Header list of 2h8b.pdb file
Complete list - r 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR 07-JUN-06 2H8B
TITLE SOLUTION STRUCTURE OF INSL3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE 3;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: INSULIN-LIKE 3 B CHAIN;
COMPND 5 SYNONYM: INSULIN-LIKE PEPTIDE-3, INSL3, LEYDIG INSULIN-LIKE PEPTIDE,
COMPND 6 LEY-I-L, RELAXIN-LIKE FACTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INSULIN-LIKE 3;
COMPND 10 CHAIN: A;
COMPND 11 FRAGMENT: INSULIN-LIKE 3 A CHAIN;
COMPND 12 SYNONYM: INSULIN-LIKE PEPTIDE-3, INSL3, LEYDIG INSULIN-LIKE PEPTIDE,
COMPND 13 LEY-I-L, RELAXIN-LIKE FACTOR;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: FOR THIS STUDY THE PEPTIDE HAS BEEN GENERATED BY
SOURCE 4 SOLID PHASE PEPTIDE SYNTHESIS.; THIS SEQUENCE OCCURS NATURALLY IN
SOURCE 5 HUMANS.;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: FOR THIS STUDY THE PEPTIDE HAS BEEN GENERATED BY
SOURCE 9 SOLID PHASE PEPTIDE SYNTHESIS.; THIS SEQUENCE OCCURS NATURALLY IN
SOURCE 10 HUMANS.
KEYWDS INSULIN/RELAXIN SUPARFAMILY FOLD, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,D.J.CRAIK,N.L.DALY
REVDAT 4 09-MAR-22 2H8B 1 REMARK
REVDAT 3 24-FEB-09 2H8B 1 VERSN
REVDAT 2 03-OCT-06 2H8B 1 JRNL
REVDAT 1 01-AUG-06 2H8B 0
JRNL AUTH K.J.ROSENGREN,S.ZHANG,F.LIN,N.L.DALY,D.J.SCOTT,R.A.HUGHES,
JRNL AUTH 2 R.A.D.BATHGATE,D.J.CRAIK,J.D.WADE
JRNL TITL SOLUTION STRUCTURE AND CHARACTERIZATION OF THE LGR8 RECEPTOR
JRNL TITL 2 BINDING SURFACE OF INSULIN-LIKE PEPTIDE 3
JRNL REF J.BIOL.CHEM. V. 281 28287 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16867980
JRNL DOI 10.1074/JBC.M603829200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS AND REFINEMENTS
REMARK 3 WERE DONE IN CNS USING PROTOCOLS FROM ARIA.
REMARK 4
REMARK 4 2H8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038055.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 303; 290; 298; 298; 298
REMARK 210 PH : 4.0; 4.0; 4.0; 2.7; 5.1; 6.1
REMARK 210 IONIC STRENGTH : 0; 0; 0; 0; 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM INSL3; 90% H2O, 10% D20; 1MM
REMARK 210 INSL3; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, CYANA 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST 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: B, 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 HG LEU B 18 HE1 TRP B 27 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 PRO B 3 53.34 -69.91
REMARK 500 1 ARG B 26 -34.06 -166.26
REMARK 500 1 THR B 29 -33.00 -178.55
REMARK 500 1 GLU B 30 32.04 -86.46
REMARK 500 1 ASN A 5 116.11 -173.73
REMARK 500 1 SER A 13 -63.65 -92.02
REMARK 500 1 THR A 16 -168.64 -100.89
REMARK 500 2 GLU B 4 -169.04 -176.28
REMARK 500 2 TRP B 27 -18.93 -154.28
REMARK 500 2 SER B 28 -146.20 -157.58
REMARK 500 2 ALA A 3 55.21 -161.17
REMARK 500 2 ASN A 5 116.05 -170.09
REMARK 500 2 SER A 13 -63.21 -92.56
REMARK 500 2 PRO A 25 -157.43 -90.29
REMARK 500 3 CYS B 22 41.16 -90.40
REMARK 500 3 TRP B 27 49.92 -98.03
REMARK 500 3 SER B 28 62.97 -63.56
REMARK 500 3 THR B 29 -37.61 -169.84
REMARK 500 3 ASN A 5 117.14 -169.14
REMARK 500 3 SER A 13 -63.07 -99.68
REMARK 500 3 CYS A 15 -157.93 -144.07
REMARK 500 3 THR A 16 -162.77 -171.32
REMARK 500 4 TRP B 27 -45.35 -158.62
REMARK 500 4 SER B 28 -138.76 -105.92
REMARK 500 4 ALA A 3 129.50 -173.62
REMARK 500 5 CYS B 22 36.82 -79.05
REMARK 500 5 ARG B 26 36.87 -94.21
REMARK 500 5 SER B 28 60.06 -69.49
REMARK 500 5 THR B 29 -46.41 -164.71
REMARK 500 5 ALA A 3 135.50 -175.42
REMARK 500 5 PRO A 25 -157.12 -88.77
REMARK 500 6 PRO B 3 86.77 -22.92
REMARK 500 6 CYS B 22 42.25 -86.48
REMARK 500 6 TRP B 27 -15.55 -173.52
REMARK 500 6 SER B 28 -130.65 -151.59
REMARK 500 6 ALA A 3 127.67 -173.68
REMARK 500 6 PRO A 25 -158.41 -92.49
REMARK 500 7 PRO B 3 65.09 -67.86
REMARK 500 7 CYS B 22 47.60 -97.70
REMARK 500 7 SER B 28 63.47 -61.37
REMARK 500 7 THR B 29 -38.77 -169.32
REMARK 500 7 THR A 4 -62.25 -141.18
REMARK 500 7 ASN A 5 109.76 -170.93
REMARK 500 8 TRP B 27 -90.26 -147.29
REMARK 500 8 SER B 28 58.76 -166.68
REMARK 500 8 THR B 29 -90.40 -166.73
REMARK 500 8 ALA A 3 142.53 -178.12
REMARK 500 8 SER A 13 -92.88 -95.14
REMARK 500 9 PRO B 3 59.94 -67.82
REMARK 500 9 CYS B 22 27.79 -77.66
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2H8B A 1 26 UNP P51460 INSL3_HUMAN 106 131
DBREF 2H8B B 1 31 UNP P51460 INSL3_HUMAN 25 55
SEQRES 1 B 31 PRO THR PRO GLU MET ARG GLU LYS LEU CYS GLY HIS HIS
SEQRES 2 B 31 PHE VAL ARG ALA LEU VAL ARG VAL CYS GLY GLY PRO ARG
SEQRES 3 B 31 TRP SER THR GLU ALA
SEQRES 1 A 26 ALA ALA ALA THR ASN PRO ALA ARG TYR CYS CYS LEU SER
SEQRES 2 A 26 GLY CYS THR GLN GLN ASP LEU LEU THR LEU CYS PRO TYR
HELIX 1 1 GLY B 11 GLY B 23 1 13
HELIX 2 2 ASN A 5 SER A 13 1 9
HELIX 3 3 THR A 16 THR A 22 1 7
SSBOND 1 CYS B 10 CYS A 11 1555 1555 2.03
SSBOND 2 CYS B 22 CYS A 24 1555 1555 2.03
SSBOND 3 CYS A 10 CYS A 15 1555 1555 2.03
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 - r 9 2 Bytes