Header list of 1sf1.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR 19-FEB-04 1SF1
TITLE NMR STRUCTURE OF HUMAN INSULIN UNDER AMYLOIDOGENIC CONDITION, 15
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: INS;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HORMONE, HUMAN INSULIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.A.WEISS,Q.X.HUA
REVDAT 4 02-MAR-22 1SF1 1 REMARK
REVDAT 3 24-FEB-09 1SF1 1 VERSN
REVDAT 2 22-JUN-04 1SF1 1 JRNL
REVDAT 1 30-MAR-04 1SF1 0
JRNL AUTH Q.X.HUA,M.A.WEISS
JRNL TITL MECHANISM OF INSULIN FIBRILLATION: THE STRUCTURE OF INSULIN
JRNL TITL 2 UNDER AMYLOIDOGENIC CONDITIONS RESEMBLES A PROTEIN-FOLDING
JRNL TITL 3 INTERMEDIATE
JRNL REF J.BIOL.CHEM. V. 279 21449 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14988398
JRNL DOI 10.1074/JBC.M314141200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMSD VALUES FOR ALL 15 STRUCTURES
REMARK 3 VERSUS GEOMETRIC AVERAGE: (BACKBONE, A2-A20, B4-B24) 2.27
REMARK 3 ANGSTROM
REMARK 4
REMARK 4 1SF1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021651.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 333
REMARK 210 PH : 2.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM 15N-LABELED SAMPLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; NOESY; COSY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B 6.1B
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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 USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 15N-3D HETERONUCLEAR NMR 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: DIMERIC
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 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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 4 ASN A 21 C ASN A 21 O 0.161
REMARK 500 13 ASN A 21 C ASN A 21 O 0.200
REMARK 500
REMARK 500 REMARK: NULL
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 1 ASN A 21 CA - C - O ANGL. DEV. = -32.0 DEGREES
REMARK 500 13 ASN A 21 CA - C - O ANGL. DEV. = -20.5 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 THR A 8 44.83 161.65
REMARK 500 1 SER A 9 106.14 161.27
REMARK 500 1 ILE A 10 177.37 82.09
REMARK 500 1 CYS A 11 122.36 73.91
REMARK 500 1 SER A 12 61.66 169.30
REMARK 500 1 LEU A 13 87.74 62.91
REMARK 500 1 TYR A 14 -51.14 164.98
REMARK 500 1 LEU A 16 -125.71 -70.28
REMARK 500 1 GLU A 17 26.17 46.19
REMARK 500 1 ASN A 18 30.83 175.15
REMARK 500 1 CYS B 7 -177.66 53.61
REMARK 500 1 PHE B 25 -74.32 -73.64
REMARK 500 2 GLU A 4 83.08 68.55
REMARK 500 2 GLN A 5 130.35 176.03
REMARK 500 2 CYS A 6 -83.68 -42.78
REMARK 500 2 THR A 8 60.33 176.70
REMARK 500 2 SER A 9 25.53 -171.37
REMARK 500 2 ILE A 10 110.00 52.38
REMARK 500 2 CYS A 20 77.51 -157.89
REMARK 500 2 ASN B 3 65.31 -174.97
REMARK 500 2 CYS B 7 48.58 162.61
REMARK 500 2 GLU B 21 -173.04 64.89
REMARK 500 2 ARG B 22 67.32 75.24
REMARK 500 2 PHE B 24 138.37 67.44
REMARK 500 2 PHE B 25 -68.36 178.32
REMARK 500 2 THR B 27 146.45 61.81
REMARK 500 3 GLU A 4 -129.01 -126.52
REMARK 500 3 GLN A 5 -91.44 -56.16
REMARK 500 3 CYS A 6 101.89 161.88
REMARK 500 3 CYS A 7 -36.05 -159.50
REMARK 500 3 SER A 9 -77.09 163.69
REMARK 500 3 CYS A 11 81.92 -153.05
REMARK 500 3 LEU A 16 -119.96 -79.86
REMARK 500 3 GLU A 17 27.52 44.67
REMARK 500 3 ASN A 18 35.53 -171.38
REMARK 500 3 ASN B 3 -175.46 -54.88
REMARK 500 3 GLN B 4 53.74 -91.66
REMARK 500 3 LEU B 6 -164.31 -114.94
REMARK 500 3 CYS B 7 -169.41 60.12
REMARK 500 3 SER B 9 -3.32 78.17
REMARK 500 3 GLU B 13 -72.92 -100.59
REMARK 500 3 GLU B 21 -86.98 60.98
REMARK 500 3 TYR B 26 -126.74 -123.63
REMARK 500 4 ILE A 2 48.93 -93.52
REMARK 500 4 GLU A 4 55.65 -159.57
REMARK 500 4 GLN A 5 -33.81 -148.10
REMARK 500 4 CYS A 6 92.00 67.76
REMARK 500 4 CYS A 7 -34.02 -159.98
REMARK 500 4 SER A 9 -56.99 171.06
REMARK 500 4 ILE A 10 127.31 164.93
REMARK 500
REMARK 500 THIS ENTRY HAS 274 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 B 22 0.22 SIDE CHAIN
REMARK 500 2 ARG B 22 0.32 SIDE CHAIN
REMARK 500 3 ARG B 22 0.31 SIDE CHAIN
REMARK 500 4 ARG B 22 0.25 SIDE CHAIN
REMARK 500 5 ARG B 22 0.28 SIDE CHAIN
REMARK 500 6 ARG B 22 0.32 SIDE CHAIN
REMARK 500 7 ARG B 22 0.17 SIDE CHAIN
REMARK 500 8 ARG B 22 0.26 SIDE CHAIN
REMARK 500 9 ARG B 22 0.31 SIDE CHAIN
REMARK 500 10 ARG B 22 0.29 SIDE CHAIN
REMARK 500 11 ARG B 22 0.29 SIDE CHAIN
REMARK 500 12 ARG B 22 0.32 SIDE CHAIN
REMARK 500 13 ARG B 22 0.31 SIDE CHAIN
REMARK 500 14 ARG B 22 0.30 SIDE CHAIN
REMARK 500 15 ARG B 22 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HIU RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 10
REMARK 900 STRUCTURES: NATIVE HUMAN INSULIN AT 25 DEGREE, NMR SOLUTION
REMARK 900 STRUCTURE
DBREF 1SF1 A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1SF1 B 1 30 UNP P01308 INS_HUMAN 25 54
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 30 THR PRO LYS THR
HELIX 1 1 TYR A 14 TYR A 19 1 6
HELIX 2 2 SER B 9 CYS B 19 1 11
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.02
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 - 2 20 Bytes