Header list of 2hh4.pdb file
Complete list - t 20 2 Bytes
HEADER HORMONE/GROWTH FACTOR 27-JUN-06 2HH4
TITLE NMR STRUCTURE OF HUMAN INSULIN MUTANT GLY-B8-D-SER, HIS-B10-ASP PRO-
TITLE 2 B28-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,S.NAKAGAWA,S.Q.HU,W.JIA,M.A.WEISS
REVDAT 4 20-OCT-21 2HH4 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2HH4 1 VERSN
REVDAT 2 05-SEP-06 2HH4 1 JRNL
REVDAT 1 18-JUL-06 2HH4 0
JRNL AUTH Q.X.HUA,S.NAKAGAWA,S.Q.HU,W.JIA,S.WANG,M.A.WEISS
JRNL TITL TOWARD THE ACTIVE CONFORMATION OF INSULIN: STEREOSPECIFIC
JRNL TITL 2 MODULATION OF A STRUCTURAL SWITCH IN THE B CHAIN.
JRNL REF J.BIOL.CHEM. V. 281 24900 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16762918
JRNL DOI 10.1074/JBC.M602691200
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) 0.51
REMARK 3 ANGSTROM
REMARK 4
REMARK 4 2HH4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038341.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 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 ALA B 14 H VAL B 18 1.52
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 -104.43 -70.30
REMARK 500 1 GLN A 5 -30.70 -39.85
REMARK 500 1 CYS A 6 -74.92 -59.71
REMARK 500 1 SER A 9 -133.35 -141.67
REMARK 500 1 VAL B 2 -41.10 -156.82
REMARK 500 1 GLN B 4 -159.74 -127.51
REMARK 500 1 SER B 9 -4.50 -49.61
REMARK 500 1 PHE B 25 119.17 -160.99
REMARK 500 1 TYR B 26 -130.68 -77.33
REMARK 500 1 THR B 27 -91.43 -79.88
REMARK 500 1 LYS B 28 64.60 30.57
REMARK 500 1 PRO B 29 91.85 -66.57
REMARK 500 2 CYS A 6 -70.70 -90.50
REMARK 500 2 SER A 9 -176.51 173.22
REMARK 500 2 CYS A 20 166.16 -40.90
REMARK 500 2 VAL B 2 -88.95 -79.96
REMARK 500 2 ASN B 3 -97.16 -94.19
REMARK 500 2 GLN B 4 -27.78 -160.79
REMARK 500 2 LEU B 6 119.47 -160.11
REMARK 500 2 SER B 9 -29.53 -39.78
REMARK 500 2 CYS B 19 -70.43 -72.32
REMARK 500 2 THR B 27 -87.12 -40.59
REMARK 500 2 PRO B 29 -158.41 -58.60
REMARK 500 3 CYS A 6 -77.58 -57.58
REMARK 500 3 THR A 8 -71.90 -84.95
REMARK 500 3 SER A 9 -106.94 -117.60
REMARK 500 3 ILE A 10 -128.28 -79.89
REMARK 500 3 CYS A 11 105.81 179.30
REMARK 500 3 CYS B 7 155.79 179.82
REMARK 500 3 CYS B 19 -76.43 -64.61
REMARK 500 3 THR B 27 -55.71 -153.75
REMARK 500 3 LYS B 28 89.07 59.46
REMARK 500 4 VAL A 3 43.34 -90.68
REMARK 500 4 CYS A 6 -80.52 -72.22
REMARK 500 4 CYS A 7 28.34 -75.95
REMARK 500 4 SER A 9 -80.68 -160.06
REMARK 500 4 ASN B 3 -81.92 -145.25
REMARK 500 4 GLN B 4 -9.32 -162.01
REMARK 500 4 HIS B 5 102.52 -50.67
REMARK 500 4 SER B 9 -10.20 -47.69
REMARK 500 4 LEU B 15 -36.66 -36.80
REMARK 500 4 CYS B 19 -83.00 -51.54
REMARK 500 4 ARG B 22 -36.41 179.97
REMARK 500 4 PHE B 24 -169.29 -120.46
REMARK 500 4 PHE B 25 -99.25 -142.26
REMARK 500 4 TYR B 26 -163.47 -164.61
REMARK 500 5 CYS A 6 -72.13 -72.95
REMARK 500 5 SER A 9 -85.30 -156.74
REMARK 500 5 CYS A 11 -159.17 -157.90
REMARK 500 5 CYS A 20 158.54 -45.35
REMARK 500
REMARK 500 THIS ENTRY HAS 220 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HHO RELATED DB: PDB
DBREF 2HH4 A 1 21 UNP Q5EEX2 Q5EEX2_HUMAN 90 110
DBREF 2HH4 B 1 30 UNP Q5EEX2 Q5EEX2_HUMAN 25 54
SEQADV 2HH4 DSN B 8 UNP Q5EEX2 GLY 32 ENGINEERED MUTATION
SEQADV 2HH4 ASP B 10 UNP Q5EEX2 HIS 34 ENGINEERED MUTATION
SEQADV 2HH4 LYS B 28 UNP Q5EEX2 PRO 52 ENGINEERED MUTATION
SEQADV 2HH4 PRO B 29 UNP Q5EEX2 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 DSN 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
MODRES 2HH4 DSN B 8 SER D-SERINE
HET DSN B 8 11
HETNAM DSN D-SERINE
FORMUL 2 DSN C3 H7 N O3
HELIX 1 1 VAL A 3 SER A 9 1 7
HELIX 2 2 SER A 12 CYS A 20 1 9
HELIX 3 3 CYS B 7 GLY B 20 1 14
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.03
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.03
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.03
LINK C CYS B 7 N DSN B 8 1555 1555 1.33
LINK C DSN B 8 N SER B 9 1555 1555 1.34
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