Header list of 2h67.pdb file
Complete list - t 20 2 Bytes
HEADER HORMONE/GROWTH FACTOR 30-MAY-06 2H67
TITLE NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B5-ALA, HIS-B10-ASP PRO-B28-
TITLE 2 LYS, LYS-B29-PRO, 20 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 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 GENE: INS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: INS;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HORMONE, HUMAN INSULIN, MUTANT, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.X.HUA,M.LIU,S.Q.HU,W.JIA,P.ARVAN,M.A.WEISS
REVDAT 4 20-OCT-21 2H67 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2H67 1 VERSN
REVDAT 2 05-SEP-06 2H67 1 JRNL
REVDAT 1 18-JUL-06 2H67 0
JRNL AUTH Q.X.HUA,M.LIU,S.Q.HU,W.JIA,P.ARVAN,M.A.WEISS
JRNL TITL A CONSERVED HISTIDINE IN INSULIN IS REQUIRED FOR THE
JRNL TITL 2 FOLDABILITY OF HUMAN PROINSULIN: STRUCTURE AND FUNCTION OF
JRNL TITL 3 AN ALAB5 ANALOG.
JRNL REF J.BIOL.CHEM. V. 281 24889 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16728398
JRNL DOI 10.1074/JBC.M602617200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMSD VALUES FOR ALL 20 STRUCTURES
REMARK 3 VERSUS GEOMETRIC AVERAGE: (BACKBONE, A2-A20, B4-B24) 0.49
REMARK 3 ANGSTROM
REMARK 4
REMARK 4 2H67 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000037979.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 305; 298
REMARK 210 PH : 7.0; 8.0; 2.0
REMARK 210 IONIC STRENGTH : NULL; NULL; 20% ACETIC ACID
REMARK 210 PRESSURE : NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 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 O VAL B 12 H TYR B 16 1.43
REMARK 500 O SER B 9 H GLU B 13 1.44
REMARK 500 O VAL A 3 H CYS A 7 1.45
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 14 ASN A 21 C ASN A 21 O 0.140
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 3 ASN A 21 CA - C - O ANGL. DEV. = -29.7 DEGREES
REMARK 500 14 ASN A 21 CA - C - O ANGL. DEV. = -22.6 DEGREES
REMARK 500 20 ASN A 21 CA - C - O ANGL. DEV. = -15.3 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 GLU A 4 -34.86 -36.40
REMARK 500 1 CYS A 7 -76.04 -78.16
REMARK 500 1 THR A 8 -87.19 -55.86
REMARK 500 1 SER A 9 173.46 -49.37
REMARK 500 1 CYS A 20 178.89 -49.89
REMARK 500 1 LEU B 11 -73.45 -66.69
REMARK 500 1 CYS B 19 -73.25 -107.03
REMARK 500 1 LYS B 28 124.04 172.18
REMARK 500 2 THR A 8 -83.63 -61.89
REMARK 500 2 SER A 9 -163.20 -57.67
REMARK 500 2 LEU B 11 -70.82 -68.29
REMARK 500 3 GLN A 5 -66.04 -100.32
REMARK 500 3 SER A 9 -140.76 75.65
REMARK 500 3 VAL B 2 -167.71 -127.03
REMARK 500 3 ALA B 5 177.30 -59.59
REMARK 500 3 TYR B 16 -31.63 -39.13
REMARK 500 3 GLU B 21 -8.03 75.54
REMARK 500 3 LYS B 28 -49.19 160.44
REMARK 500 4 GLN A 5 -78.51 -63.27
REMARK 500 4 SER A 9 -175.10 -177.82
REMARK 500 4 VAL B 2 -159.63 -107.80
REMARK 500 4 ASN B 3 43.36 -93.27
REMARK 500 4 ALA B 5 -166.98 -72.81
REMARK 500 4 LEU B 6 108.19 -165.66
REMARK 500 4 LEU B 11 -70.60 -76.06
REMARK 500 4 GLU B 21 -0.95 77.96
REMARK 500 4 PHE B 25 -82.16 -98.25
REMARK 500 4 TYR B 26 75.36 38.44
REMARK 500 4 PRO B 29 170.91 -59.59
REMARK 500 5 ALA B 5 -164.70 -68.17
REMARK 500 5 LEU B 6 105.99 -160.18
REMARK 500 6 ILE A 2 -33.17 -39.77
REMARK 500 6 VAL A 3 -75.29 -90.74
REMARK 500 6 GLU A 4 -30.89 -39.52
REMARK 500 6 GLN A 5 -71.37 -88.79
REMARK 500 6 THR A 8 -85.13 -84.43
REMARK 500 6 CYS A 11 163.23 -41.19
REMARK 500 6 CYS A 20 109.99 -55.40
REMARK 500 6 VAL B 2 -154.13 -154.79
REMARK 500 6 ALA B 5 -53.85 -134.49
REMARK 500 6 LEU B 6 87.43 65.09
REMARK 500 6 PHE B 24 177.31 -54.37
REMARK 500 6 PHE B 25 -84.12 -101.46
REMARK 500 6 TYR B 26 72.23 35.01
REMARK 500 6 LYS B 28 50.54 -148.98
REMARK 500 7 GLU A 4 -31.09 -38.77
REMARK 500 7 GLN A 5 -78.56 -68.91
REMARK 500 7 SER A 9 -177.38 69.54
REMARK 500 7 CYS A 20 153.79 -48.74
REMARK 500 7 ALA B 5 -176.94 -64.36
REMARK 500
REMARK 500 THIS ENTRY HAS 173 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 0.27 SIDE CHAIN
REMARK 500 2 ARG B 22 0.24 SIDE CHAIN
REMARK 500 3 ARG B 22 0.12 SIDE CHAIN
REMARK 500 5 ARG B 22 0.32 SIDE CHAIN
REMARK 500 7 ARG B 22 0.31 SIDE CHAIN
REMARK 500 9 ARG B 22 0.21 SIDE CHAIN
REMARK 500 10 ARG B 22 0.27 SIDE CHAIN
REMARK 500 11 ARG B 22 0.29 SIDE CHAIN
REMARK 500 13 ARG B 22 0.09 SIDE CHAIN
REMARK 500 14 ARG B 22 0.30 SIDE CHAIN
REMARK 500 18 ARG B 22 0.09 SIDE CHAIN
REMARK 500 20 ARG B 22 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2H67 A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 2H67 B 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 2H67 ALA B 5 UNP P01308 HIS 29 ENGINEERED MUTATION
SEQADV 2H67 ASP B 10 UNP P01308 HIS 34 ENGINEERED MUTATION
SEQADV 2H67 LYS B 28 UNP P01308 PRO 52 ENGINEERED MUTATION
SEQADV 2H67 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 ALA 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 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 GLU A 17 1 6
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 - t 20 2 Bytes