Header list of 1l2z.pdb file
Complete list - b 23 2 Bytes
HEADER PEPTIDE BINDING/SIGNALING PROTEIN 26-FEB-02 1L2Z
TITLE CD2BP2-GYF DOMAIN IN COMPLEX WITH PROLINE-RICH CD2 TAIL SEGMENT
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD2 ANTIGEN (CYTOPLASMIC TAIL)-BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUE 1-62;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: T-CELL SURFACE ANTIGEN CD2;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUE 63-73;
COMPND 10 SYNONYM: T-CELL SURFACE ANTIGEN T11/LEU-5, LFA-2, LFA-3 RECEPTOR,
COMPND 11 ERYTHROCYTE RECEPTOR, ROSETTE RECEPTOR;
COMPND 12 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: CD2BP2 (AMINO ACIDS 280-341);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PTFT74;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 14 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS GYF DOMAIN, PROTEIN-PROTEIN INTERACTION, PROLINE-RICH PEPTIDE, CD2,
KEYWDS 2 CD2BP2, PEPTIDE BINDING-SIGNALING PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.FREUND,R.KUHNE,H.YANG,S.PARK,E.L.REINHERZ,G.WAGNER
REVDAT 3 23-FEB-22 1L2Z 1 REMARK
REVDAT 2 24-FEB-09 1L2Z 1 VERSN
REVDAT 1 20-NOV-02 1L2Z 0
JRNL AUTH C.FREUND,R.KUHNE,H.YANG,S.PARK,E.L.REINHERZ,G.WAGNER
JRNL TITL DYNAMIC INTERACTION OF CD2 WITH THE GYF AND THE SH3 DOMAIN
JRNL TITL 2 OF COMPARTMENTALIZED EFFECTOR MOLECULES
JRNL REF EMBO J. V. 21 5985 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12426371
JRNL DOI 10.1093/EMBOJ/CDF602
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 1000K, FORCE CONSTANT NOE 50 KCAL MOL-1A-2, FORCE CONSTANT
REMARK 3 DIHEDRAL ANGLES 200 KCAL MOL-1 RAD-2, 1000 STEPS MINIMIZATION,
REMARK 3 INTERMOLECULAR NOES 33, INTRAMOLECULAR NOES (PEPTIDE) 49,
REMARK 3 INTRAMOLECULAR NOES (GYF DOMAIN) 754
REMARK 4
REMARK 4 1L2Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.3; 6.3
REMARK 210 IONIC STRENGTH : 50 MM NAPO4; 50 MM NAPO4
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM GYF DOMAIN U-DEUTERATED, U
REMARK 210 -15N, 1MM PEPTIDE, 50 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.3, 100%
REMARK 210 D2O; 1 MM GYF DOMAIN, AROMATIC
REMARK 210 AMINO ACIDS PROTONATED ONLY, 1
REMARK 210 MM PEPTIDE PROTONATED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 2D TOCSY; 3D 15N EDITED
REMARK 210 TOCSY; 15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, PROSA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 THR A 27 H GLU A 31 1.52
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 A 14 163.75 -43.01
REMARK 500 1 ARG A 41 137.41 -170.40
REMARK 500 1 GLN A 49 75.56 -67.00
REMARK 500 1 PHE A 50 163.81 -42.15
REMARK 500 1 TYR A 61 -46.10 -142.78
REMARK 500 1 PRO B 69 -179.44 -61.42
REMARK 500 1 HIS B 71 -163.79 41.98
REMARK 500 1 ARG B 72 106.63 176.05
REMARK 500 2 ALA A 14 159.11 -42.21
REMARK 500 2 TYR A 17 -166.10 -114.30
REMARK 500 2 PHE A 34 62.38 62.90
REMARK 500 2 ARG A 41 138.27 -178.28
REMARK 500 2 GLN A 49 77.14 -67.38
REMARK 500 2 PHE A 50 144.43 -31.87
REMARK 500 2 TYR A 61 -46.57 -138.27
REMARK 500 2 PRO B 69 -178.06 -59.69
REMARK 500 2 HIS B 71 -167.19 45.02
REMARK 500 2 ARG B 72 135.54 176.09
REMARK 500 3 ASN A 10 40.12 -97.88
REMARK 500 3 ALA A 14 178.09 -51.18
REMARK 500 3 TYR A 17 -164.49 -111.31
REMARK 500 3 PHE A 34 78.67 -105.35
REMARK 500 3 ARG A 41 141.88 -178.85
REMARK 500 3 GLN A 49 74.55 -67.11
REMARK 500 3 PHE A 50 159.88 -44.27
REMARK 500 3 TYR A 61 -62.71 -140.09
REMARK 500 3 PRO B 69 -179.21 -65.14
REMARK 500 3 HIS B 71 -165.26 43.34
REMARK 500 3 ARG B 72 92.39 174.73
REMARK 500 4 GLU A 15 179.31 -58.40
REMARK 500 4 TYR A 17 -161.91 -107.73
REMARK 500 4 GLN A 49 72.65 -68.71
REMARK 500 4 PHE A 50 160.07 -47.45
REMARK 500 4 ASP A 57 79.32 -107.63
REMARK 500 4 TYR A 61 -52.23 -145.28
REMARK 500 4 PRO B 69 -179.57 -62.10
REMARK 500 4 HIS B 71 120.88 66.31
REMARK 500 5 ASN A 10 39.74 -98.12
REMARK 500 5 ALA A 14 163.04 -45.76
REMARK 500 5 TYR A 17 -163.49 -111.02
REMARK 500 5 PRO A 19 28.68 -79.02
REMARK 500 5 ARG A 41 142.42 -175.20
REMARK 500 5 GLN A 49 75.16 -66.42
REMARK 500 5 PHE A 50 158.77 -42.80
REMARK 500 5 TYR A 61 -51.71 -140.19
REMARK 500 5 HIS B 64 -41.89 -166.28
REMARK 500 5 PRO B 69 -178.39 -59.36
REMARK 500 5 HIS B 71 -167.26 44.81
REMARK 500 5 ARG B 72 88.85 178.81
REMARK 500 6 GLU A 15 -176.80 -56.90
REMARK 500
REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GYF RELATED DB: PDB
REMARK 900 GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN
DBREF 1L2Z A 1 62 UNP O95400 CD2B2_HUMAN 280 341
DBREF 1L2Z B 63 73 UNP P06729 CD2_HUMAN 294 304
SEQRES 1 A 62 ASP VAL MET TRP GLU TYR LYS TRP GLU ASN THR GLY ASP
SEQRES 2 A 62 ALA GLU LEU TYR GLY PRO PHE THR SER ALA GLN MET GLN
SEQRES 3 A 62 THR TRP VAL SER GLU GLY TYR PHE PRO ASP GLY VAL TYR
SEQRES 4 A 62 CYS ARG LYS LEU ASP PRO PRO GLY GLY GLN PHE TYR ASN
SEQRES 5 A 62 SER LYS ARG ILE ASP PHE ASP LEU TYR THR
SEQRES 1 B 11 SER HIS ARG PRO PRO PRO PRO GLY HIS ARG VAL
HELIX 1 1 THR A 21 GLY A 32 1 12
HELIX 2 2 LYS A 54 ILE A 56 5 3
HELIX 3 3 ASP A 57 TYR A 61 5 5
SHEET 1 A 3 GLU A 5 LYS A 7 0
SHEET 2 A 3 TYR A 39 ARG A 41 -1 O TYR A 39 N LYS A 7
SHEET 3 A 3 TYR A 51 ASN A 52 -1 O TYR A 51 N CYS A 40
CISPEP 1 ASP A 44 PRO A 45 1 0.03
CISPEP 2 ASP A 44 PRO A 45 2 0.03
CISPEP 3 ASP A 44 PRO A 45 3 -0.02
CISPEP 4 ASP A 44 PRO A 45 4 -0.01
CISPEP 5 ASP A 44 PRO A 45 5 -0.08
CISPEP 6 ASP A 44 PRO A 45 6 -0.05
CISPEP 7 ASP A 44 PRO A 45 7 -0.11
CISPEP 8 ASP A 44 PRO A 45 8 -0.06
CISPEP 9 ASP A 44 PRO A 45 9 0.12
CISPEP 10 ASP A 44 PRO A 45 10 0.17
CISPEP 11 ASP A 44 PRO A 45 11 -0.01
CISPEP 12 ASP A 44 PRO A 45 12 0.00
CISPEP 13 ASP A 44 PRO A 45 13 -0.04
CISPEP 14 ASP A 44 PRO A 45 14 0.11
CISPEP 15 ASP A 44 PRO A 45 15 0.00
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 - b 23 2 Bytes