Header list of 1hpy.pdb file
Complete list - 23 20 Bytes
HEADER PEPTIDE HORMONE 30-SEP-98 1HPY
TITLE THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN
TITLE 2 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARATHYROID HORMONE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-34;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PEPTIDE HORMONE, SOLUTION STRUCTURE, HUMAN PARATHYROID HORMONE,
KEYWDS 2 TRIFLUORETHANOL
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR U.C.MARX,P.ROESCH,K.ADERMANN,P.BAYER,W.-G.FORSSMANN
REVDAT 4 23-FEB-22 1HPY 1 REMARK
REVDAT 3 24-FEB-09 1HPY 1 VERSN
REVDAT 2 01-APR-03 1HPY 1 JRNL
REVDAT 1 14-JAN-00 1HPY 0
JRNL AUTH U.C.MARX,K.ADERMANN,P.BAYER,W.G.FORSSMANN,P.ROSCH
JRNL TITL SOLUTION STRUCTURES OF HUMAN PARATHYROID HORMONE FRAGMENTS
JRNL TITL 2 HPTH(1-34) AND HPTH(1-39) AND BOVINE PARATHYROID HORMONE
JRNL TITL 3 FRAGMENT BPTH(1-37).
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 267 213 2000
JRNL REFN ISSN 0006-291X
JRNL PMID 10623601
JRNL DOI 10.1006/BBRC.1999.1958
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: THE STRUCTURE CALCULATION FOLLOWED
REMARK 3 STANDARD PROCEDURES EMPLOYING A HYBRID DISTANCE GEOMETRY
REMARK 3 MOLECULAR DYNAMICS APPROACH WITH SIMULATED ANNEALING REFINEMENT
REMARK 3 AND SUBSEQUENT ENERGY MINIMIZATION. FOR THE REFINEMENT THE
REMARK 3 DIELECTRIC CONSTANT WAS CHANGED TO 4. STRUCTURE PARAMETERS WERE
REMARK 3 EXTRACTED FROM THE STANDARD FILES PARALLHDG.PRO AND
REMARK 3 TOPALLHDG.PRO OF X-PLOR 3.1. IN EACH ROUND OF THE STRUCTURE
REMARK 3 CALCULATION 30 STRUCTURES WERE CALCULATED. OF THE 30 STRUCTURES
REMARK 3 RESULTING FROM THE FINAL ROUND OF STRUCTURE CALCULATION, THOSE
REMARK 3 10 STRUCTURES THAT SHOWED THE LOWEST TOTAL ENERGY VALUES WERE
REMARK 3 SELECTED FOR FURTHER CHARACTERIZATION.
REMARK 4
REMARK 4 1HPY 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_1000173965.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20% TFE/80% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY
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 : 30
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: THE DISTANCE RESTRAINTS USED FOR STRUCTURE CALCULATION
REMARK 210 WERE OBTAINED FROM TWO-DIMENSIONAL HOMONUCLEAR 1H-NOESY SPECTRA.
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 O VAL A 21 H ARG A 25 1.57
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 SER A 3 -59.70 -160.81
REMARK 500 1 ASN A 16 -45.46 -139.93
REMARK 500 1 MET A 18 125.65 67.63
REMARK 500 1 GLU A 19 -60.90 75.20
REMARK 500 1 HIS A 32 -65.05 -126.45
REMARK 500 1 ASN A 33 -54.66 -167.25
REMARK 500 2 SER A 3 130.48 71.97
REMARK 500 2 GLU A 4 -42.34 85.48
REMARK 500 2 ASN A 16 -56.55 70.72
REMARK 500 2 SER A 17 -80.08 -85.94
REMARK 500 2 ASP A 30 -138.62 -89.61
REMARK 500 2 HIS A 32 -175.00 97.34
REMARK 500 2 ASN A 33 -71.23 -51.59
REMARK 500 3 SER A 3 -66.57 -126.99
REMARK 500 3 HIS A 9 -83.35 -88.29
REMARK 500 3 ASN A 10 -42.89 70.86
REMARK 500 3 HIS A 14 24.11 -172.89
REMARK 500 3 SER A 17 -27.60 84.38
REMARK 500 3 VAL A 31 53.24 -101.74
REMARK 500 4 GLU A 4 -45.99 85.08
REMARK 500 4 SER A 17 -57.52 -143.13
REMARK 500 4 ASP A 30 -165.17 -120.07
REMARK 500 4 ASN A 33 -55.96 -120.73
REMARK 500 5 SER A 3 131.04 73.35
REMARK 500 5 GLU A 4 -48.46 83.25
REMARK 500 5 SER A 17 -146.41 -125.04
REMARK 500 5 VAL A 21 -39.37 -39.73
REMARK 500 5 ASP A 30 -148.35 -100.21
REMARK 500 5 ASN A 33 32.22 -161.12
REMARK 500 6 LYS A 13 39.17 -95.22
REMARK 500 6 HIS A 14 -55.68 -134.71
REMARK 500 6 MET A 18 -47.58 -158.80
REMARK 500 6 ASN A 33 -56.20 -149.70
REMARK 500 7 VAL A 2 140.30 62.35
REMARK 500 7 SER A 3 -56.89 -122.80
REMARK 500 7 HIS A 14 -149.24 -74.53
REMARK 500 7 ASN A 16 -26.81 81.04
REMARK 500 7 SER A 17 -47.38 82.12
REMARK 500 7 ASP A 30 -148.78 -121.86
REMARK 500 7 HIS A 32 122.47 -176.57
REMARK 500 8 VAL A 2 -55.69 77.10
REMARK 500 8 HIS A 14 -94.69 -75.42
REMARK 500 8 LEU A 15 -60.80 68.15
REMARK 500 8 ASN A 33 -63.02 76.19
REMARK 500 9 SER A 3 -74.11 -141.17
REMARK 500 9 SER A 17 -55.37 -142.22
REMARK 500 9 GLU A 19 41.89 -94.77
REMARK 500 9 ARG A 20 -56.80 -152.20
REMARK 500 9 VAL A 21 -39.31 -39.85
REMARK 500 9 ASP A 30 -144.66 -124.18
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 0.28 SIDE CHAIN
REMARK 500 1 ARG A 25 0.29 SIDE CHAIN
REMARK 500 2 ARG A 20 0.32 SIDE CHAIN
REMARK 500 2 ARG A 25 0.29 SIDE CHAIN
REMARK 500 3 ARG A 20 0.31 SIDE CHAIN
REMARK 500 3 ARG A 25 0.31 SIDE CHAIN
REMARK 500 4 ARG A 20 0.29 SIDE CHAIN
REMARK 500 4 ARG A 25 0.29 SIDE CHAIN
REMARK 500 5 ARG A 20 0.30 SIDE CHAIN
REMARK 500 5 ARG A 25 0.30 SIDE CHAIN
REMARK 500 6 ARG A 20 0.32 SIDE CHAIN
REMARK 500 6 ARG A 25 0.31 SIDE CHAIN
REMARK 500 7 ARG A 20 0.32 SIDE CHAIN
REMARK 500 7 ARG A 25 0.29 SIDE CHAIN
REMARK 500 8 ARG A 20 0.32 SIDE CHAIN
REMARK 500 8 ARG A 25 0.32 SIDE CHAIN
REMARK 500 9 ARG A 20 0.32 SIDE CHAIN
REMARK 500 9 ARG A 25 0.31 SIDE CHAIN
REMARK 500 10 ARG A 20 0.28 SIDE CHAIN
REMARK 500 10 ARG A 25 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HPY A 1 34 UNP P01270 PTHY_HUMAN 32 65
SEQRES 1 A 34 SER VAL SER GLU ILE GLN LEU MET HIS ASN LEU GLY LYS
SEQRES 2 A 34 HIS LEU ASN SER MET GLU ARG VAL GLU TRP LEU ARG LYS
SEQRES 3 A 34 LYS LEU GLN ASP VAL HIS ASN PHE
HELIX 1 1 GLU A 4 LYS A 13 1 10
HELIX 2 2 ARG A 20 GLN A 29 5 10
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