Header list of 1bzb.pdb file
Complete list - 29 20 Bytes
HEADER HORMONE/GROWTH FACTOR 27-OCT-98 1BZB
TITLE GLYCOSYLATED EEL CALCITONIN
CAVEAT 1BZB MAN B 3 HAS WRONG CHIRALITY AT ATOM C1 NAG B 1 HAS WRONG
CAVEAT 2 1BZB CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CALCITONIN);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SYNTHETICALLY GLYCOSYLATED AT ASN3
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN ANGUILLA JAPONICA
SOURCE 4 (JAPANESE EEL)
KEYWDS HORMONE, CALCIUM-REGULATOR, OSTEOPOROSIS, HORMONE-GROWTH FACTOR
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.HASHIMOTO,K.TOMA,J.NISHIKIDO,K.YAMAMOTO,K.HANEDA,T.INAZU,
AUTHOR 2 K.VALENTINE,S.J.OPELLA
REVDAT 8 29-JUL-20 1BZB 1 CAVEAT COMPND REMARK HETNAM
REVDAT 8 2 1 LINK SITE ATOM
REVDAT 7 13-JUL-11 1BZB 1 VERSN
REVDAT 6 04-MAY-11 1BZB 1 DBREF
REVDAT 5 27-APR-11 1BZB 1 DBREF
REVDAT 4 24-FEB-09 1BZB 1 VERSN
REVDAT 3 01-APR-03 1BZB 1 JRNL
REVDAT 2 29-DEC-99 1BZB 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 11-NOV-98 1BZB 0
JRNL AUTH Y.HASHIMOTO,K.TOMA,J.NISHIKIDO,K.YAMAMOTO,K.HANEDA,T.INAZU,
JRNL AUTH 2 K.G.VALENTINE,S.J.OPELLA
JRNL TITL EFFECTS OF GLYCOSYLATION ON THE STRUCTURE AND DYNAMICS OF
JRNL TITL 2 EEL CALCITONIN IN MICELLES AND LIPID BILAYERS DETERMINED BY
JRNL TITL 3 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 38 8377 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10387083
JRNL DOI 10.1021/BI983018J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BZB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008343.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING A SERIES OF 2D NMR SPECTROSCOPY
REMARK 210 ON UNLABLED
REMARK 210 SAMPLE. SODIUM DODECYL SULFATE (SDS) WAS ADDED TO THE NMR SAMPLE
REMARK 210 AT A SDS/
REMARK 210 PEPTIDE RATIO OF 100/1.
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, B
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ARG A 24 NH1
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 ASN A 3 -70.95 -55.17
REMARK 500 1 SER A 5 -72.99 -158.68
REMARK 500 1 ARG A 24 103.37 -160.55
REMARK 500 1 ASP A 26 67.94 64.30
REMARK 500 2 SER A 2 45.89 -88.80
REMARK 500 2 ASN A 3 -46.08 -179.19
REMARK 500 2 SER A 5 -63.33 -162.49
REMARK 500 2 GLN A 20 -84.57 53.37
REMARK 500 2 PRO A 23 -174.79 -64.95
REMARK 500 2 THR A 25 -51.40 -161.67
REMARK 500 2 ALA A 29 -66.73 70.79
REMARK 500 3 SER A 5 -82.81 -114.90
REMARK 500 3 THR A 21 44.27 -88.28
REMARK 500 3 TYR A 22 127.32 65.45
REMARK 500 3 ASP A 26 78.31 59.70
REMARK 500 3 ALA A 29 79.52 -154.23
REMARK 500 4 SER A 2 -49.87 76.47
REMARK 500 4 SER A 5 -63.05 -151.94
REMARK 500 4 TYR A 22 70.58 55.68
REMARK 500 4 ASP A 26 -107.67 53.38
REMARK 500 4 THR A 31 73.71 58.71
REMARK 500 5 SER A 2 -48.81 -140.47
REMARK 500 5 SER A 5 -64.54 -158.43
REMARK 500 5 TYR A 22 72.52 61.64
REMARK 500 5 ASP A 26 75.29 -156.88
REMARK 500 5 ALA A 29 179.93 67.54
REMARK 500 6 SER A 2 40.26 -154.05
REMARK 500 6 ASN A 3 -31.77 168.41
REMARK 500 6 LEU A 4 70.98 70.57
REMARK 500 6 SER A 5 -72.27 -142.37
REMARK 500 6 TYR A 22 83.42 48.34
REMARK 500 7 SER A 2 -38.51 92.49
REMARK 500 7 SER A 5 -55.29 -161.04
REMARK 500 7 LEU A 19 -79.46 -68.93
REMARK 500 7 GLN A 20 -80.25 63.60
REMARK 500 7 ASP A 26 -77.65 69.57
REMARK 500 7 VAL A 27 -34.46 -130.40
REMARK 500 7 ALA A 29 80.10 51.89
REMARK 500 8 SER A 2 -85.25 -50.21
REMARK 500 8 ASN A 3 148.12 179.58
REMARK 500 8 SER A 5 -61.19 168.14
REMARK 500 8 TYR A 22 90.41 47.82
REMARK 500 8 ARG A 24 82.17 60.96
REMARK 500 8 THR A 25 49.42 -88.81
REMARK 500 8 ASP A 26 70.45 -172.56
REMARK 500 9 ASN A 3 -167.22 50.31
REMARK 500 9 LEU A 4 54.49 -148.67
REMARK 500 9 SER A 5 -65.50 -139.28
REMARK 500 9 GLN A 20 60.96 26.95
REMARK 500 9 VAL A 27 57.01 -143.20
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
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 SER A 2 ASN A 3 8 148.58
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 0.08 SIDE CHAIN
REMARK 500 10 TYR A 22 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BZB A 1 32 UNP P01262 CALC_ANGJA 1 32
SEQRES 1 A 33 CYS SER ASN LEU SER THR CYS VAL LEU GLY LYS LEU SER
SEQRES 2 A 33 GLN GLU LEU HIS LYS LEU GLN THR TYR PRO ARG THR ASP
SEQRES 3 A 33 VAL GLY ALA GLY THR PRO NH2
MODRES 1BZB ASN A 3 ASN GLYCOSYLATION SITE
HET NH2 A 41 3
HET NAG B 1 27
HET NAG B 2 27
HET MAN B 3 20
HET MAN B 4 21
HET MAN B 5 22
HET MAN B 6 20
HET MAN B 7 22
HET MAN B 8 22
HETNAM NH2 AMINO GROUP
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 1 NH2 H2 N
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 MAN 6(C6 H12 O6)
HELIX 1 H1 SER A 5 LEU A 19 5 15
SSBOND 1 CYS A 1 CYS A 7 1555 1555 2.04
LINK ND2 ASN A 3 C1 NAG B 1 1555 1555 1.45
LINK C PRO A 32 N NH2 A 41 1555 1555 1.34
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.40
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.40
LINK O3 MAN B 3 C1 MAN B 4 1555 1555 1.42
LINK O6 MAN B 3 C1 MAN B 6 1555 1555 1.40
LINK O2 MAN B 4 C1 MAN B 5 1555 1555 1.42
LINK O3 MAN B 6 C1 MAN B 7 1555 1555 1.42
LINK O6 MAN B 6 C1 MAN B 8 1555 1555 1.40
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 - 29 20 Bytes