Header list of 1k3m.pdb file
Complete list - 27 20 Bytes
HEADER HORMONE/GROWTH FACTOR 03-OCT-01 1K3M
TITLE NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-ALA, HIS-B10-ASP, 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 (RESIDUES 90-110);
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 (RESIDUES 25-54);
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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 HORMONE, HUMAN INSULIN, MUTANT, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.XU,Q.-X.HUA,S.H.NAKAGAWA,W.JIA,Y.-C.CHU,P.G.KATSOYANNIS,M.A.WEISS
REVDAT 5 27-OCT-21 1K3M 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1K3M 1 VERSN
REVDAT 3 01-APR-03 1K3M 1 JRNL
REVDAT 2 13-FEB-02 1K3M 1 JRNL AUTHOR
REVDAT 1 17-OCT-01 1K3M 0
JRNL AUTH B.XU,Q.X.HUA,S.H.NAKAGAWA,W.JIA,Y.C.CHU,P.G.KATSOYANNIS,
JRNL AUTH 2 M.A.WEISS
JRNL TITL A CAVITY-FORMING MUTATION IN INSULIN INDUCES SEGMENTAL
JRNL TITL 2 UNFOLDING OF A SURROUNDING ALPHA-HELIX.
JRNL REF PROTEIN SCI. V. 11 104 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 11742127
JRNL DOI 10.1110/PS.PS.32102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85, DGII INSIGHTII 2000
REMARK 3 AUTHORS : BRUNGER (X-PLOR), MOLECULAR SIMULATIONS INC.
REMARK 3 (DGII)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF
REMARK 3 416 RESTRAINTS, 367 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 32
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 17 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1K3M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014518.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 303; 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 ALAA2-DKP-INSULIN; 100%
REMARK 210 D2O;; 1.2 MM ALAA2-DKP-INSULIN;
REMARK 210 90% H2O, 10% D2O;; 1.2 MM ALAA2-
REMARK 210 DKP-INSULIN; 20% DEUTEROACETIC
REMARK 210 ACID, 80% D2O;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 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
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
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 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 LEU B 15 H CYS B 19 1.26
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 A 3 -69.27 -122.64
REMARK 500 1 GLN A 5 60.57 -163.14
REMARK 500 1 CYS A 6 -32.48 160.00
REMARK 500 1 SER A 9 -139.82 164.97
REMARK 500 1 CYS A 11 -138.40 -78.77
REMARK 500 1 LEU A 13 -29.85 -37.36
REMARK 500 1 CYS A 20 -162.35 -74.41
REMARK 500 1 ASN B 3 138.16 -177.35
REMARK 500 1 HIS B 5 120.89 65.90
REMARK 500 2 VAL A 3 -62.85 -161.83
REMARK 500 2 SER A 9 170.82 167.76
REMARK 500 2 CYS A 11 -124.75 -73.65
REMARK 500 2 LEU A 13 -36.25 -32.74
REMARK 500 2 TYR B 26 49.92 -86.60
REMARK 500 2 LYS B 28 78.52 55.38
REMARK 500 3 ALA A 2 89.89 -69.15
REMARK 500 3 VAL A 3 -62.07 -133.65
REMARK 500 3 SER A 9 -179.93 163.23
REMARK 500 3 CYS A 11 -112.63 -59.25
REMARK 500 3 LEU A 13 -31.23 -35.90
REMARK 500 3 CYS A 20 -165.61 -104.60
REMARK 500 3 ASN B 3 54.19 -159.24
REMARK 500 3 GLN B 4 98.26 -160.49
REMARK 500 3 HIS B 5 114.62 55.12
REMARK 500 3 SER B 9 -71.94 -51.15
REMARK 500 3 GLU B 21 -56.35 81.72
REMARK 500 3 ARG B 22 176.65 -54.13
REMARK 500 4 ALA A 2 72.23 -108.22
REMARK 500 4 VAL A 3 -56.33 -167.56
REMARK 500 4 GLU A 4 -139.75 -60.30
REMARK 500 4 GLN A 5 -76.30 76.29
REMARK 500 4 SER A 9 179.36 159.57
REMARK 500 4 CYS A 11 -117.58 -61.36
REMARK 500 4 LEU A 13 -32.03 -35.25
REMARK 500 4 CYS A 20 -166.12 -129.46
REMARK 500 4 ASN B 3 58.56 -112.16
REMARK 500 4 GLN B 4 -72.33 -146.42
REMARK 500 4 ARG B 22 -100.68 -109.07
REMARK 500 4 LYS B 28 57.07 -174.04
REMARK 500 5 ALA A 2 84.27 52.13
REMARK 500 5 VAL A 3 -146.95 -95.67
REMARK 500 5 GLU A 4 6.56 81.59
REMARK 500 5 SER A 9 -138.11 164.35
REMARK 500 5 CYS A 11 -174.05 -53.15
REMARK 500 5 LEU A 13 -47.17 -29.75
REMARK 500 5 CYS A 20 -165.62 -126.74
REMARK 500 5 VAL B 2 -149.80 -139.58
REMARK 500 5 ASN B 3 -172.62 171.50
REMARK 500 5 GLN B 4 -141.48 -127.43
REMARK 500 6 ALA A 2 87.52 72.99
REMARK 500
REMARK 500 THIS ENTRY HAS 153 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 0.19 SIDE CHAIN
REMARK 500 2 ARG B 22 0.18 SIDE CHAIN
REMARK 500 3 ARG B 22 0.31 SIDE CHAIN
REMARK 500 4 ARG B 22 0.31 SIDE CHAIN
REMARK 500 5 ARG B 22 0.28 SIDE CHAIN
REMARK 500 6 ARG B 22 0.28 SIDE CHAIN
REMARK 500 7 ARG B 22 0.22 SIDE CHAIN
REMARK 500 8 ARG B 22 0.27 SIDE CHAIN
REMARK 500 9 ARG B 22 0.25 SIDE CHAIN
REMARK 500 10 ARG B 22 0.22 SIDE CHAIN
REMARK 500 11 ARG B 22 0.19 SIDE CHAIN
REMARK 500 12 ARG B 22 0.26 SIDE CHAIN
REMARK 500 13 ARG B 22 0.25 SIDE CHAIN
REMARK 500 14 ARG B 22 0.28 SIDE CHAIN
REMARK 500 15 ARG B 22 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
DBREF 1K3M A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1K3M B 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 1K3M ALA A 2 UNP P01308 ILE 91 ENGINEERED MUTATION
SEQADV 1K3M ASP B 10 UNP P01308 HIS 34 ENGINEERED MUTATION
SEQADV 1K3M LYS B 28 UNP P01308 PRO 52 ENGINEERED MUTATION
SEQADV 1K3M PRO B 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQRES 1 A 21 GLY ALA 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 VAL 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 LEU A 13 TYR A 19 1 7
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 - 27 20 Bytes