Header list of 1h3h.pdb file
Complete list - l 24 2 Bytes
HEADER PROTEIN-BINDING 03-SEP-02 1H3H
TITLE STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN
TITLE 2 RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3
TITLE 3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRB2-RELATED ADAPTOR PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SH3 DOMAIN, RESIDUES 263-322;
COMPND 5 SYNONYM: GADS PROTEIN, GRBLG, GRB2L;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LYMPHOCYTE CYTOSOLIC PROTEIN 2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 226-235;
COMPND 11 SYNONYM: SLP-76;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL: T-LYMPHOCYTE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2TK;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PAED4
KEYWDS PROTEIN-BINDING, COMPLEX (SH3/PEPTIDE), T-CELL SIGNALING,
KEYWDS 2 SH3 DOMAIN, SH2 DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.LIU,D.BERRY,P.NASH,T.PAWSON,C.J.MCGLADE,S.S.LI
REVDAT 3 24-JUL-13 1H3H 1 SOURCE REMARK VERSN SCALE1
REVDAT 3 2 SCALE2
REVDAT 2 24-FEB-09 1H3H 1 VERSN
REVDAT 1 06-MAR-03 1H3H 0
JRNL AUTH Q.LIU,D.BERRY,P.NASH,T.PAWSON,C.J.MCGLADE,S.S.LI
JRNL TITL STRUCTURAL BASIS FOR SPECIFIC BINDING OF THE GADS
JRNL TITL 2 SH3 DOMAIN TO AN RXXK MOTIF-CONTAINING SLP-76
JRNL TITL 3 PEPTIDE: A NOVEL MODE OF PEPTIDE RECOGNITION
JRNL REF MOL.CELL V. 11 471 2003
JRNL REFN ISSN 1097-2765
JRNL PMID 12620234
JRNL DOI 10.1016/S1097-2765(03)00046-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.BERRY,P.NASH,S.LIU,T.PAWSON,C.MCGLADE
REMARK 1 TITL A HIGH-AFFINITY ARG-X-X-LYS SH3 BINDING MOTIF
REMARK 1 TITL 2 CONFERS SPECIFICITY FOR THE INTERACTION BETWEEN
REMARK 1 TITL 3 GADS AND SLP-76 IN T-CELL SIGNALING
REMARK 1 REF CURR.BIOL. V. 12 1336 2002
REMARK 1 REFN ISSN 0960-9822
REMARK 1 PMID 12176364
REMARK 1 DOI 10.1016/S0960-9822(02)01038-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.0
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-02.
REMARK 100 THE PDBE ID CODE IS EBI-11343.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100MM NACL, 50MM SODIUM
REMARK 210 PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB,CBCA(CO)NH,
REMARK 210 HCC(CO)NH,CC(CO)NH,HBCB(CRCD)HD,
REMARK 210 HBCB(CRCDCE)HE,HCCH-TOCSY,
REMARK 210 HNHA,15N/13C-EDITED NOESY,HALF-FILT
REMARK 210 15N/13C-EDITED NOESY,1H/13C-HSQC,1H
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.0
REMARK 210 METHOD USED : MDSA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C,15N-LABLED GADS C-TERMINAL SH3
REMARK 210 DOMAIN AND SLP-76 PEPTIDE.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
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 400
REMARK 400 COMPOUND
REMARK 400 GRB2-RELATED ADAPTOR PROTEIN 2: CHAIN A
REMARK 400 REGULATES NF-AT ACTIVATION BY INTERACTING WITH SLP-76.
REMARK 400 CONTAINS 1 SH2 DOMAIN AND 1 SH3 DOMAIN.
REMARK 400
REMARK 400 LYMPHOCYTE CYTOSOLIC PROTEIN 2: CHAIN B
REMARK 400 T CELL ANTIGEN RECEPTOR MEDIATED SIGNALING. INTERACTS
REMARK 400 WITH ADAPTER PROTEINS GRB2 AND FYB.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HD2 PHE A 27 - H ALA A 29 1.51
REMARK 500 HA GLU A 34 - H LEU A 64 1.44
REMARK 500 HZ PHE A 37 - HD2 PRO A 66 1.59
REMARK 500 HH11 ARG A 57 - HD22 LEU A 62 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 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 ARG A 19 38.19 -157.85
REMARK 500 1 ASP A 26 -176.78 -51.46
REMARK 500 1 ASN A 50 155.78 159.84
REMARK 500 1 SER A 52 -64.26 -170.84
REMARK 500 1 HIS A 59 -84.54 64.91
REMARK 500 1 PRO A 72 -178.55 -57.95
REMARK 500 1 PRO B 85 99.68 -46.48
REMARK 500 2 ARG A 17 90.98 58.92
REMARK 500 2 ARG A 19 48.06 -160.49
REMARK 500 2 ASP A 26 178.45 -47.65
REMARK 500 2 ASN A 50 161.32 163.45
REMARK 500 2 SER A 52 -42.70 -171.39
REMARK 500 2 HIS A 59 -84.93 65.53
REMARK 500 2 PRO A 72 -178.55 -60.61
REMARK 500 2 PRO B 85 103.12 -45.65
REMARK 500 3 ARG A 19 53.83 -156.30
REMARK 500 3 ASP A 26 -178.79 -51.55
REMARK 500 3 GLU A 34 -168.56 -110.92
REMARK 500 3 ASP A 47 96.15 -166.15
REMARK 500 3 ASN A 50 161.81 160.18
REMARK 500 3 SER A 52 -41.98 -164.84
REMARK 500 3 HIS A 59 -90.14 64.18
REMARK 500 3 PRO A 72 -178.53 -60.75
REMARK 500 3 PRO B 85 100.41 -43.24
REMARK 500 4 VAL A 18 93.31 -68.28
REMARK 500 4 ARG A 19 52.65 -157.00
REMARK 500 4 ASP A 26 -176.38 -51.16
REMARK 500 4 ASN A 50 158.54 160.08
REMARK 500 4 SER A 52 -38.33 -169.61
REMARK 500 4 HIS A 59 -84.86 65.66
REMARK 500 4 PRO A 72 -178.95 -63.07
REMARK 500 4 PRO B 85 101.66 -45.85
REMARK 500 5 ASP A 26 -172.00 -54.52
REMARK 500 5 GLU A 34 -169.48 -109.85
REMARK 500 5 ASP A 47 77.76 -151.62
REMARK 500 5 ASN A 50 165.29 162.09
REMARK 500 5 SER A 52 -33.92 -165.75
REMARK 500 5 HIS A 59 -81.78 65.87
REMARK 500 5 ASN A 60 10.46 -141.02
REMARK 500 5 PRO A 72 -179.78 -56.34
REMARK 500 5 LYS B 84 153.83 -49.78
REMARK 500 5 PRO B 85 102.96 -47.15
REMARK 500 6 ARG A 19 59.30 -152.79
REMARK 500 6 ASP A 26 -179.34 -51.24
REMARK 500 6 GLU A 34 -169.32 -103.14
REMARK 500 6 ASP A 47 85.94 -162.49
REMARK 500 6 ASN A 50 158.99 161.26
REMARK 500 6 SER A 52 -57.75 -172.24
REMARK 500 6 HIS A 59 -87.38 64.54
REMARK 500 6 PRO A 72 -177.73 -58.50
REMARK 500 6 PRO B 85 99.94 -45.28
REMARK 500 7 ASP A 26 178.76 -54.41
REMARK 500 7 ASP A 47 101.74 -160.51
REMARK 500 7 ASN A 50 161.11 162.08
REMARK 500 7 SER A 52 -41.53 -170.16
REMARK 500 7 HIS A 59 -82.19 64.67
REMARK 500 7 PRO A 72 -179.83 -57.59
REMARK 500 8 ARG A 17 94.51 60.60
REMARK 500 8 ASP A 26 -178.63 -52.78
REMARK 500 8 GLU A 34 -169.72 -107.51
REMARK 500 8 ASN A 50 156.18 161.55
REMARK 500 8 SER A 52 -60.39 -172.28
REMARK 500 8 HIS A 59 -85.39 65.26
REMARK 500 8 PRO A 72 178.88 -54.57
REMARK 500 9 ARG A 19 52.40 -148.84
REMARK 500 9 ASP A 26 -176.73 -53.46
REMARK 500 9 PHE A 37 -169.08 -113.01
REMARK 500 9 ASN A 50 155.60 160.91
REMARK 500 9 SER A 52 -57.23 -173.94
REMARK 500 9 HIS A 59 -77.53 65.47
REMARK 500 9 ASN A 60 12.28 -146.88
REMARK 500 9 PRO A 72 -178.98 -58.46
REMARK 500 10 ASP A 26 -173.57 -53.34
REMARK 500 10 ASP A 47 73.22 -165.99
REMARK 500 10 ASN A 50 161.80 162.18
REMARK 500 10 SER A 52 -54.23 -168.41
REMARK 500 10 HIS A 59 -84.60 66.66
REMARK 500 10 PRO B 77 101.11 -54.75
REMARK 500 11 ASP A 26 -178.74 -54.25
REMARK 500 11 ASN A 50 163.97 163.79
REMARK 500 11 SER A 52 -40.51 -168.91
REMARK 500 11 HIS A 59 -83.14 65.14
REMARK 500 11 ASN A 60 10.12 -140.51
REMARK 500 11 PRO A 72 -178.32 -61.87
REMARK 500 12 ASP A 26 -173.75 -54.30
REMARK 500 12 ASN A 50 161.90 162.93
REMARK 500 12 SER A 52 -46.55 -167.62
REMARK 500 12 HIS A 59 -85.87 65.52
REMARK 500 12 PRO A 72 178.97 -55.93
REMARK 500 13 ARG A 17 46.52 -141.19
REMARK 500 13 ARG A 19 43.05 -146.25
REMARK 500 13 ASP A 26 -175.92 -52.36
REMARK 500 13 ASN A 50 158.28 160.54
REMARK 500 13 SER A 52 -57.64 -171.99
REMARK 500 13 HIS A 59 -79.66 66.55
REMARK 500 13 PRO A 72 -178.56 -60.31
REMARK 500 13 PRO B 85 101.16 -48.28
REMARK 500 14 ARG A 19 51.90 -141.34
REMARK 500 14 ASP A 26 -175.98 -50.31
REMARK 500 14 ASP A 47 64.87 -158.68
REMARK 500 14 ASN A 50 163.35 162.80
REMARK 500 14 SER A 52 -38.72 -168.57
REMARK 500 14 HIS A 59 -85.73 65.15
REMARK 500 14 ASN A 60 10.98 -140.33
REMARK 500 14 PRO A 72 -179.63 -58.88
REMARK 500 14 PRO B 77 92.19 -53.23
REMARK 500 14 PRO B 85 101.49 -45.28
REMARK 500 15 ARG A 17 95.34 59.30
REMARK 500 15 ARG A 19 51.84 -152.47
REMARK 500 15 ASP A 26 -178.06 -53.07
REMARK 500 15 ASP A 33 20.53 -78.77
REMARK 500 15 ASN A 50 158.69 162.69
REMARK 500 15 SER A 52 -56.17 -171.27
REMARK 500 15 HIS A 59 -78.73 63.83
REMARK 500 15 ASN A 60 15.57 -145.82
REMARK 500 15 PRO B 85 104.29 -47.93
REMARK 500 16 ASP A 26 -172.07 -52.79
REMARK 500 16 ASP A 47 92.67 -163.27
REMARK 500 16 ASN A 50 158.75 158.98
REMARK 500 16 SER A 52 -58.23 -171.90
REMARK 500 16 HIS A 59 -85.97 65.00
REMARK 500 16 PRO A 72 -179.13 -57.19
REMARK 500 16 PRO B 85 101.74 -49.54
REMARK 500 17 ARG A 19 60.98 -160.72
REMARK 500 17 ASP A 26 -173.25 -55.38
REMARK 500 17 ASP A 47 -60.63 -143.99
REMARK 500 17 SER A 48 -1.96 58.95
REMARK 500 17 ASN A 50 161.27 161.04
REMARK 500 17 SER A 52 -57.58 -170.95
REMARK 500 17 HIS A 59 -85.11 64.54
REMARK 500 17 PRO A 72 -178.95 -57.39
REMARK 500 17 PRO B 85 102.92 -46.51
REMARK 500 18 ARG A 19 45.52 -142.22
REMARK 500 18 ASP A 26 -179.22 -50.17
REMARK 500 18 ASN A 50 158.29 160.73
REMARK 500 18 SER A 52 -60.61 -171.32
REMARK 500 18 HIS A 59 -67.52 56.19
REMARK 500 18 PRO A 72 -179.07 -57.26
REMARK 500 18 PRO B 77 104.68 -48.52
REMARK 500 18 PRO B 85 101.98 -48.61
REMARK 500 19 ARG A 19 55.57 -118.87
REMARK 500 19 ASP A 26 -179.68 -51.24
REMARK 500 19 ASP A 47 -65.33 -146.92
REMARK 500 19 SER A 48 -1.97 56.84
REMARK 500 19 ASN A 50 162.28 161.64
REMARK 500 19 SER A 52 -62.38 -170.17
REMARK 500 19 HIS A 59 -78.47 65.15
REMARK 500 19 ASN A 60 14.14 -145.07
REMARK 500 19 PRO A 72 176.42 -55.00
REMARK 500 19 PRO B 85 102.61 -45.09
REMARK 500 20 ARG A 19 61.62 -150.25
REMARK 500 20 ASP A 26 -177.27 -50.09
REMARK 500 20 GLU A 34 -168.84 -111.79
REMARK 500 20 ASP A 47 74.77 -158.02
REMARK 500 20 ASN A 50 162.01 161.50
REMARK 500 20 SER A 52 -38.95 -167.95
REMARK 500 20 HIS A 59 -77.90 64.32
REMARK 500 20 ASN A 60 17.00 -149.78
REMARK 500 20 PRO A 72 175.25 -53.35
REMARK 500 20 PRO B 85 99.33 -49.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
DBREF 1H3H A 16 75 UNP O89100 GRP2_MOUSE 263 322
DBREF 1H3H B 76 85 UNP Q13094 LCP2_HUMAN 226 235
DBREF 1H3H B 86 86 PDB 1H3H 1H3H 86 86
SEQRES 1 A 60 GLY ARG VAL ARG TRP ALA ARG ALA LEU TYR ASP PHE GLU
SEQRES 2 A 60 ALA LEU GLU GLU ASP GLU LEU GLY PHE ARG SER GLY GLU
SEQRES 3 A 60 VAL VAL GLU VAL LEU ASP SER SER ASN PRO SER TRP TRP
SEQRES 4 A 60 THR GLY ARG LEU HIS ASN LYS LEU GLY LEU PHE PRO ALA
SEQRES 5 A 60 ASN TYR VAL ALA PRO MET MET ARG
SEQRES 1 B 11 ALA PRO SER ILE ASP ARG SER THR LYS PRO ALA
HELIX 1 1 ARG B 81 THR B 83 5 3
SHEET 1 BB 5 VAL A 70 PRO A 72 0
SHEET 2 BB 5 ALA A 21 ALA A 23 -1 O ARG A 22 N ALA A 71
SHEET 3 BB 5 GLU A 41 LEU A 46 -1 O VAL A 43 N ALA A 21
SHEET 4 BB 5 TRP A 53 LEU A 58 -1 O THR A 55 N LEU A 46
SHEET 5 BB 5 LYS A 61 PRO A 66 -1 O LYS A 61 N LEU A 58
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 - l 24 2 Bytes