Header list of 1u2n.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 19-JUL-04 1U2N
TITLE STRUCTURE CBP TAZ1 DOMAIN
CAVEAT 1U2N CHIRALITY ERROR AT THE CA CENTER OF CYS A 421 IN MODEL 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CBP TAZ1 DOMAIN;
COMPND 5 EC: 2.3.1.48;
COMPND 6 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 GENE: CBP;
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: PET21A
KEYWDS TAZ1, CBP, TAZ2, P300, CH1, CH3, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.N.DE GUZMAN,J.M.WOJCIAK,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
REVDAT 3 02-MAR-22 1U2N 1 REMARK LINK
REVDAT 2 24-FEB-09 1U2N 1 VERSN
REVDAT 1 26-APR-05 1U2N 0
JRNL AUTH R.N.DE GUZMAN,J.M.WOJCIAK,M.A.MARTINEZ-YAMOUT,H.J.DYSON,
JRNL AUTH 2 P.E.WRIGHT
JRNL TITL CBP/P300 TAZ1 DOMAIN FORMS A STRUCTURED SCAFFOLD FOR LIGAND
JRNL TITL 2 BINDING
JRNL REF BIOCHEMISTRY V. 44 490 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15641773
JRNL DOI 10.1021/BI048161T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 7
REMARK 3 AUTHORS : GUNTERT, P. ET AL. (DYANA), CASE, D. ET AL.
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U2N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023167.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM N15 TAZ1; 10MM TRIS-D11 PH
REMARK 210 6.9; 50MM NACL; 2MM DTT; 1MM C13,
REMARK 210 N15 TAZ1; 10MM TRIS-D11 PH 6.9;
REMARK 210 50MM NACL; 2MM DTT; 1MM C13,N15
REMARK 210 TAZ1; 10MM TRIS-D11 PH 6.9; 50MM
REMARK 210 NACL; 2MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2003
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS BY DYANA,
REMARK 210 SIMULATED ANNEALING AND
REMARK 210 MOLECULAR DYNAMICS BY AMBER
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 PRO A 400 CB CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 423 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 1 CYS A 426 CB - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 2 ARG A 369 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 423 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 5 ARG A 377 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 368 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 377 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 GLN A 404 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 7 ARG A 439 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 PRO A 400 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 10 ARG A 368 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 PRO A 400 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 10 CYS A 426 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 12 ARG A 385 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 412 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 CYS A 426 CB - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 14 ARG A 423 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 15 CYS A 366 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 16 ARG A 350 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 368 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 385 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 439 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 19 CYS A 366 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 19 ARG A 369 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 ARG A 385 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 19 ARG A 412 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 19 CYS A 426 CB - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 20 ARG A 423 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
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 PRO A 343 47.95 -71.47
REMARK 500 1 PRO A 400 -71.19 63.31
REMARK 500 1 GLN A 404 -9.88 -30.93
REMARK 500 1 ARG A 423 -17.37 0.13
REMARK 500 1 ASP A 425 48.77 -154.80
REMARK 500 2 THR A 344 -7.27 -56.97
REMARK 500 2 ARG A 377 49.68 -71.14
REMARK 500 2 ALA A 399 -45.83 -142.60
REMARK 500 2 PRO A 400 -67.01 61.44
REMARK 500 2 CYS A 403 43.47 -80.25
REMARK 500 2 GLN A 404 -9.94 -28.55
REMARK 500 2 ASP A 425 48.88 -149.71
REMARK 500 2 VAL A 428 -45.96 -130.03
REMARK 500 3 ASN A 373 -41.01 -163.17
REMARK 500 3 GLU A 375 -39.43 -143.48
REMARK 500 3 ALA A 399 -39.93 -151.34
REMARK 500 3 PRO A 400 -66.98 59.85
REMARK 500 3 GLN A 404 -9.86 -35.46
REMARK 500 4 ALA A 345 112.89 -178.19
REMARK 500 4 ASN A 373 -13.93 -152.91
REMARK 500 4 VAL A 376 47.02 -80.14
REMARK 500 4 ALA A 399 -40.36 -147.92
REMARK 500 4 PRO A 400 -66.93 57.78
REMARK 500 4 GLN A 404 -9.85 -36.59
REMARK 500 4 ARG A 423 -18.25 0.67
REMARK 500 4 ASP A 425 46.67 -153.99
REMARK 500 4 VAL A 428 -43.81 -131.74
REMARK 500 4 LYS A 438 39.36 -166.65
REMARK 500 5 ASP A 346 88.86 -152.89
REMARK 500 5 ALA A 378 25.31 -145.46
REMARK 500 5 PRO A 400 -68.23 61.94
REMARK 500 5 GLN A 404 -10.00 -32.88
REMARK 500 5 ASP A 425 44.06 -145.28
REMARK 500 6 ALA A 345 30.01 -151.55
REMARK 500 6 ARG A 377 11.30 -69.64
REMARK 500 6 SER A 380 -3.92 -140.44
REMARK 500 6 PRO A 400 -67.93 59.59
REMARK 500 6 GLN A 404 -9.82 -37.56
REMARK 500 6 PRO A 427 -9.85 -56.59
REMARK 500 6 SER A 436 36.33 -76.08
REMARK 500 7 ASN A 373 89.62 -170.19
REMARK 500 7 PRO A 400 -68.29 60.44
REMARK 500 7 GLN A 404 -9.96 -20.03
REMARK 500 7 ASP A 425 46.18 -142.82
REMARK 500 7 VAL A 428 -43.57 -133.26
REMARK 500 7 LYS A 438 67.37 -150.97
REMARK 500 8 THR A 341 48.08 -82.88
REMARK 500 8 ASP A 346 113.78 -31.17
REMARK 500 8 ASN A 373 -11.40 -161.84
REMARK 500 8 PRO A 400 -63.81 57.78
REMARK 500
REMARK 500 THIS ENTRY HAS 153 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 HIS A 417 0.10 SIDE CHAIN
REMARK 500 4 HIS A 417 0.10 SIDE CHAIN
REMARK 500 7 HIS A 393 0.13 SIDE CHAIN
REMARK 500 9 HIS A 417 0.10 SIDE CHAIN
REMARK 500 10 HIS A 417 0.10 SIDE CHAIN
REMARK 500 13 HIS A 417 0.12 SIDE CHAIN
REMARK 500 14 HIS A 417 0.12 SIDE CHAIN
REMARK 500 15 HIS A 417 0.09 SIDE CHAIN
REMARK 500 16 HIS A 417 0.09 SIDE CHAIN
REMARK 500 17 HIS A 417 0.10 SIDE CHAIN
REMARK 500 18 HIS A 417 0.09 SIDE CHAIN
REMARK 500 19 HIS A 417 0.12 SIDE CHAIN
REMARK 500 20 HIS A 417 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 440 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 362 NE2
REMARK 620 2 CYS A 366 SG 112.7
REMARK 620 3 CYS A 379 SG 106.4 109.7
REMARK 620 4 CYS A 384 SG 106.9 110.8 110.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 441 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 393 NE2
REMARK 620 2 CYS A 397 SG 112.4
REMARK 620 3 CYS A 403 SG 110.0 104.5
REMARK 620 4 CYS A 408 SG 107.7 113.0 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 442 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 417 NE2
REMARK 620 2 CYS A 421 SG 106.4
REMARK 620 3 CYS A 426 SG 108.3 113.1
REMARK 620 4 CYS A 429 SG 113.3 110.0 105.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 440
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 442
DBREF 1U2N A 340 439 UNP P45481 CBP_MOUSE 340 439
SEQRES 1 A 100 ALA THR GLY PRO THR ALA ASP PRO GLU LYS ARG LYS LEU
SEQRES 2 A 100 ILE GLN GLN GLN LEU VAL LEU LEU LEU HIS ALA HIS LYS
SEQRES 3 A 100 CYS GLN ARG ARG GLU GLN ALA ASN GLY GLU VAL ARG ALA
SEQRES 4 A 100 CYS SER LEU PRO HIS CYS ARG THR MET LYS ASN VAL LEU
SEQRES 5 A 100 ASN HIS MET THR HIS CYS GLN ALA PRO LYS ALA CYS GLN
SEQRES 6 A 100 VAL ALA HIS CYS ALA SER SER ARG GLN ILE ILE SER HIS
SEQRES 7 A 100 TRP LYS ASN CYS THR ARG HIS ASP CYS PRO VAL CYS LEU
SEQRES 8 A 100 PRO LEU LYS ASN ALA SER ASP LYS ARG
HET ZN A 440 1
HET ZN A 441 1
HET ZN A 442 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
HELIX 1 1 ASP A 346 ALA A 372 1 27
HELIX 2 2 LEU A 381 CYS A 397 1 17
HELIX 3 3 VAL A 405 CYS A 421 1 17
HELIX 4 4 VAL A 428 ALA A 435 1 8
LINK NE2 HIS A 362 ZN ZN A 440 1555 1555 2.09
LINK SG CYS A 366 ZN ZN A 440 1555 1555 2.31
LINK SG CYS A 379 ZN ZN A 440 1555 1555 2.29
LINK SG CYS A 384 ZN ZN A 440 1555 1555 2.29
LINK NE2 HIS A 393 ZN ZN A 441 1555 1555 2.09
LINK SG CYS A 397 ZN ZN A 441 1555 1555 2.30
LINK SG CYS A 403 ZN ZN A 441 1555 1555 2.29
LINK SG CYS A 408 ZN ZN A 441 1555 1555 2.30
LINK NE2 HIS A 417 ZN ZN A 442 1555 1555 2.09
LINK SG CYS A 421 ZN ZN A 442 1555 1555 2.30
LINK SG CYS A 426 ZN ZN A 442 1555 1555 2.29
LINK SG CYS A 429 ZN ZN A 442 1555 1555 2.29
SITE 1 AC1 4 HIS A 362 CYS A 366 CYS A 379 CYS A 384
SITE 1 AC2 4 HIS A 393 CYS A 397 CYS A 403 CYS A 408
SITE 1 AC3 4 HIS A 417 CYS A 421 CYS A 426 CYS A 429
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 2 2 Bytes