Header list of 2ain.pdb file
Complete list - r 9 2 Bytes
HEADER CELL ADHESION/TRANSFERASE 30-JUL-05 2AIN
TITLE SOLUTION STRUCTURE OF THE AF-6 PDZ DOMAIN COMPLEXED WITH THE C-
TITLE 2 TERMINAL PEPTIDE FROM THE BCR PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AFADIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AF-6 PDZ DOMAIN;
COMPND 5 SYNONYM: AF-6 PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 6-MER PEPTIDE FROM BREAKPOINT CLUSTER REGION PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: C-TERMINAL PEPTIDE;
COMPND 11 EC: 2.7.1.-;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B (+);
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS AF-6 PDZ DOMAIN-BCR COMPLEX, CELL ADHESION-TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.CHEN,J.WU,Y.SHI
REVDAT 4 09-MAR-22 2AIN 1 REMARK SEQADV
REVDAT 3 19-JAN-10 2AIN 1 JRNL
REVDAT 2 24-FEB-09 2AIN 1 VERSN
REVDAT 1 18-JUL-06 2AIN 0
JRNL AUTH Q.CHEN,X.NIU,Y.XU,J.WU,Y.SHI
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE AF-6 PDZ
JRNL TITL 2 DOMAIN/BCR PEPTIDE COMPLEX.
JRNL REF PROTEIN SCI. V. 16 1053 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17473018
JRNL DOI 10.1110/PS.062440607
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.1
REMARK 3 AUTHORS : F.DELAGLIO (NMRPIPE),
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: THE COMPLEX STRUCTURE IS SOLVED USING A
REMARK 3 TOTAL OF 1606 EXPERIMENTAL RESTRAINTS THAT INCLUDES 1471
REMARK 3 INTRAMOLECULAR NOES, 61 INTERMOLECULAR NOES AND 74 DIHEDRAL
REMARK 3 ANGLES RESTRAINTS
REMARK 4
REMARK 4 2AIN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033938.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.0MM 15N, 13C-LABELED AF-6 PDZ
REMARK 210 DOMAIN, 50MM PHOSPHATE BUFFER
REMARK 210 (PH 5.9), 1MM EDTA, 10%(V/V) D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3, CNS 1.1, CSI 1.0,
REMARK 210 MOLMOL 2K.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: INTERMOLECULAR INTERACTIONS WERE IDENTIFIED IN A 13C/15N
REMARK 210 -FILTERED (F1), 13C-EDITED(F3) 3D NOESY SPECTRUM
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: 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 LYS A 2 41.43 -159.49
REMARK 500 1 GLU A 3 98.97 62.18
REMARK 500 1 PRO A 4 -173.77 -67.31
REMARK 500 1 ASN A 15 37.42 -168.41
REMARK 500 1 ARG A 50 -61.87 -133.16
REMARK 500 1 LEU A 58 -59.31 -126.52
REMARK 500 1 ARG A 79 43.93 -82.96
REMARK 500 2 LYS A 2 -174.31 62.55
REMARK 500 2 PRO A 4 -164.42 -62.66
REMARK 500 2 LYS A 13 96.75 -68.26
REMARK 500 2 ALA A 44 -60.47 -95.25
REMARK 500 2 ARG A 50 30.79 -141.02
REMARK 500 2 ARG A 79 44.45 -92.42
REMARK 500 2 SER A 81 -164.66 -103.07
REMARK 500 3 PRO A 4 -178.53 -58.36
REMARK 500 3 GLN A 14 -60.75 -92.11
REMARK 500 3 ASN A 15 36.38 -157.86
REMARK 500 3 LEU A 65 42.22 -109.11
REMARK 500 3 ARG A 79 42.67 -91.31
REMARK 500 3 SER B 101 100.84 179.53
REMARK 500 4 LYS A 2 82.50 63.54
REMARK 500 4 PRO A 4 -171.47 -62.50
REMARK 500 4 ASN A 15 44.82 -163.68
REMARK 500 4 LEU A 58 -58.83 -122.41
REMARK 500 4 VAL A 66 83.62 -68.88
REMARK 500 4 THR B 102 -151.89 -98.96
REMARK 500 4 GLU B 103 44.89 -174.11
REMARK 500 5 ASN A 15 42.86 -161.58
REMARK 500 5 LEU A 58 -55.95 -127.00
REMARK 500 5 ARG A 79 32.82 -96.47
REMARK 500 5 PHE B 100 31.58 -170.54
REMARK 500 5 SER B 101 43.45 168.98
REMARK 500 6 ASN A 15 38.11 -158.99
REMARK 500 6 SER A 38 125.54 -178.00
REMARK 500 6 LEU A 58 -55.52 -140.21
REMARK 500 6 LEU A 65 43.67 -96.33
REMARK 500 6 ARG A 79 47.48 -84.20
REMARK 500 7 PRO A 4 -166.02 -62.71
REMARK 500 7 SER A 38 137.83 -175.34
REMARK 500 7 LEU A 58 -53.26 -141.48
REMARK 500 7 LYS A 90 91.37 -69.02
REMARK 500 7 PHE B 100 94.03 70.05
REMARK 500 7 SER B 101 -50.90 -154.23
REMARK 500 7 THR B 102 -172.74 53.65
REMARK 500 7 GLU B 103 51.94 179.35
REMARK 500 8 PRO A 4 -172.18 -69.98
REMARK 500 8 GLN A 14 -58.66 -131.98
REMARK 500 8 ARG A 50 -66.99 -128.24
REMARK 500 8 LEU A 58 -59.02 -148.18
REMARK 500 8 VAL A 66 73.43 -107.39
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T2M RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE AF-6 PDZ DOMAIN
DBREF 2AIN A 2 93 UNP P55196 AFAD_HUMAN 987 1077
DBREF 2AIN B 99 104 UNP P11274 BCR_HUMAN 1266 1271
SEQADV 2AIN MET A 1 UNP P55196 INITIATING METHIONINE
SEQRES 1 A 93 MET LYS GLU PRO GLU ILE ILE THR VAL THR LEU LYS LYS
SEQRES 2 A 93 GLN ASN GLY MET GLY LEU SER ILE VAL ALA ALA LYS GLY
SEQRES 3 A 93 ALA GLY GLN ASP LYS LEU GLY ILE TYR VAL LYS SER VAL
SEQRES 4 A 93 VAL LYS GLY GLY ALA ALA ASP VAL ASP GLY ARG LEU ALA
SEQRES 5 A 93 ALA GLY ASP GLN LEU LEU SER VAL ASP GLY ARG SER LEU
SEQRES 6 A 93 VAL GLY LEU SER GLN GLU ARG ALA ALA GLU LEU MET THR
SEQRES 7 A 93 ARG THR SER SER VAL VAL THR LEU GLU VAL ALA LYS GLN
SEQRES 8 A 93 GLY ALA
SEQRES 1 B 6 LEU PHE SER THR GLU VAL
HELIX 1 1 GLY A 43 GLY A 49 1 7
HELIX 2 2 SER A 69 ARG A 79 1 11
SHEET 1 A 4 GLU A 5 LYS A 12 0
SHEET 2 A 4 VAL A 83 LYS A 90 -1 O VAL A 88 N ILE A 7
SHEET 3 A 4 GLN A 56 VAL A 60 -1 N SER A 59 O GLU A 87
SHEET 4 A 4 ARG A 63 SER A 64 -1 O ARG A 63 N VAL A 60
SHEET 1 B 3 GLY A 33 VAL A 39 0
SHEET 2 B 3 LEU A 19 ALA A 24 -1 N SER A 20 O SER A 38
SHEET 3 B 3 SER B 101 VAL B 104 -1 O THR B 102 N ILE A 21
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