HEADER HORMONE 09-AUG-12 2LWZ
TITLE NMR STRUCTURES OF SINGLE-CHAIN INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SINGLE-CHAIN INSULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INSULIN;
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 GENE: INS;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZ
KEYWDS SINGLE CHAIN INSULIN, HORMONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.WEISS,Y.YANG
REVDAT 1 28-AUG-13 2LWZ 0
JRNL AUTH Y.YANG,Z.WAN,Q.HUA,N.B.PHILLIPS,K.HUANG,I.YEH,Y.LIU,S.HU,
JRNL AUTH 2 T.HATTIER,J.WHITTAKER,M.A.WEISS
JRNL TITL DYNAMIC REPAIR OF AN AMYLOIDOGENIC PROTEIN: INSULIN
JRNL TITL 2 FIBRILLATION IS BLOCKED BY TETHERING A NASCENT ALPHA-HELIX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB102936.
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 : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM [U-100% 13C; U-100% 15N]
REMARK 210 INSULIN, 93% H2O/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HNCO; 3D C(CO)NH; 3D H(CCO)NH; 3D
REMARK 210 HCCH-TOCSY; 3D 1H-15N NOESY; 4D
REMARK 210 TIME-SHARED NOESY (4D-N15,C13-
REMARK 210 EDITED AND 4D-C13,C13-EDITED
REMARK 210 NOESY)
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR_NIH, NMRDRAW, NMRPIPE,
REMARK 210 PIPP, XWINNMR, INSIGHTII, MOLMOL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 70
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 O VAL A 39 H CYS A 43 1.56
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 2 -91.60 -103.13
REMARK 500 1 ASP A 28 150.22 -43.52
REMARK 500 1 PRO A 34 -174.14 -68.75
REMARK 500 1 ARG A 35 86.92 -56.23
REMARK 500 1 ARG A 36 -2.48 -59.15
REMARK 500 2 VAL A 2 -91.93 -101.61
REMARK 500 2 ASP A 28 150.74 -43.58
REMARK 500 2 ARG A 35 85.48 -61.53
REMARK 500 3 VAL A 2 -91.88 -105.13
REMARK 500 3 PRO A 34 -175.19 -68.86
REMARK 500 3 ARG A 35 86.47 -58.04
REMARK 500 3 ARG A 36 -2.01 -59.75
REMARK 500 4 VAL A 2 -91.69 -101.92
REMARK 500 4 ARG A 35 86.67 -57.90
REMARK 500 4 ARG A 36 -6.24 -59.37
REMARK 500 5 VAL A 2 -91.51 -99.55
REMARK 500 5 PRO A 34 -175.54 -69.52
REMARK 500 5 ARG A 35 86.45 -59.68
REMARK 500 6 VAL A 2 -91.65 -102.38
REMARK 500 6 ARG A 35 86.30 -56.67
REMARK 500 6 ARG A 36 0.16 -60.10
REMARK 500 7 VAL A 2 -91.36 -94.70
REMARK 500 7 ASP A 28 150.38 -42.29
REMARK 500 7 ARG A 35 86.90 -57.60
REMARK 500 8 VAL A 2 -91.29 -98.32
REMARK 500 8 PRO A 34 -175.29 -69.48
REMARK 500 8 ARG A 35 86.02 -56.68
REMARK 500 8 ARG A 36 0.66 -60.63
REMARK 500 9 VAL A 2 -91.67 -104.39
REMARK 500 9 PRO A 34 -175.58 -69.51
REMARK 500 9 ARG A 35 85.86 -57.34
REMARK 500 9 ARG A 36 -6.81 -59.64
REMARK 500 10 VAL A 2 -91.42 -100.28
REMARK 500 10 ARG A 35 86.93 -60.49
REMARK 500 10 ARG A 36 -2.98 -59.31
REMARK 500 11 VAL A 2 -91.75 -101.13
REMARK 500 11 PRO A 34 -175.62 -69.96
REMARK 500 11 ARG A 35 86.08 -58.96
REMARK 500 11 ARG A 36 -5.49 -59.57
REMARK 500 12 VAL A 2 -91.99 -102.73
REMARK 500 12 PRO A 34 -173.95 -67.81
REMARK 500 12 ARG A 35 87.10 -56.24
REMARK 500 12 ARG A 36 -1.55 -58.99
REMARK 500 13 VAL A 2 -91.78 -102.85
REMARK 500 13 PRO A 34 -175.44 -69.39
REMARK 500 13 ARG A 35 86.19 -59.84
REMARK 500 13 ARG A 36 3.08 -61.58
REMARK 500 14 VAL A 2 -91.75 -101.99
REMARK 500 14 PRO A 34 -174.46 -69.17
REMARK 500 14 ARG A 35 86.52 -56.34
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18654 RELATED DB: BMRB
DBREF 2LWZ A 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 2LWZ A 36 57 UNP P01308 INS_HUMAN 89 110
SEQADV 2LWZ ASP A 10 UNP P01308 HIS 34 CONFLICT
SEQADV 2LWZ ASP A 28 UNP P01308 PRO 52 CONFLICT
SEQADV 2LWZ PRO A 29 UNP P01308 LYS 53 CONFLICT
SEQADV 2LWZ GLY A 31 UNP P01308 LINKER
SEQADV 2LWZ GLY A 32 UNP P01308 LINKER
SEQADV 2LWZ GLY A 33 UNP P01308 LINKER
SEQADV 2LWZ PRO A 34 UNP P01308 LINKER
SEQADV 2LWZ ARG A 35 UNP P01308 LINKER
SEQADV 2LWZ HIS A 44 UNP P01308 THR 97 CONFLICT
SEQRES 1 A 57 PHE VAL ASN GLN HIS LEU CYS GLY SER ASP LEU VAL GLU
SEQRES 2 A 57 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 A 57 THR ASP PRO THR GLY GLY GLY PRO ARG ARG GLY ILE VAL
SEQRES 4 A 57 GLU GLN CYS CYS HIS SER ILE CYS SER LEU TYR GLN LEU
SEQRES 5 A 57 GLU ASN TYR CYS ASN
HELIX 1 1 GLY A 8 GLY A 20 1 13
HELIX 2 2 GLU A 21 GLY A 23 5 3
HELIX 3 3 ILE A 38 SER A 45 1 8
HELIX 4 4 SER A 48 GLU A 53 1 6
SSBOND 1 CYS A 7 CYS A 43 1555 1555 2.02
SSBOND 2 CYS A 19 CYS A 56 1555 1555 2.02
SSBOND 3 CYS A 42 CYS A 47 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
