Header list of 1fb9.pdb file
Complete list - 27 20 Bytes
HEADER SIGNALING PROTEIN 14-JUL-00 1FB9
TITLE EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON
TITLE 2 CALCITONIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCITONIN ANALOGUE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ONCORHYNCHUS GORBUSCHA;
SOURCE 3 ORGANISM_COMMON: PINK SALMON;
SOURCE 4 ORGANISM_TAXID: 8017;
SOURCE 5 ORGAN: PAROTID;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHARMACIA BIOTECH, PGEX-4T-3 GST GENE
SOURCE 10 FUSION VECTOR
KEYWDS ALPHA HELIX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR H.WU,J.MAO,Y.WANG,H.DOU
REVDAT 3 27-JUN-18 1FB9 1 REMARK SEQADV ATOM
REVDAT 2 24-FEB-09 1FB9 1 VERSN
REVDAT 1 01-JUL-03 1FB9 0
JRNL AUTH Y.WANG,H.DOU,C.CAO,N.ZHANG,J.MA,J.MAO,H.WU
JRNL TITL SOLUTION STRUCTURE AND BIOLOGICAL ACTIVITY OF RECOMBINANT
JRNL TITL 2 SALMON CALCITONIN S-SULFONATED ANALOG
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 306 582 2003
JRNL REFN ISSN 0006-291X
JRNL PMID 12804605
JRNL DOI 10.1016/S0006-291X(03)01028-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, AMBER 5.0
REMARK 3 AUTHORS : MIKE CARLISLE, DAN STEELE, MIKE MILLER (VNMR),
REMARK 3 PETER KOLLMAN, DAVE CASE, KEN MERZ, THOMAS
REMARK 3 CHEATHAM, CARLOS SIMMERLING, VERTEX
REMARK 3 PHARMACEUTICALS. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 530 RESTRAINTS, 478 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 26
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 26 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1FB9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011454.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.64
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3.5 MM; 3.5 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY 1994, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED
REMARK 210 USING STANDARD 2D HOMONUCLEAR
REMARK 210 TECHNIQUES.
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
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 2 41.03 -81.07
REMARK 500 1 ASN A 3 59.63 -111.35
REMARK 500 1 ARG A 24 106.40 -165.51
REMARK 500 1 SER A 29 -87.66 -167.95
REMARK 500 2 SER A 2 28.15 -147.39
REMARK 500 2 THR A 27 60.97 -119.63
REMARK 500 3 SER A 2 40.78 -150.32
REMARK 500 3 SER A 29 -57.87 -154.30
REMARK 500 3 THR A 31 76.54 -114.08
REMARK 500 4 ASN A 3 99.89 -167.13
REMARK 500 5 SER A 2 52.37 -159.71
REMARK 500 5 ARG A 24 75.90 -68.12
REMARK 500 6 PRO A 23 -174.69 -68.46
REMARK 500 6 ASN A 26 74.74 113.31
REMARK 500 6 THR A 27 71.68 -66.84
REMARK 500 6 SER A 29 -70.68 -84.80
REMARK 500 7 ASN A 3 101.77 74.65
REMARK 500 7 PRO A 23 91.03 -65.76
REMARK 500 7 ARG A 24 75.95 -66.41
REMARK 500 7 THR A 27 69.88 -69.28
REMARK 500 8 SER A 2 174.32 63.85
REMARK 500 8 ASN A 3 130.37 67.20
REMARK 500 8 THR A 25 -78.64 -91.78
REMARK 500 8 THR A 31 134.23 98.22
REMARK 500 9 SER A 2 42.17 -78.65
REMARK 500 9 ASN A 3 77.22 -104.06
REMARK 500 9 PRO A 23 -179.05 -67.14
REMARK 500 9 ARG A 24 78.20 -55.20
REMARK 500 9 ASN A 26 63.14 -155.26
REMARK 500 9 THR A 27 82.33 -69.37
REMARK 500 10 SER A 2 34.00 -74.81
REMARK 500 10 PRO A 23 88.88 -67.60
REMARK 500 10 ASN A 26 101.80 -43.26
REMARK 500 10 THR A 27 -57.99 69.77
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 2 TYR A 22 0.08 SIDE CHAIN
REMARK 500 3 TYR A 22 0.10 SIDE CHAIN
REMARK 500 5 TYR A 22 0.08 SIDE CHAIN
REMARK 500 8 TYR A 22 0.08 SIDE CHAIN
REMARK 500 10 ARG A 24 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BKU RELATED DB: PDB
REMARK 900 1BKU CONTAINS THE SOLUTION STRUCTURES OF EEL CALCITONIN IN SDS.
REMARK 900 RELATED ID: 1BYV RELATED DB: PDB
REMARK 900 1BYV CONTAINS THE SOLUTION STRUCTURES OF ONE GLYCOSYLATED EEL
REMARK 900 CALCITONIN IN SDS.
REMARK 900 RELATED ID: 1BZB RELATED DB: PDB
REMARK 900 1BZB CONTAINS THE SOLUTION STRUCTURES OF ANOTHER GLYCOSYLATED EEL
REMARK 900 CALCITONIN IN SDS.
DBREF 1FB9 A 1 32 GB 459541 CAA54988 3 34
SEQADV 1FB9 CSU A 1 GB 459541 CYS 3 MODIFIED RESIDUE
SEQADV 1FB9 CSU A 7 GB 459541 CYS 9 MODIFIED RESIDUE
SEQADV 1FB9 NH2 A 33 GB 459541 AMIDATION
SEQRES 1 A 33 CSU SER ASN LEU SER THR CSU VAL LEU GLY LYS LEU SER
SEQRES 2 A 33 GLN GLU LEU HIS LYS LEU GLN THR TYR PRO ARG THR ASN
SEQRES 3 A 33 THR GLY SER GLY THR PRO NH2
MODRES 1FB9 CSU A 1 CYS CYSTEINE-S-SULFONIC ACID
MODRES 1FB9 CSU A 7 CYS CYSTEINE-S-SULFONIC ACID
HET CSU A 1 17
HET CSU A 7 15
HET NH2 A 33 3
HETNAM CSU CYSTEINE-S-SULFONIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 CSU 2(C3 H7 N O5 S2)
FORMUL 1 NH2 H2 N
HELIX 1 1 VAL A 8 TYR A 22 1 15
LINK C CSU A 1 N SER A 2 1555 1555 1.34
LINK C PRO A 32 N NH2 A 33 1555 1555 1.34
LINK C THR A 6 N CSU A 7 1555 1555 1.34
LINK C CSU A 7 N VAL A 8 1555 1555 1.34
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 - 27 20 Bytes