HEADER TRANSCRIPTION/DNA 16-JUN-05 2A07
TITLE CRYSTAL STRUCTURE OF FOXP2 BOUND SPECIFICALLY TO DNA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*AP*AP*CP*TP*AP*TP*GP*AP*AP*AP*CP*AP*AP*AP*TP*TP*TP*TP
COMPND 3 *CP*CP*T)-3';
COMPND 4 CHAIN: A, C;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PROMOTER ELEMENT OF A FOXP REGULATED GENE, PLUS
COMPND 7 STRAND;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5'-D(*TP*TP*AP*GP*GP*AP*AP*AP*AP*TP*TP*TP*GP*TP*TP*TP*CP*AP
COMPND 10 *TP*AP*G)-3';
COMPND 11 CHAIN: B, D;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: PROMOTER ELEMENT OF A FOXP REGULATED GENE, MINUS
COMPND 14 STRAND;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: FORKHEAD BOX PROTEIN P2;
COMPND 17 CHAIN: F, G, H, I, J, K;
COMPND 18 FRAGMENT: FOXP2 FORKHEAD DOMAIN;
COMPND 19 SYNONYM: CAG REPEAT PROTEIN 44, TRINUCLEOTIDE REPEAT-CONTAINING GENE
COMPND 20 10 PROTEIN;
COMPND 21 ENGINEERED: YES;
COMPND 22 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: DNA IS SYNTHESIZED BY SOLID PHASE METHOD;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 OTHER_DETAILS: DNA IS SYNTHESIZED BY SOLID PHASE METHOD;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: FOXP2, CAGH44, TNRC10;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FORKHEAD, DOUBLE-HELIX, SWAPPING, HOMODIMER, MONOMER, WINGED-HELIX,
KEYWDS 2 MAGNESIUM, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.STROUD,Y.WU,D.L.BATES,A.HAN,K.NOWICK,S.PAABO,H.TONG,L.CHEN
REVDAT 4 14-FEB-24 2A07 1 REMARK
REVDAT 3 20-OCT-21 2A07 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2A07 1 VERSN
REVDAT 1 31-JAN-06 2A07 0
JRNL AUTH J.C.STROUD,Y.WU,D.L.BATES,A.HAN,K.NOWICK,S.PAABO,H.TONG,
JRNL AUTH 2 L.CHEN
JRNL TITL STRUCTURE OF THE FORKHEAD DOMAIN OF FOXP2 BOUND TO DNA.
JRNL REF STRUCTURE V. 14 159 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16407075
JRNL DOI 10.1016/J.STR.2005.10.005
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 73908
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7443
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4149
REMARK 3 NUCLEIC ACID ATOMS : 1710
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 581
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.067
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.99
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.953
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.68
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07810
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79203
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 8.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BTP, SODIUM CHLORIDE, PEG 3K,
REMARK 280 MAGNESIUM CHLORIDE, SODIUM AZIDE, PH 6.68, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 62.10500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G, H, I, J, K
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ILE F 502
REMARK 465 SER F 585
REMARK 465 GLN F 586
REMARK 465 LYS F 587
REMARK 465 ILE F 588
REMARK 465 THR F 589
REMARK 465 GLY F 590
REMARK 465 SER F 591
REMARK 465 PRO F 592
REMARK 465 THR F 593
REMARK 465 LEU F 594
REMARK 465 ILE G 502
REMARK 465 VAL G 503
REMARK 465 ARG G 504
REMARK 465 PRO G 505
REMARK 465 SER G 585
REMARK 465 GLN G 586
REMARK 465 LYS G 587
REMARK 465 ILE G 588
REMARK 465 THR G 589
REMARK 465 GLY G 590
REMARK 465 SER G 591
REMARK 465 PRO G 592
REMARK 465 THR G 593
REMARK 465 LEU G 594
REMARK 465 ILE H 502
REMARK 465 VAL H 503
REMARK 465 ARG H 504
REMARK 465 PRO H 505
REMARK 465 SER H 585
REMARK 465 GLN H 586
REMARK 465 LYS H 587
REMARK 465 ILE H 588
REMARK 465 THR H 589
REMARK 465 GLY H 590
REMARK 465 SER H 591
REMARK 465 PRO H 592
REMARK 465 THR H 593
REMARK 465 LEU H 594
REMARK 465 ILE I 502
REMARK 465 ARG I 584
REMARK 465 SER I 585
REMARK 465 GLN I 586
REMARK 465 LYS I 587
REMARK 465 ILE I 588
REMARK 465 THR I 589
REMARK 465 GLY I 590
REMARK 465 SER I 591
REMARK 465 PRO I 592
REMARK 465 THR I 593
REMARK 465 LEU I 594
REMARK 465 SER J 585
REMARK 465 GLN J 586
REMARK 465 LYS J 587
REMARK 465 ILE J 588
REMARK 465 THR J 589
REMARK 465 GLY J 590
REMARK 465 SER J 591
REMARK 465 PRO J 592
REMARK 465 THR J 593
REMARK 465 LEU J 594
REMARK 465 SER K 585
REMARK 465 GLN K 586
REMARK 465 LYS K 587
REMARK 465 ILE K 588
REMARK 465 THR K 589
REMARK 465 GLY K 590
REMARK 465 SER K 591
REMARK 465 PRO K 592
REMARK 465 THR K 593
REMARK 465 LEU K 594
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 ASN F 567 -150.41 -111.03
REMARK 500 VAL F 568 -98.53 -39.44
REMARK 500 TRP F 573 -158.70 -90.12
REMARK 500 THR F 574 168.30 170.11
REMARK 500 ASN G 567 -155.38 -104.03
REMARK 500 VAL G 568 -86.69 -43.00
REMARK 500 GLU H 519 70.88 -108.07
REMARK 500 ASP H 522 0.16 95.48
REMARK 500 ASN H 567 -154.25 -104.43
REMARK 500 VAL H 568 -86.79 -43.82
REMARK 500 ASN I 567 -167.02 -109.57
REMARK 500 LYS I 569 -33.38 -155.82
REMARK 500 ALA I 571 128.37 -171.46
REMARK 500 ARG J 583 -12.08 81.31
REMARK 500 ARG K 583 -1.29 77.66
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 DT B 1 0.06 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 MG K 606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 24 O
REMARK 620 2 LEU K 556 O 93.7
REMARK 620 3 SER K 557 O 74.6 80.7
REMARK 620 4 HIS K 559 O 164.4 94.7 93.9
REMARK 620 5 PHE K 562 O 98.1 100.8 172.7 93.1
REMARK 620 6 HOH K 645 O 73.2 149.3 69.2 93.1 108.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER F 557 O
REMARK 620 2 LEU F 558 O 92.1
REMARK 620 3 HOH F 613 O 113.7 130.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU G 556 O
REMARK 620 2 HIS G 559 O 96.0
REMARK 620 3 PHE G 562 O 100.8 90.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H 397 O
REMARK 620 2 LEU H 556 O 94.9
REMARK 620 3 HIS H 559 O 172.7 91.7
REMARK 620 4 PHE H 562 O 93.2 95.5 89.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER I 557 O
REMARK 620 2 HIS I 559 O 127.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU J 556 O
REMARK 620 2 HIS J 559 O 96.3
REMARK 620 3 PHE J 562 O 101.7 92.6
REMARK 620 4 HOH J 673 O 151.0 94.4 104.7
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 MG F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 606
DBREF 2A07 F 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 G 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 H 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 I 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 J 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 K 502 594 UNP O15409 FOXP2_HUMAN 502 594
DBREF 2A07 A 1 21 PDB 2A07 2A07 1 21
DBREF 2A07 B 1 21 PDB 2A07 2A07 1 21
DBREF 2A07 C 1 21 PDB 2A07 2A07 1 21
DBREF 2A07 D 1 21 PDB 2A07 2A07 1 21
SEQADV 2A07 ILE F 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQADV 2A07 ILE G 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQADV 2A07 ILE H 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQADV 2A07 ILE I 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQADV 2A07 ILE J 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQADV 2A07 ILE K 502 UNP O15409 ASP 502 ENGINEERED MUTATION
SEQRES 1 A 21 DA DA DC DT DA DT DG DA DA DA DC DA DA
SEQRES 2 A 21 DA DT DT DT DT DC DC DT
SEQRES 1 B 21 DT DT DA DG DG DA DA DA DA DT DT DT DG
SEQRES 2 B 21 DT DT DT DC DA DT DA DG
SEQRES 1 C 21 DA DA DC DT DA DT DG DA DA DA DC DA DA
SEQRES 2 C 21 DA DT DT DT DT DC DC DT
SEQRES 1 D 21 DT DT DA DG DG DA DA DA DA DT DT DT DG
SEQRES 2 D 21 DT DT DT DC DA DT DA DG
SEQRES 1 F 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 F 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 F 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 F 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 F 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 F 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 F 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 F 93 THR LEU
SEQRES 1 G 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 G 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 G 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 G 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 G 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 G 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 G 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 G 93 THR LEU
SEQRES 1 H 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 H 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 H 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 H 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 H 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 H 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 H 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 H 93 THR LEU
SEQRES 1 I 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 I 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 I 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 I 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 I 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 I 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 I 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 I 93 THR LEU
SEQRES 1 J 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 J 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 J 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 J 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 J 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 J 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 J 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 J 93 THR LEU
SEQRES 1 K 93 ILE VAL ARG PRO PRO PHE THR TYR ALA THR LEU ILE ARG
SEQRES 2 K 93 GLN ALA ILE MET GLU SER SER ASP ARG GLN LEU THR LEU
SEQRES 3 K 93 ASN GLU ILE TYR SER TRP PHE THR ARG THR PHE ALA TYR
SEQRES 4 K 93 PHE ARG ARG ASN ALA ALA THR TRP LYS ASN ALA VAL ARG
SEQRES 5 K 93 HIS ASN LEU SER LEU HIS LYS CYS PHE VAL ARG VAL GLU
SEQRES 6 K 93 ASN VAL LYS GLY ALA VAL TRP THR VAL ASP GLU VAL GLU
SEQRES 7 K 93 TYR GLN LYS ARG ARG SER GLN LYS ILE THR GLY SER PRO
SEQRES 8 K 93 THR LEU
HET MG F 601 1
HET MG G 604 1
HET MG H 602 1
HET MG I 603 1
HET MG J 605 1
HET MG K 606 1
HETNAM MG MAGNESIUM ION
FORMUL 11 MG 6(MG 2+)
FORMUL 17 HOH *581(H2 O)
HELIX 1 1 THR F 508 SER F 520 1 13
HELIX 2 2 THR F 526 ARG F 542 1 17
HELIX 3 3 ASN F 544 HIS F 559 1 16
HELIX 4 4 ASP F 576 ARG F 584 1 9
HELIX 5 5 THR G 508 SER G 520 1 13
HELIX 6 6 SER G 521 GLN G 524 5 4
HELIX 7 7 THR G 526 ASN G 544 1 19
HELIX 8 8 THR G 547 HIS G 559 1 13
HELIX 9 9 ASP G 576 ARG G 584 1 9
HELIX 10 10 THR H 508 GLU H 519 1 12
HELIX 11 11 THR H 526 ASN H 544 1 19
HELIX 12 12 THR H 547 HIS H 559 1 13
HELIX 13 13 ASP H 576 GLN H 581 1 6
HELIX 14 14 THR I 508 GLU I 519 1 12
HELIX 15 15 THR I 526 ARG I 542 1 17
HELIX 16 16 ASN I 544 HIS I 559 1 16
HELIX 17 17 ASP I 576 LYS I 582 1 7
HELIX 18 18 THR J 508 SER J 520 1 13
HELIX 19 19 THR J 526 PHE J 538 1 13
HELIX 20 20 ALA J 539 ARG J 543 5 5
HELIX 21 21 ASN J 544 HIS J 559 1 16
HELIX 22 22 ASP J 576 LYS J 582 1 7
HELIX 23 23 THR K 508 SER K 520 1 13
HELIX 24 24 THR K 526 PHE K 538 1 13
HELIX 25 25 ALA K 539 ARG K 543 5 5
HELIX 26 26 ASN K 544 HIS K 559 1 16
HELIX 27 27 ASP K 576 LYS K 582 1 7
SHEET 1 A 2 VAL F 565 GLU F 566 0
SHEET 2 A 2 ALA F 571 VAL F 572 -1 O VAL F 572 N VAL F 565
SHEET 1 B 2 PHE G 562 GLU G 566 0
SHEET 2 B 2 ALA G 571 VAL G 575 -1 O VAL G 572 N VAL G 565
SHEET 1 C 2 PHE H 562 GLU H 566 0
SHEET 2 C 2 ALA H 571 VAL H 575 -1 O VAL H 572 N VAL H 565
SHEET 1 D 2 PHE I 562 VAL I 565 0
SHEET 2 D 2 VAL I 572 VAL I 575 -1 O VAL I 572 N VAL I 565
SHEET 1 E 2 PHE J 562 ASN J 567 0
SHEET 2 E 2 GLY J 570 VAL J 575 -1 O VAL J 572 N VAL J 565
SHEET 1 F 2 PHE K 562 ASN K 567 0
SHEET 2 F 2 GLY K 570 VAL K 575 -1 O VAL K 572 N VAL K 565
LINK O HOH D 24 MG MG K 606 1555 1555 2.74
LINK O SER F 557 MG MG F 601 1555 1555 2.58
LINK O LEU F 558 MG MG F 601 1555 1555 3.01
LINK MG MG F 601 O HOH F 613 1555 1555 2.80
LINK O LEU G 556 MG MG G 604 1555 1555 2.43
LINK O HIS G 559 MG MG G 604 1555 1555 2.45
LINK O PHE G 562 MG MG G 604 1555 1555 2.44
LINK O HOH H 397 MG MG H 602 1555 1555 2.66
LINK O LEU H 556 MG MG H 602 1555 1555 2.56
LINK O HIS H 559 MG MG H 602 1555 1555 2.48
LINK O PHE H 562 MG MG H 602 1555 1555 2.55
LINK O SER I 557 MG MG I 603 1555 1555 3.13
LINK O HIS I 559 MG MG I 603 1555 1555 3.15
LINK O LEU J 556 MG MG J 605 1555 1555 2.26
LINK O HIS J 559 MG MG J 605 1555 1555 2.44
LINK O PHE J 562 MG MG J 605 1555 1555 2.41
LINK MG MG J 605 O HOH J 673 1555 1555 2.59
LINK O LEU K 556 MG MG K 606 1555 1555 2.29
LINK O SER K 557 MG MG K 606 1555 1555 3.05
LINK O HIS K 559 MG MG K 606 1555 1555 2.45
LINK O PHE K 562 MG MG K 606 1555 1555 2.45
LINK MG MG K 606 O HOH K 645 1555 1555 2.58
SITE 1 AC1 4 SER F 557 LEU F 558 HIS F 559 HOH F 613
SITE 1 AC2 4 HOH H 397 LEU H 556 HIS H 559 PHE H 562
SITE 1 AC3 3 SER I 557 LEU I 558 HIS I 559
SITE 1 AC4 3 LEU G 556 HIS G 559 PHE G 562
SITE 1 AC5 5 LEU J 556 SER J 557 HIS J 559 PHE J 562
SITE 2 AC5 5 HOH J 673
SITE 1 AC6 6 HOH D 24 LEU K 556 SER K 557 HIS K 559
SITE 2 AC6 6 PHE K 562 HOH K 645
CRYST1 67.542 124.210 67.666 90.00 110.81 90.00 P 1 21 1 12
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 0.014806 0.000000 0.005627 0.00000
SCALE2 0.000000 0.008051 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
