HEADER STRUCTURAL PROTEIN 25-OCT-06 2JMA
TITLE R21A SPC-SH3:P41 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, BRAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 965-1025;
COMPND 5 SYNONYM: SPECTRIN, NON-ERYTHROID ALPHA CHAIN, FODRIN ALPHA CHAIN,
COMPND 6 ALPHA SPECTRIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: P41 PEPTIDE;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: SPTAN1, SPTA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630
KEYWDS SH3 DOMAIN, P41-BOUND, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.A.J.VAN NULAND,S.CASARES,E.AB,H.ESHUIS,O.LOPEZ-MAYORGA,F.CONEJERO-
AUTHOR 2 LARA
REVDAT 4 20-DEC-23 2JMA 1 REMARK
REVDAT 3 20-OCT-21 2JMA 1 SOURCE REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2JMA 1 VERSN
REVDAT 1 24-APR-07 2JMA 0
JRNL AUTH S.CASARES,E.AB,H.ESHUIS,O.LOPEZ-MAYORGA,N.A.J.VAN NULAND,
JRNL AUTH 2 F.CONEJERO-LARA
JRNL TITL THE HIGH-RESOLUTION NMR STRUCTURE OF THE R21A SPC-SH3:P41
JRNL TITL 2 COMPLEX: UNDERSTANDING THE DETERMINANTS OF BINDING AFFINITY
JRNL TITL 3 BY COMPARISON WITH ABL-SH3
JRNL REF BMC STRUCT.BIOL. V. 7 22 2007
JRNL REFN ESSN 1472-6807
JRNL PMID 17407569
JRNL DOI 10.1186/1472-6807-7-22
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRVIEW, ARIA
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRVIEW), LINGE, O'DONOGHUE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FINAL REFINEMENT IN EXPLICIT SOLVENT
REMARK 3 WITHIN ARIA
REMARK 4
REMARK 4 2JMA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000100010.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 2 MM R21A SPC-SH3, 5.2 MM P41,
REMARK 210 90 % H2O, 10 % D2O, 20 MM D5-
REMARK 210 GLYCINE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, ARIA, HADDOCK 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 INTERACTION ENERGY
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: 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 VAL A 46 H ASP A 48 1.60
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 ASP A 2 61.24 -117.43
REMARK 500 1 ASN A 47 -58.02 60.21
REMARK 500 1 ASP A 48 -9.86 -155.53
REMARK 500 2 ASP A 2 76.08 -102.96
REMARK 500 2 ASN A 47 -56.47 59.58
REMARK 500 2 ASP A 48 -8.40 -161.37
REMARK 500 2 SER B 3 31.43 -82.76
REMARK 500 3 LYS A 6 -151.35 172.94
REMARK 500 3 ASN A 47 -55.94 60.39
REMARK 500 3 ASP A 48 -7.12 -161.44
REMARK 500 3 SER B 3 46.25 -96.43
REMARK 500 4 LYS A 6 -151.88 169.49
REMARK 500 4 SER A 36 36.15 -143.50
REMARK 500 4 ASN A 47 -55.62 63.27
REMARK 500 4 ASP A 48 -9.81 -166.17
REMARK 500 4 SER B 3 38.54 -88.64
REMARK 500 5 ASN A 47 -61.89 58.33
REMARK 500 5 ASP A 48 -10.06 -151.70
REMARK 500 5 SER B 3 38.98 -86.06
REMARK 500 6 GLU A 3 59.08 -150.28
REMARK 500 6 LYS A 6 -149.69 173.98
REMARK 500 6 ASN A 47 -56.65 61.80
REMARK 500 6 ASP A 48 -7.37 -165.65
REMARK 500 6 SER B 3 55.30 -94.71
REMARK 500 7 LYS A 6 -152.97 171.91
REMARK 500 7 ASN A 47 -56.28 57.53
REMARK 500 7 ASP A 48 -11.54 -154.72
REMARK 500 7 SER B 3 40.77 -92.00
REMARK 500 8 GLU A 3 -9.89 -59.78
REMARK 500 8 ASN A 47 -65.07 57.00
REMARK 500 8 ASP A 48 -5.98 -150.36
REMARK 500 8 SER B 3 49.43 -100.15
REMARK 500 9 GLU A 3 58.24 -151.38
REMARK 500 9 LYS A 6 -152.31 173.36
REMARK 500 9 SER A 36 35.57 -142.01
REMARK 500 9 ASN A 47 -54.55 60.47
REMARK 500 9 ASP A 48 -11.46 -167.06
REMARK 500 9 SER B 3 53.53 -93.26
REMARK 500 10 ASN A 47 -56.11 61.32
REMARK 500 10 ASP A 48 -8.48 -165.25
REMARK 500 10 SER B 3 51.60 -105.84
REMARK 500 11 LYS A 6 -143.89 171.53
REMARK 500 11 ASN A 47 -57.23 63.00
REMARK 500 11 ASP A 48 -5.85 -164.06
REMARK 500 11 SER B 3 51.86 -100.06
REMARK 500 12 ASN A 47 -56.24 60.21
REMARK 500 12 ASP A 48 -8.42 -162.09
REMARK 500 13 GLU A 3 55.05 -144.70
REMARK 500 13 LYS A 6 -152.92 172.84
REMARK 500 13 ASN A 47 -55.78 62.40
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JM8 RELATED DB: PDB
REMARK 900 R21A SPC-SH3 FREE
REMARK 900 RELATED ID: 2JM9 RELATED DB: PDB
REMARK 900 R21A SPC-SH3 BOUND
REMARK 900 RELATED ID: 7305 RELATED DB: BMRB
REMARK 900 R21A SPC-SH3 FREE
REMARK 900 RELATED ID: 7306 RELATED DB: BMRB
REMARK 900 R21A SPC-SH3 BOUND
DBREF 2JMA A 2 62 UNP P07751 SPTA2_CHICK 965 1025
DBREF 2JMA B 0 10 PDB 2JMA 2JMA 0 10
SEQADV 2JMA MET A 1 UNP P07751 CLONING ARTIFACT
SEQADV 2JMA ALA A 21 UNP P07751 ARG 984 ENGINEERED MUTATION
SEQRES 1 A 62 MET ASP GLU THR GLY LYS GLU LEU VAL LEU ALA LEU TYR
SEQRES 2 A 62 ASP TYR GLN GLU LYS SER PRO ALA GLU VAL THR MET LYS
SEQRES 3 A 62 LYS GLY ASP ILE LEU THR LEU LEU ASN SER THR ASN LYS
SEQRES 4 A 62 ASP TRP TRP LYS VAL GLU VAL ASN ASP ARG GLN GLY PHE
SEQRES 5 A 62 VAL PRO ALA ALA TYR VAL LYS LYS LEU ASP
SEQRES 1 B 11 ACE ALA PRO SER TYR SER PRO PRO PRO PRO PRO
HET ACE B 0 6
HETNAM ACE ACETYL GROUP
FORMUL 2 ACE C2 H4 O
SHEET 1 A 5 ARG A 49 PRO A 54 0
SHEET 2 A 5 TRP A 41 VAL A 46 -1 N TRP A 42 O VAL A 53
SHEET 3 A 5 ILE A 30 ASN A 35 -1 N LEU A 34 O LYS A 43
SHEET 4 A 5 LEU A 8 ALA A 11 -1 N VAL A 9 O LEU A 31
SHEET 5 A 5 VAL A 58 LYS A 60 -1 O LYS A 59 N LEU A 10
LINK C ACE B 0 N ALA B 1 1555 1555 1.33
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
