Header list of 1jco.pdb file
Complete list - t 27 2 Bytes
HEADER HORMONE/GROWTH FACTOR 11-JUN-01 1JCO
TITLE SOLUTION STRUCTURE OF THE MONOMERIC [THR(B27)->PRO,PRO(B28)->THR]
TITLE 2 INSULIN MUTANT (PT INSULIN)
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 B CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPIC9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS HELIX-TURN-HELIX, COIL-HELIX-COIL, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.KELLER,R.CLAUSEN,K.JOSEFSEN,J.J.LED
REVDAT 3 27-OCT-21 1JCO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JCO 1 VERSN
REVDAT 1 03-OCT-01 1JCO 0
JRNL AUTH D.KELLER,R.CLAUSEN,K.JOSEFSEN,J.J.LED
JRNL TITL FLEXIBILITY AND BIOACTIVITY OF INSULIN: AN NMR INVESTIGATION
JRNL TITL 2 OF THE SOLUTION STRUCTURE AND FOLDING OF AN UNUSUALLY
JRNL TITL 3 FLEXIBLE HUMAN INSULIN MUTANT WITH INCREASED BIOLOGICAL
JRNL TITL 4 ACTIVITY.
JRNL REF BIOCHEMISTRY V. 40 10732 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11524020
JRNL DOI 10.1021/BI0108150
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER, BAX
REMARK 3 (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 197 NOES, 52 DIHEDRAL ANGLES, 11
REMARK 3 HYDROGEN BONDS. FORCE CONSTANTS: K(NOE)= 50 KCAL MOL-1 AA-1,
REMARK 3 K(DIHE)= 200 KCAL MOL-1 AA-1
REMARK 4
REMARK 4 1JCO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013628.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.13
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.8 MM PT-INSULIN; 10%D2O;
REMARK 210 90%H2O; 2.8 MM PT-INSULIN; 100%
REMARK 210 D2O; 2.8 MM PT-INSULIN; 35%
REMARK 210 TRIFLUOROETHANOL; 5% D2O; 60%
REMARK 210 H2O; 2.8 MM PT-INSULIN; 35%
REMARK 210 TRIFLUOROETHANOL; 65% D2O;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY DIGITAL UNIX V4.0 VERSION
REMARK 210 1, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
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: 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 O ALA B 14 H VAL B 18 1.47
REMARK 500 O ILE A 2 H CYS A 6 1.55
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 CYS A 7 108.89 -50.80
REMARK 500 1 THR A 8 -147.23 174.63
REMARK 500 1 SER A 9 -71.21 -56.15
REMARK 500 1 SER A 12 84.52 -32.40
REMARK 500 1 CYS A 20 -163.06 40.93
REMARK 500 1 HIS B 5 164.85 -43.57
REMARK 500 1 CYS B 7 100.46 65.09
REMARK 500 1 CYS B 19 35.77 177.77
REMARK 500 1 THR B 28 99.25 68.45
REMARK 500 2 THR A 8 100.76 166.04
REMARK 500 2 SER A 9 -86.22 56.05
REMARK 500 2 SER A 12 85.04 -29.81
REMARK 500 2 CYS A 20 -162.49 39.90
REMARK 500 2 ASN B 3 92.17 44.15
REMARK 500 2 HIS B 5 163.00 178.25
REMARK 500 2 SER B 9 -44.20 82.36
REMARK 500 2 CYS B 19 18.01 -160.34
REMARK 500 2 PHE B 24 22.75 -162.86
REMARK 500 2 THR B 28 72.41 70.28
REMARK 500 3 SER A 9 -149.00 -172.70
REMARK 500 3 SER A 12 96.58 36.70
REMARK 500 3 CYS A 20 -162.36 40.89
REMARK 500 3 VAL B 2 84.36 57.70
REMARK 500 3 GLN B 4 72.34 178.97
REMARK 500 3 HIS B 5 -72.61 -37.04
REMARK 500 3 LEU B 6 -25.70 175.80
REMARK 500 3 CYS B 7 103.82 70.56
REMARK 500 3 CYS B 19 26.70 -172.71
REMARK 500 3 THR B 28 86.24 45.06
REMARK 500 4 THR A 8 89.87 -51.83
REMARK 500 4 SER A 9 -145.00 52.17
REMARK 500 4 SER A 12 93.27 36.48
REMARK 500 4 CYS A 20 -159.68 37.48
REMARK 500 4 VAL B 2 83.74 -161.68
REMARK 500 4 GLN B 4 65.38 -179.75
REMARK 500 4 HIS B 5 -86.80 -40.45
REMARK 500 4 LEU B 6 -17.48 162.62
REMARK 500 4 CYS B 7 -43.00 81.86
REMARK 500 4 SER B 9 -26.81 84.52
REMARK 500 4 CYS B 19 19.46 -165.00
REMARK 500 5 CYS A 7 83.59 -59.30
REMARK 500 5 THR A 8 -151.05 -158.46
REMARK 500 5 SER A 9 -109.37 -59.42
REMARK 500 5 SER A 12 74.74 17.37
REMARK 500 5 CYS A 20 -160.59 38.00
REMARK 500 5 VAL B 2 143.20 -174.54
REMARK 500 5 GLN B 4 40.89 -90.20
REMARK 500 5 LEU B 6 -45.26 80.65
REMARK 500 5 CYS B 7 101.04 66.46
REMARK 500 5 SER B 9 -48.12 81.14
REMARK 500
REMARK 500 THIS ENTRY HAS 263 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 0.26 SIDE CHAIN
REMARK 500 2 ARG B 22 0.25 SIDE CHAIN
REMARK 500 3 ARG B 22 0.22 SIDE CHAIN
REMARK 500 4 ARG B 22 0.20 SIDE CHAIN
REMARK 500 5 ARG B 22 0.23 SIDE CHAIN
REMARK 500 6 ARG B 22 0.27 SIDE CHAIN
REMARK 500 7 ARG B 22 0.21 SIDE CHAIN
REMARK 500 8 ARG B 22 0.12 SIDE CHAIN
REMARK 500 9 ARG B 22 0.20 SIDE CHAIN
REMARK 500 10 ARG B 22 0.32 SIDE CHAIN
REMARK 500 11 ARG B 22 0.30 SIDE CHAIN
REMARK 500 12 ARG B 22 0.31 SIDE CHAIN
REMARK 500 13 ARG B 22 0.17 SIDE CHAIN
REMARK 500 14 ARG B 22 0.31 SIDE CHAIN
REMARK 500 15 ARG B 22 0.30 SIDE CHAIN
REMARK 500 16 ARG B 22 0.23 SIDE CHAIN
REMARK 500 17 ARG B 22 0.25 SIDE CHAIN
REMARK 500 18 ARG B 22 0.27 SIDE CHAIN
REMARK 500 19 ARG B 22 0.21 SIDE CHAIN
REMARK 500 20 ARG B 22 0.30 SIDE CHAIN
REMARK 500 21 ARG B 22 0.24 SIDE CHAIN
REMARK 500 22 ARG B 22 0.28 SIDE CHAIN
REMARK 500 23 ARG B 22 0.24 SIDE CHAIN
REMARK 500 24 ARG B 22 0.27 SIDE CHAIN
REMARK 500 25 ARG B 22 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JCO A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1JCO B 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 1JCO PRO B 27 UNP P01308 THR 51 ENGINEERED MUTATION
SEQADV 1JCO THR B 28 UNP P01308 PRO 52 ENGINEERED MUTATION
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 PRO THR LYS THR
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 CYS A 20 1 9
HELIX 3 3 SER B 9 GLY B 20 1 12
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
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 - t 27 2 Bytes