HEADER HORMONE/GROWTH FACTOR 08-FEB-00 1EFE
TITLE AN ACTIVE MINI-PROINSULIN, M2PI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MINI-PROINSULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: M2PI;
COMPND 5 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS LINKER, INSULIN, PROINSULIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.CHO,S.G.CHANG,K.D.CHOI,H.SHIN,B.AHN,K.S.KIM
REVDAT 4 16-FEB-22 1EFE 1 REMARK
REVDAT 3 24-FEB-09 1EFE 1 VERSN
REVDAT 2 29-MAR-00 1EFE 1 JRNL
REVDAT 1 17-MAR-00 1EFE 0
JRNL AUTH Y.CHO,S.G.CHANG,K.D.CHOI,H.SHIN,B.AHN,K.S.KIM
JRNL TITL SOLUTION STRUCTURE OF AN ACTIVE MINI-PROINSULIN, M2PI:
JRNL TITL 2 INTER-CHAIN FLEXIBILITY IS CRUCIAL FOR INSULIN ACTIVITY
JRNL REF J.BIOCHEM.MOL.BIOL. V. 33 120 2000
JRNL REFN ISSN 1225-8687
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.G.CHANG,D.Y.KIM,K.D.CHOI,J.M.SHIN,H.C.SHIN
REMARK 1 TITL HUMAN INSULIN PRODUCTION FROM A NOVEL MINI-PROINSULIN WHICH
REMARK 1 TITL 2 HAS HIGH RECEPTOR-BINDING ACTIVITY
REMARK 1 REF BIOCHEM.J. V. 329 631 1998
REMARK 1 REFN ISSN 0264-6021
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EFE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010524.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 2.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM M2PI U-15N; 20% ACETIC ACID;
REMARK 210 70% H2O, 10% D2O; 2MM M2PI; 20%
REMARK 210 ACETIC ACID; 70% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
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 ASN A 3 84.51 -151.18
REMARK 500 1 THR A 30 -52.93 70.08
REMARK 500 1 ARG A 32 -98.68 57.45
REMARK 500 1 ARG A 39 -49.25 -151.17
REMARK 500 2 ASN A 3 81.58 -152.88
REMARK 500 2 THR A 30 -63.42 66.62
REMARK 500 2 ARG A 31 -144.49 49.99
REMARK 500 3 ASN A 3 54.13 -163.76
REMARK 500 3 THR A 30 28.73 36.40
REMARK 500 3 VAL A 37 -80.36 58.91
REMARK 500 4 ASN A 3 72.50 -162.94
REMARK 500 4 LEU A 6 93.82 -66.01
REMARK 500 4 ARG A 31 -89.99 46.19
REMARK 500 4 VAL A 37 28.38 40.63
REMARK 500 4 LYS A 38 29.86 -161.32
REMARK 500 5 PRO A 28 -166.26 -75.20
REMARK 500 6 ASN A 3 80.14 -153.79
REMARK 500 6 TYR A 26 71.88 45.72
REMARK 500 6 PRO A 28 -162.81 -72.84
REMARK 500 6 THR A 30 88.36 54.63
REMARK 500 6 ARG A 31 -48.55 -154.89
REMARK 500 6 VAL A 37 -86.83 55.08
REMARK 500 7 ASN A 3 45.08 -156.73
REMARK 500 7 PRO A 28 -160.62 -71.20
REMARK 500 7 THR A 30 39.83 36.33
REMARK 500 7 ARG A 31 -70.00 -79.98
REMARK 500 7 VAL A 37 -64.37 65.33
REMARK 500 7 ARG A 39 -36.97 -151.44
REMARK 500 8 ASN A 3 39.47 -159.44
REMARK 500 8 TYR A 26 69.39 61.16
REMARK 500 8 THR A 30 24.10 -160.37
REMARK 500 8 SER A 48 -154.34 -126.46
REMARK 500 9 ASN A 3 88.74 -154.92
REMARK 500 9 TYR A 26 27.67 45.72
REMARK 500 9 ARG A 32 18.94 59.59
REMARK 500 9 PRO A 34 80.84 -67.83
REMARK 500 9 VAL A 37 -65.54 64.19
REMARK 500 9 ARG A 39 -42.02 -167.45
REMARK 500 10 ASN A 3 38.61 -156.41
REMARK 500 10 TYR A 26 27.53 43.10
REMARK 500 10 ARG A 31 -167.63 46.77
REMARK 500 11 ASN A 3 40.56 -156.36
REMARK 500 11 TYR A 26 73.29 49.43
REMARK 500 11 PRO A 28 -168.92 -67.39
REMARK 500 11 THR A 30 -86.07 -159.74
REMARK 500 11 VAL A 37 67.14 -155.14
REMARK 500 11 ARG A 39 -44.60 -155.41
REMARK 500 12 ARG A 32 32.17 -168.97
REMARK 500 12 TYR A 33 82.64 -159.62
REMARK 500 12 ASP A 36 -175.61 53.18
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 A 22 0.30 SIDE CHAIN
REMARK 500 1 ARG A 31 0.28 SIDE CHAIN
REMARK 500 1 ARG A 32 0.23 SIDE CHAIN
REMARK 500 1 ARG A 39 0.21 SIDE CHAIN
REMARK 500 2 ARG A 22 0.16 SIDE CHAIN
REMARK 500 2 ARG A 31 0.18 SIDE CHAIN
REMARK 500 2 ARG A 32 0.23 SIDE CHAIN
REMARK 500 2 ARG A 39 0.32 SIDE CHAIN
REMARK 500 3 ARG A 22 0.27 SIDE CHAIN
REMARK 500 3 ARG A 31 0.32 SIDE CHAIN
REMARK 500 3 ARG A 32 0.22 SIDE CHAIN
REMARK 500 3 ARG A 39 0.27 SIDE CHAIN
REMARK 500 4 ARG A 22 0.32 SIDE CHAIN
REMARK 500 4 ARG A 31 0.32 SIDE CHAIN
REMARK 500 4 ARG A 32 0.20 SIDE CHAIN
REMARK 500 4 ARG A 39 0.24 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 5 ARG A 31 0.25 SIDE CHAIN
REMARK 500 5 ARG A 32 0.23 SIDE CHAIN
REMARK 500 5 ARG A 39 0.30 SIDE CHAIN
REMARK 500 6 ARG A 22 0.30 SIDE CHAIN
REMARK 500 6 ARG A 31 0.15 SIDE CHAIN
REMARK 500 6 ARG A 32 0.26 SIDE CHAIN
REMARK 500 6 ARG A 39 0.24 SIDE CHAIN
REMARK 500 7 ARG A 22 0.27 SIDE CHAIN
REMARK 500 7 ARG A 31 0.15 SIDE CHAIN
REMARK 500 7 ARG A 32 0.27 SIDE CHAIN
REMARK 500 7 ARG A 39 0.30 SIDE CHAIN
REMARK 500 8 ARG A 22 0.30 SIDE CHAIN
REMARK 500 8 ARG A 31 0.28 SIDE CHAIN
REMARK 500 8 ARG A 32 0.26 SIDE CHAIN
REMARK 500 8 ARG A 39 0.30 SIDE CHAIN
REMARK 500 9 ARG A 22 0.28 SIDE CHAIN
REMARK 500 9 ARG A 31 0.26 SIDE CHAIN
REMARK 500 9 ARG A 32 0.28 SIDE CHAIN
REMARK 500 9 ARG A 39 0.32 SIDE CHAIN
REMARK 500 10 ARG A 22 0.31 SIDE CHAIN
REMARK 500 10 ARG A 31 0.29 SIDE CHAIN
REMARK 500 10 ARG A 32 0.24 SIDE CHAIN
REMARK 500 10 ARG A 39 0.32 SIDE CHAIN
REMARK 500 11 ARG A 22 0.31 SIDE CHAIN
REMARK 500 11 ARG A 31 0.31 SIDE CHAIN
REMARK 500 11 ARG A 32 0.29 SIDE CHAIN
REMARK 500 11 ARG A 39 0.23 SIDE CHAIN
REMARK 500 12 ARG A 22 0.29 SIDE CHAIN
REMARK 500 12 ARG A 31 0.24 SIDE CHAIN
REMARK 500 12 ARG A 32 0.32 SIDE CHAIN
REMARK 500 12 ARG A 39 0.32 SIDE CHAIN
REMARK 500 13 ARG A 22 0.23 SIDE CHAIN
REMARK 500 13 ARG A 31 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EFE A 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1EFE A 40 60 UNP P01308 INS_HUMAN 90 110
SEQADV 1EFE ARG A 31 UNP P01308 SEE REMARK 999
SEQADV 1EFE ARG A 32 UNP P01308 SEE REMARK 999
SEQADV 1EFE TYR A 33 UNP P01308 SEE REMARK 999
SEQADV 1EFE PRO A 34 UNP P01308 SEE REMARK 999
SEQADV 1EFE GLY A 35 UNP P01308 SEE REMARK 999
SEQADV 1EFE ASP A 36 UNP P01308 SEE REMARK 999
SEQADV 1EFE VAL A 37 UNP P01308 SEE REMARK 999
SEQADV 1EFE LYS A 38 UNP P01308 SEE REMARK 999
SEQADV 1EFE ARG A 39 UNP P01308 SEE REMARK 999
SEQRES 1 A 60 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 A 60 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 A 60 THR PRO LYS THR ARG ARG TYR PRO GLY ASP VAL LYS ARG
SEQRES 4 A 60 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 5 A 60 TYR GLN LEU GLU ASN TYR CYS ASN
HELIX 1 1 CYS A 7 GLY A 20 1 14
HELIX 2 2 GLY A 40 SER A 48 1 9
HELIX 3 3 SER A 51 CYS A 59 1 9
SSBOND 1 CYS A 7 CYS A 46 1555 1555 2.02
SSBOND 2 CYS A 19 CYS A 59 1555 1555 2.02
SSBOND 3 CYS A 45 CYS A 50 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
(ATOM LINES ARE NOT SHOWN.)
END