 1 ORN A 13 -53.62 -129.15
REMARK 500 1 HIS A 14 128.17 168.84
REMARK 500 1 NLE A 18 25.06 -145.47
REMARK 500 1 GLU A 19 -77.26 -83.72
REMARK 500 1 VAL A 31 96.35 37.18
REMARK 500 1 HIS A 32 87.23 -53.76
REMARK 500 2 ILE A 5 37.90 -91.16
REMARK 500 2 LEU A 11 -87.85 -85.00
REMARK 500 2 ORN A 13 121.98 61.18
REMARK 500 2 HIS A 14 -122.75 -127.95
REMARK 500 2 GLU A 22 -70.37 -70.84
REMARK 500 2 LYS A 26 -165.16 -76.96
REMARK 500 2 LYS A 27 -88.81 61.36
REMARK 500 2 GLN A 29 101.87 -46.01
REMARK 500 2 ASP A 30 -38.94 178.99
REMARK 500 2 VAL A 31 26.68 40.93
REMARK 500 2 HIS A 32 50.44 39.05
REMARK 500 2 ASN A 33 30.61 -92.56
REMARK 500 3 ORN A 13 40.90 32.49
REMARK 500 3 HIS A 14 127.09 74.44
REMARK 500 3 NLE A 18 30.89 -96.63
REMARK 500 3 LYS A 26 37.11 -80.11
REMARK 500 3 ASP A 30 53.14 -100.71
REMARK 500 4 SER A 3 40.31 -86.52
REMARK 500 4 GLN A 6 -50.70 -158.48
REMARK 500 4 ORN A 13 -4.40 77.68
REMARK 500 4 HIS A 14 134.77 72.40
REMARK 500 4 LEU A 28 -7.61 80.01
REMARK 500 4 HIS A 32 55.35 -161.41
REMARK 500 4 ASN A 33 -76.72 166.19
REMARK 500 5 VAL A 2 -177.95 53.04
REMARK 500 5 ILE A 5 32.27 -93.43
REMARK 500 5 HIS A 14 -97.29 -74.21
REMARK 500 5 LYS A 26 37.08 -98.46
REMARK 500 5 VAL A 31 87.51 172.47
REMARK 500 5 HIS A 32 38.44 -166.55
REMARK 500 5 ASN A 33 -77.82 -102.26
REMARK 500 6 VAL A 2 -169.89 -63.40
REMARK 500 6 ILE A 5 37.78 -91.00
REMARK 500 6 ORN A 13 -51.81 -127.91
REMARK 500 6 LYS A 26 44.94 -83.66
REMARK 500 6 LYS A 27 -47.46 -143.07
REMARK 500 6 VAL A 31 59.13 -91.14
REMARK 500 6 HIS A 32 -37.04 178.56
REMARK 500 6 ASN A 33 94.91 70.18
REMARK 500 7 VAL A 2 -171.97 44.08
REMARK 500 7 ILE A 5 41.71 -91.30
REMARK 500 7 ORN A 13 -33.23 84.69
REMARK 500 7 HIS A 14 145.43 78.74
REMARK 500
REMARK 500 THIS ENTRY HAS 76 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 20 0.14 SIDE CHAIN
REMARK 500 1 ARG A 25 0.31 SIDE CHAIN
REMARK 500 2 ARG A 20 0.26 SIDE CHAIN
REMARK 500 2 ARG A 25 0.28 SIDE CHAIN
REMARK 500 3 ARG A 20 0.28 SIDE CHAIN
REMARK 500 3 ARG A 25 0.30 SIDE CHAIN
REMARK 500 4 ARG A 20 0.28 SIDE CHAIN
REMARK 500 4 ARG A 25 0.30 SIDE CHAIN
REMARK 500 5 ARG A 20 0.24 SIDE CHAIN
REMARK 500 5 ARG A 25 0.30 SIDE CHAIN
REMARK 500 6 ARG A 20 0.19 SIDE CHAIN
REMARK 500 6 ARG A 25 0.31 SIDE CHAIN
REMARK 500 7 ARG A 20 0.18 SIDE CHAIN
REMARK 500 7 ARG A 25 0.32 SIDE CHAIN
REMARK 500 8 ARG A 20 0.23 SIDE CHAIN
REMARK 500 8 ARG A 25 0.26 SIDE CHAIN
REMARK 500 9 ARG A 20 0.25 SIDE CHAIN
REMARK 500 9 ARG A 25 0.27 SIDE CHAIN
REMARK 500 10 ARG A 20 0.22 SIDE CHAIN
REMARK 500 10 ARG A 25 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HTH A 1 34 UNP P01270 PTHY_HUMAN 32 65
SEQADV 1HTH NLE A 8 UNP P01270 MET 39 ENGINEERED MUTATION
SEQADV 1HTH ORN A 13 UNP P01270 LYS 44 ENGINEERED MUTATION
SEQADV 1HTH GLU A 17 UNP P01270 SER 48 ENGINEERED MUTATION
SEQADV 1HTH NLE A 18 UNP P01270 MET 49 ENGINEERED MUTATION
SEQRES 1 A 34 SER VAL SER GLU ILE GLN LEU NLE HIS ASN LEU GLY ORN
SEQRES 2 A 34 HIS LEU ASN GLU NLE GLU ARG VAL GLU TRP LEU ARG LYS
SEQRES 3 A 34 LYS LEU GLN ASP VAL HIS ASN PHE
MODRES 1HTH NLE A 8 LEU NORLEUCINE
MODRES 1HTH ORN A 13 ALA ORNITHINE
MODRES 1HTH NLE A 18 LEU NORLEUCINE
HET NLE A 8 19
HET ORN A 13 17
HET NLE A 18 19
HETNAM NLE NORLEUCINE
HETNAM ORN L-ORNITHINE
FORMUL 1 NLE 2(C6 H13 N O2)
FORMUL 1 ORN C5 H12 N2 O2
HELIX 1 1 GLU A 4 GLN A 6 5 3
HELIX 2 2 ARG A 20 GLN A 29 1 10
LINK C LEU A 7 N NLE A 8 1555 1555 1.29
LINK C NLE A 8 N HIS A 9 1555 1555 1.31
LINK C GLY A 12 N ORN A 13 1555 1555 1.31
LINK C ORN A 13 N HIS A 14 1555 1555 1.31
LINK NE ORN A 13 CD GLU A 17 1555 1555 1.31
LINK C GLU A 17 N NLE A 18 1555 1555 1.30
LINK C NLE A 18 N GLU A 19 1555 1555 1.30
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 - 3 20 Bytes