Header list of 2fhw.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 27-DEC-05 2FHW
TITLE SOLUTION STRUCTURE OF HUMAN RELAXIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RELAXIN 3 (PRORELAXIN H3) (INSULIN-LIKE PEPTIDE INSL7)
COMPND 3 (INSULIN-LIKE PEPTIDE 7);
COMPND 4 CHAIN: B;
COMPND 5 FRAGMENT: RELAXIN 3 B CHAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RELAXIN 3 (PRORELAXIN H3) (INSULIN-LIKE PEPTIDE INSL7)
COMPND 9 (INSULIN-LIKE PEPTIDE 7);
COMPND 10 CHAIN: A;
COMPND 11 FRAGMENT: RELAXIN 3 A CHAIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS. FOR THIS
SOURCE 4 STUDY THE PEPTIDE HAS BEEN GENERATED BY SOLID PHASE PEPTIDE
SOURCE 5 SYNTHESIS.;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS. FOR THIS
SOURCE 9 STUDY THE PEPTIDE HAS BEEN GENERATED BY SOLID PHASE PEPTIDE
SOURCE 10 SYNTHESIS.
KEYWDS INSULIN/RELAXIN SUPER-FAMILY FOLD, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,D.J.CRAIK
REVDAT 4 09-MAR-22 2FHW 1 REMARK
REVDAT 3 24-FEB-09 2FHW 1 VERSN
REVDAT 2 04-APR-06 2FHW 1 JRNL
REVDAT 1 24-JAN-06 2FHW 0
JRNL AUTH K.J.ROSENGREN,F.LIN,R.A.BATHGATE,G.W.TREGEAR,N.L.DALY,
JRNL AUTH 2 J.D.WADE,D.J.CRAIK
JRNL TITL SOLUTION STRUCTURE AND NOVEL INSIGHTS INTO THE DETERMINANTS
JRNL TITL 2 OF THE RECEPTOR SPECIFICITY OF HUMAN RELAXIN-3.
JRNL REF J.BIOL.CHEM. V. 281 5845 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16365033
JRNL DOI 10.1074/JBC.M511210200
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), BRUNGER A.T. ET AL. (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 2FHW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035896.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 303; 293
REMARK 210 PH : 3; 3; 3
REMARK 210 IONIC STRENGTH : 0; 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUMAN RELAXIN-3; 90% H2O,
REMARK 210 10% D2O; 1MM HUMAN RELAXIN-3;
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3.5, XEASY 1.3.7,
REMARK 210 CYANA 1.0, CNS 1.1
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING
REMARK 210 TORSION ANGLE DYNAMICS AND
REMARK 210 FURTHER REFINED USING CARTESIAN
REMARK 210 DYNAMICS IN EXPLICIT SOLVENT.
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
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 ALA B 2 -150.93 -119.02
REMARK 500 1 SER B 25 41.47 -105.18
REMARK 500 2 ALA B 2 -149.44 -77.13
REMARK 500 2 ALA B 3 76.10 -161.09
REMARK 500 2 TYR B 5 34.35 -81.68
REMARK 500 2 SER B 25 88.79 -172.09
REMARK 500 2 ARG B 26 -38.83 -167.36
REMARK 500 2 TRP A 13 -56.33 -123.48
REMARK 500 3 ALA B 2 -151.80 -94.75
REMARK 500 3 PRO B 4 48.45 -80.07
REMARK 500 4 ALA B 2 -150.49 -156.34
REMARK 500 4 TYR B 5 49.28 -102.06
REMARK 500 5 ALA B 2 -150.39 -126.64
REMARK 500 6 ALA B 2 -146.02 -81.49
REMARK 500 6 PRO B 4 44.44 -90.34
REMARK 500 6 SER A 22 3.72 -69.03
REMARK 500 7 ALA B 3 55.33 -161.34
REMARK 500 7 PRO B 4 38.98 -86.27
REMARK 500 7 TYR B 5 70.26 -102.51
REMARK 500 7 SER B 25 48.18 -90.85
REMARK 500 8 PRO B 4 45.66 -75.62
REMARK 500 9 ALA B 2 -153.80 -96.29
REMARK 500 9 ALA B 3 70.54 -161.05
REMARK 500 9 PRO B 4 48.88 -76.30
REMARK 500 9 TYR B 5 34.03 -84.82
REMARK 500 9 SER B 25 45.66 -102.39
REMARK 500 10 ALA B 2 -152.78 -98.59
REMARK 500 10 PRO B 4 44.27 -93.10
REMARK 500 10 TRP A 13 -60.91 -103.43
REMARK 500 11 PRO B 4 45.25 -71.13
REMARK 500 11 SER B 25 44.33 -92.16
REMARK 500 12 ALA B 3 54.49 -167.79
REMARK 500 12 PRO B 4 41.01 -99.26
REMARK 500 12 TYR B 5 73.14 -109.40
REMARK 500 12 SER B 25 49.11 -96.03
REMARK 500 13 ALA B 2 41.07 -86.29
REMARK 500 13 ALA B 3 61.32 -173.91
REMARK 500 13 PRO B 4 41.75 -90.47
REMARK 500 13 TYR B 5 79.28 -107.50
REMARK 500 13 SER B 25 52.84 -101.14
REMARK 500 13 SER A 22 7.34 -69.97
REMARK 500 14 ALA B 2 -156.76 -168.54
REMARK 500 14 PRO B 4 46.63 -78.69
REMARK 500 14 TYR B 5 59.65 -111.41
REMARK 500 14 SER B 25 50.32 -97.21
REMARK 500 15 ALA B 2 33.13 -84.54
REMARK 500 15 ALA B 3 53.09 -171.63
REMARK 500 15 PRO B 4 46.00 -78.51
REMARK 500 15 TYR B 5 59.02 -112.30
REMARK 500 16 ALA B 2 49.98 -85.33
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FHW B 1 27 UNP Q8WXF3 REL3_HUMAN 26 52
DBREF 2FHW A 1 24 UNP Q8WXF3 REL3_HUMAN 119 142
SEQRES 1 B 27 ARG ALA ALA PRO TYR GLY VAL ARG LEU CYS GLY ARG GLU
SEQRES 2 B 27 PHE ILE ARG ALA VAL ILE PHE THR CYS GLY GLY SER ARG
SEQRES 3 B 27 TRP
SEQRES 1 A 24 ASP VAL LEU ALA GLY LEU SER SER SER CYS CYS LYS TRP
SEQRES 2 A 24 GLY CYS SER LYS SER GLU ILE SER SER LEU CYS
HELIX 1 1 GLY B 11 GLY B 23 1 13
HELIX 2 2 ASP A 1 TRP A 13 1 13
HELIX 3 3 LYS A 17 SER A 22 1 6
SHEET 1 A 2 GLY B 6 VAL B 7 0
SHEET 2 A 2 CYS A 15 SER A 16 -1 O CYS A 15 N VAL B 7
SSBOND 1 CYS B 10 CYS A 11 1555 1555 2.03
SSBOND 2 CYS B 22 CYS A 24 1555 1555 2.02
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