Header list of 1t1k.pdb file
Complete list - 27 20 Bytes
HEADER HORMONE/GROWTH FACTOR 16-APR-04 1T1K
TITLE NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B10-ASP, VAL-B12-ALA, PRO-
TITLE 2 B28-LYS, LYS-B29-PRO, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INSULIN A CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INSULIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: INSULIN B CHAIN;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS(HUMAN);
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 8 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS(HUMAN)
KEYWDS ALA-B12-DKP-INSULIN, PROTEIN UNFOLDING, INSULIN RECEPTOR, RECEPTOR
KEYWDS 2 BINDING, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.HUANG,B.XU,S.Q.HU,Y.C.CHU,Q.X.HUA,J.WHITTAKER,S.H.NAKAGAWA,P.DE
AUTHOR 2 MEYTS,P.G.KATSOYANNIS,M.A.WEISS
REVDAT 3 27-OCT-21 1T1K 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1T1K 1 VERSN
REVDAT 1 10-AUG-04 1T1K 0
JRNL AUTH K.HUANG,B.XU,S.Q.HU,Y.C.CHU,Q.X.HUA,Y.QU,B.LI,S.WANG,
JRNL AUTH 2 R.Y.WANG,S.H.NAKAGAWA,A.M.THEEDE,J.WHITTAKER,P.DE MEYTS,
JRNL AUTH 3 P.G.KATSOYANNIS,M.A.WEISS
JRNL TITL HOW INSULIN BINDS: THE B-CHAIN ALPHA-HELIX CONTACTS THE L1
JRNL TITL 2 BETA-HELIX OF THE INSULIN RECEPTOR.
JRNL REF J.MOL.BIOL. V. 341 529 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15276842
JRNL DOI 10.1016/J.JMB.2004.05.023
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.H.NAKAGAWA,H.S.TAGER,D.F.STEINER
REMARK 1 TITL MUTATIONAL ANALYSIS OF INVARIANT VALINE B12 IN INSULIN:
REMARK 1 TITL 2 IMPLICATION FOR RECEPTOR BINDING
REMARK 1 REF BIOCHEMISTRY V. 39 15826 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 11123908
REMARK 1 DOI 10.1021/BI001802+
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.KRISTEN,T.KJELDSEN,F.C.WIBERG,L.SCHAFFER,M.HACH,
REMARK 1 AUTH 2 S.HAVELUND,J.BASS,D.F.STEINER,A.S.ANDERSEN
REMARK 1 TITL ALANINE SCANNING MUTAGENESIS OF INSULIN
REMARK 1 REF J.BIOL.CHEM. V. 272 12978 1997
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.272.20.12978
REMARK 1 REFERENCE 3
REMARK 1 AUTH Q.Q.WANG,Y.M.FENG,Y.S.ZHANG
REMARK 1 TITL STUDIES ON RECEPTOR BINDING SITE OF INSULIN: THE HYDROPHOBIC
REMARK 1 TITL 2 B12VAL CAN BE SUBSTITUTED BY HYDROPHILIC THR
REMARK 1 REF BIOCHEM.MOL.BIOL.INT. V. 39 1245 1996
REMARK 1 REFN ISSN 1039-9712
REMARK 1 PMID 9148904
REMARK 1 DOI 10.1074/JBC.272.20.12978
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.Q.HU,G.T.BURKE,G.P.SCHWARTZ,N.FERDERIGOS,J.B.ROSS,
REMARK 1 AUTH 2 P.G.KATSOYANNIS
REMARK 1 TITL STERIC REQUIRMENTS AT POSITION B12 FOR HIGH BIOLOGICAL
REMARK 1 TITL 2 ACTIVITY IN INSULIN
REMARK 1 REF BIOCHEMISTRY V. 32 2631 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8448120
REMARK 1 DOI 10.1021/BI00061A022
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.P.SCHWARTZ,P.G.BURKE,P.G.KATSOYANNIS
REMARK 1 TITL [12-ASPARAGINE-B] HUMAN INSULIN. AN ANALOGUE WITH
REMARK 1 TITL 2 MODIFICATION IN THE HYDROPHOBIC CORE OF INSULIN
REMARK 1 REF INT.J.PEPT.PROTEIN RES. V. 17 243 1981
REMARK 1 REFN ISSN 0367-8377
REMARK 1 PMID 7014485
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII INSIGHTII 2000, X-PLOR 3.85
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (DGII), BRUNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 668 RESTRAINTS: 607 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 39 ARE
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 22 ARE HYDROGEN BOND RESTRAINTS.
REMARK 4
REMARK 4 1T1K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022196.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 305; 298
REMARK 210 PH : 7.0; 7.6; 1.9
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2 MM ALA-B12-DKP-INSULIN, 90%
REMARK 210 H2O, 10% D2O; 1.2 MM ALA-B12-DKP-
REMARK 210 INSULIN, 100% D2O; 1.2 MM ALA-
REMARK 210 B12-DKP-INSULIN, 20% DEUTERATED
REMARK 210 ACETIC ACID, 80% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 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 : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 BY USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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 O ALA B 12 H TYR B 16 1.52
REMARK 500 O ASP B 10 H ALA B 14 1.53
REMARK 500 O CYS B 19 H ARG B 22 1.57
REMARK 500 O SER B 9 H GLU B 13 1.59
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 VAL B 2 -151.43 -91.60
REMARK 500 1 THR B 27 160.17 -34.69
REMARK 500 2 VAL B 2 -85.16 -47.68
REMARK 500 2 GLN B 4 -143.84 -100.39
REMARK 500 2 GLU B 21 37.94 29.20
REMARK 500 2 THR B 27 154.23 -33.98
REMARK 500 3 VAL B 2 -98.04 -95.75
REMARK 500 3 ASN B 3 53.04 -108.45
REMARK 500 4 LEU A 13 -36.71 -36.47
REMARK 500 4 GLU A 17 -19.34 -49.14
REMARK 500 4 ASN B 3 41.29 177.67
REMARK 500 4 GLN B 4 -169.83 -100.63
REMARK 500 4 THR B 27 -156.96 -96.17
REMARK 500 5 LEU A 13 -38.01 -36.02
REMARK 500 5 GLN B 4 -144.81 -100.42
REMARK 500 5 LYS B 28 72.58 -164.12
REMARK 500 6 VAL B 2 -65.15 -91.11
REMARK 500 6 ASN B 3 51.27 -173.15
REMARK 500 6 GLN B 4 -169.65 -101.56
REMARK 500 6 GLU B 21 28.80 37.28
REMARK 500 6 THR B 27 -156.69 -59.97
REMARK 500 7 VAL B 2 -179.63 -62.08
REMARK 500 7 ASN B 3 73.01 -65.30
REMARK 500 7 LYS B 28 101.32 62.27
REMARK 500 8 LEU A 13 -35.04 -34.36
REMARK 500 8 TYR A 19 43.99 -141.11
REMARK 500 8 VAL B 2 -166.89 -59.31
REMARK 500 8 ASN B 3 50.60 -97.55
REMARK 500 8 GLN B 4 -168.56 -101.05
REMARK 500 8 SER B 9 -73.46 -38.45
REMARK 500 8 CYS B 19 -62.85 -98.30
REMARK 500 8 GLU B 21 28.47 39.66
REMARK 500 8 THR B 27 171.75 -41.87
REMARK 500 8 LYS B 28 70.47 73.18
REMARK 500 9 LEU A 13 -33.19 -34.54
REMARK 500 9 ASN B 3 35.33 177.67
REMARK 500 9 SER B 9 -71.81 -37.30
REMARK 500 9 THR B 27 -152.95 -82.10
REMARK 500 9 LYS B 28 124.86 -39.95
REMARK 500 10 TYR A 19 38.66 -140.28
REMARK 500 10 ASN B 3 49.48 -158.28
REMARK 500 10 GLN B 4 -164.35 -100.94
REMARK 500 10 LYS B 28 83.67 -164.85
REMARK 500 11 VAL B 2 -155.66 -75.07
REMARK 500 11 ASN B 3 55.01 -174.32
REMARK 500 11 GLN B 4 -151.92 -100.23
REMARK 500 11 SER B 9 -71.87 -39.28
REMARK 500 11 GLU B 21 22.92 38.07
REMARK 500 11 THR B 27 147.99 -27.62
REMARK 500 12 VAL B 2 -91.33 -46.21
REMARK 500
REMARK 500 THIS ENTRY HAS 63 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 0.29 SIDE CHAIN
REMARK 500 2 ARG B 22 0.30 SIDE CHAIN
REMARK 500 3 ARG B 22 0.32 SIDE CHAIN
REMARK 500 4 ARG B 22 0.28 SIDE CHAIN
REMARK 500 5 ARG B 22 0.22 SIDE CHAIN
REMARK 500 6 ARG B 22 0.21 SIDE CHAIN
REMARK 500 7 ARG B 22 0.22 SIDE CHAIN
REMARK 500 8 ARG B 22 0.26 SIDE CHAIN
REMARK 500 9 ARG B 22 0.15 SIDE CHAIN
REMARK 500 10 ARG B 22 0.30 SIDE CHAIN
REMARK 500 11 ARG B 22 0.30 SIDE CHAIN
REMARK 500 12 ARG B 22 0.32 SIDE CHAIN
REMARK 500 13 ARG B 22 0.20 SIDE CHAIN
REMARK 500 14 ARG B 22 0.23 SIDE CHAIN
REMARK 500 15 ARG B 22 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LNP RELATED DB: PDB
REMARK 900 PARENT MOLECULE OF THIS DEPOSITION, CONTAINS THREE SUBSTITUTIONS
REMARK 900 RELATED ID: 1T1P RELATED DB: PDB
REMARK 900 THR-B12-DKP-INSULIN
REMARK 900 RELATED ID: 1T1Q RELATED DB: PDB
REMARK 900 ABA-B12-DKP-INSULIN
DBREF 1T1K A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1T1K B 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 1T1K ASP B 10 UNP P01308 HIS 34 ENGINEERED MUTATION
SEQADV 1T1K ALA B 12 UNP P01308 VAL 36 ENGINEERED MUTATION
SEQADV 1T1K LYS B 28 UNP P01308 PRO 52 ENGINEERED MUTATION
SEQADV 1T1K PRO B 29 UNP P01308 LYS 53 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 ASP LEU ALA GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 30 THR LYS PRO THR
HELIX 1 1 GLU A 4 SER A 9 1 6
HELIX 2 2 SER A 12 ASN A 18 1 7
HELIX 3 3 CYS B 7 CYS B 19 1 13
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 - 27 20 Bytes