HEADER ANTITUMOR PROTEIN/DNA 04-JAN-12 3VD1
TITLE STRUCTURE OF P73 DNA BINDING DOMAIN TETRAMER MODULATES P73
TITLE 2 TRANSACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR PROTEIN P73;
COMPND 3 CHAIN: A, B, C, D, I, J, K, L;
COMPND 4 FRAGMENT: UNP RESIDUE 115-312;
COMPND 5 SYNONYM: P53-LIKE TRANSCRIPTION FACTOR, P53-RELATED PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3');
COMPND 9 CHAIN: E, F, G, H, M, N, O, P;
COMPND 10 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES
KEYWDS PROTEIN DNA COMPLEX, BETA-IMMUNOGLOBULIN-LIKE FOLD, TUMOUR
KEYWDS 2 SUPPRESSOR, ANTITUMOR PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.ETHAYATHULLA,P.W.TSE,S.NGUYEN,H.VIADIU
REVDAT 6 13-SEP-23 3VD1 1 REMARK SEQADV LINK
REVDAT 5 08-OCT-14 3VD1 1 AUTHOR
REVDAT 4 22-AUG-12 3VD1 1 REMARK
REVDAT 3 25-JUL-12 3VD1 1 JRNL
REVDAT 2 16-MAY-12 3VD1 1
REVDAT 1 18-APR-12 3VD1 0
JRNL AUTH A.S.ETHAYATHULLA,P.W.TSE,P.MONTI,S.NGUYEN,A.INGA,G.FRONZA,
JRNL AUTH 2 H.VIADIU
JRNL TITL STRUCTURE OF P73 DNA-BINDING DOMAIN TETRAMER MODULATES P73
JRNL TITL 2 TRANSACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 6066 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22474346
JRNL DOI 10.1073/PNAS.1115463109
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1510416.310
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 41779
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 843
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6596
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12576
REMARK 3 NUCLEIC ACID ATOMS : 1944
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.31000
REMARK 3 B22 (A**2) : 12.41000
REMARK 3 B33 (A**2) : -17.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.58
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.71
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.380
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 36.51
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3VD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : RH COATED FLAT MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41946
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3KMD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.1M NA ACETATE, PH 6.1,
REMARK 280 TEMPERATURE 298.0K
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 52.10000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE OCTAMER IN THE ASU CORRESPONDS TO A TETRAMER P73DBD
REMARK 300 PLUS FOUR CHAINS OF TWO CONTINUOUS DNA DOUBLE STRANDS.
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, M, N, O, P
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 MET A 103
REMARK 465 GLY A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
REMARK 465 HIS A 110
REMARK 465 MET B 103
REMARK 465 GLY B 104
REMARK 465 HIS B 105
REMARK 465 HIS B 106
REMARK 465 HIS B 107
REMARK 465 HIS B 108
REMARK 465 HIS B 109
REMARK 465 HIS B 110
REMARK 465 HIS B 111
REMARK 465 HIS B 112
REMARK 465 GLU B 113
REMARK 465 MET C 103
REMARK 465 GLY C 104
REMARK 465 HIS C 105
REMARK 465 HIS C 106
REMARK 465 HIS C 107
REMARK 465 HIS C 108
REMARK 465 HIS C 109
REMARK 465 HIS C 110
REMARK 465 HIS C 111
REMARK 465 MET D 103
REMARK 465 GLY D 104
REMARK 465 HIS D 105
REMARK 465 HIS D 106
REMARK 465 HIS D 107
REMARK 465 HIS D 108
REMARK 465 HIS D 109
REMARK 465 HIS D 110
REMARK 465 HIS D 111
REMARK 465 HIS D 112
REMARK 465 GLU D 113
REMARK 465 MET I 103
REMARK 465 GLY I 104
REMARK 465 HIS I 105
REMARK 465 HIS I 106
REMARK 465 HIS I 107
REMARK 465 HIS I 108
REMARK 465 HIS I 109
REMARK 465 HIS I 110
REMARK 465 HIS I 111
REMARK 465 HIS I 112
REMARK 465 GLU I 113
REMARK 465 MET J 103
REMARK 465 GLY J 104
REMARK 465 HIS J 105
REMARK 465 HIS J 106
REMARK 465 HIS J 107
REMARK 465 HIS J 108
REMARK 465 HIS J 109
REMARK 465 HIS J 110
REMARK 465 HIS J 111
REMARK 465 HIS J 112
REMARK 465 GLU J 113
REMARK 465 MET K 103
REMARK 465 GLY K 104
REMARK 465 HIS K 105
REMARK 465 HIS K 106
REMARK 465 HIS K 107
REMARK 465 HIS K 108
REMARK 465 HIS K 109
REMARK 465 HIS K 110
REMARK 465 MET L 103
REMARK 465 GLY L 104
REMARK 465 HIS L 105
REMARK 465 HIS L 106
REMARK 465 HIS L 107
REMARK 465 HIS L 108
REMARK 465 HIS L 109
REMARK 465 HIS L 110
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 111 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 112 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 PHE B 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 113 CG CD OE1 OE2
REMARK 470 PHE C 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE I 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE J 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS K 112 CG ND1 CD2 CE1 NE2
REMARK 470 HIS L 111 CG ND1 CD2 CE1 NE2
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 PRO B 168 C - N - CD ANGL. DEV. = -15.6 DEGREES
REMARK 500 PRO B 169 C - N - CD ANGL. DEV. = -20.3 DEGREES
REMARK 500 PRO B 170 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO B 171 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 DA F 415 C3' - O3' - P ANGL. DEV. = 12.3 DEGREES
REMARK 500 DC O 710 C3' - C2' - C1' ANGL. DEV. = -4.9 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 THR A 119 126.33 -33.30
REMARK 500 ALA A 140 148.46 -33.82
REMARK 500 TRP A 142 142.96 -171.11
REMARK 500 LYS A 149 46.22 31.32
REMARK 500 PHE A 203 8.22 -178.98
REMARK 500 SER A 208 -45.77 -137.86
REMARK 500 ALA A 211 5.06 -68.67
REMARK 500 ASN A 220 120.99 -38.53
REMARK 500 ASP A 227 74.41 -150.41
REMARK 500 PRO A 243 137.40 -33.15
REMARK 500 VAL A 245 123.25 -38.38
REMARK 500 SER A 260 -19.16 -37.63
REMARK 500 MET A 266 95.13 -64.35
REMARK 500 ARG A 268 19.95 56.59
REMARK 500 PHE A 290 125.38 -178.84
REMARK 500 ARG A 310 31.41 -78.28
REMARK 500 ILE B 115 71.78 65.97
REMARK 500 ASN B 118 21.63 -76.29
REMARK 500 TYR B 121 97.14 -172.09
REMARK 500 SER B 139 30.24 -93.89
REMARK 500 LYS B 149 54.87 -98.27
REMARK 500 ALA B 156 10.51 55.10
REMARK 500 PRO B 169 5.98 -158.16
REMARK 500 LYS B 192 -165.73 -107.12
REMARK 500 SER B 223 150.38 -43.55
REMARK 500 VAL B 245 114.42 -36.51
REMARK 500 ARG B 268 2.17 81.39
REMARK 500 GLN B 283 95.97 -167.47
REMARK 500 VAL B 284 103.36 -57.24
REMARK 500 ARG B 287 162.51 179.72
REMARK 500 PHE B 290 135.78 -172.29
REMARK 500 GLU B 311 -35.90 -39.35
REMARK 500 PRO C 116 122.37 -39.14
REMARK 500 TYR C 121 91.40 -171.69
REMARK 500 GLN C 132 -77.84 -94.48
REMARK 500 LYS C 149 51.36 37.19
REMARK 500 ALA C 156 18.89 53.59
REMARK 500 PRO C 170 161.44 -49.76
REMARK 500 ASP C 202 107.71 -41.21
REMARK 500 PHE C 203 -3.36 83.47
REMARK 500 ASN C 220 93.48 -161.44
REMARK 500 PRO C 243 -114.21 -31.07
REMARK 500 CYS C 262 107.55 -51.84
REMARK 500 ARG C 268 -3.44 73.00
REMARK 500 ILE C 271 -168.61 -102.27
REMARK 500 LEU C 272 114.14 -160.53
REMARK 500 ARG C 287 145.99 -176.13
REMARK 500 CYS C 297 94.51 -168.06
REMARK 500 ILE D 115 -106.15 -132.94
REMARK 500 SER D 117 -151.31 -56.91
REMARK 500
REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS.
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 194 SG
REMARK 620 2 HIS A 197 ND1 82.3
REMARK 620 3 CYS A 258 SG 107.3 102.3
REMARK 620 4 CYS A 262 SG 88.5 96.8 156.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 194 SG
REMARK 620 2 HIS B 197 ND1 84.5
REMARK 620 3 CYS B 258 SG 96.6 98.7
REMARK 620 4 CYS B 262 SG 98.8 123.4 136.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 194 SG
REMARK 620 2 HIS C 197 ND1 110.8
REMARK 620 3 CYS C 258 SG 117.5 113.5
REMARK 620 4 CYS C 262 SG 122.8 99.0 91.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 194 SG
REMARK 620 2 HIS D 197 ND1 97.0
REMARK 620 3 CYS D 258 SG 110.7 97.6
REMARK 620 4 CYS D 262 SG 118.3 101.7 123.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 194 SG
REMARK 620 2 HIS I 197 ND1 96.6
REMARK 620 3 CYS I 258 SG 106.2 120.5
REMARK 620 4 CYS I 262 SG 133.4 104.4 98.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 194 SG
REMARK 620 2 HIS J 197 ND1 158.5
REMARK 620 3 CYS J 258 SG 86.4 99.1
REMARK 620 4 CYS J 262 SG 82.9 115.1 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 194 SG
REMARK 620 2 HIS K 197 ND1 98.1
REMARK 620 3 CYS K 258 SG 104.4 112.9
REMARK 620 4 CYS K 262 SG 105.0 79.4 145.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 194 SG
REMARK 620 2 HIS L 197 ND1 94.2
REMARK 620 3 CYS L 258 SG 112.4 102.0
REMARK 620 4 CYS L 262 SG 122.5 102.1 117.2
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VD0 RELATED DB: PDB
REMARK 900 RELATED ID: 3VD2 RELATED DB: PDB
DBREF 3VD1 A 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 B 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 C 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 D 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 I 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 J 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 K 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 L 115 312 UNP O15350 P73_HUMAN 115 312
DBREF 3VD1 E 398 409 PDB 3VD1 3VD1 398 409
DBREF 3VD1 F 410 421 PDB 3VD1 3VD1 410 421
DBREF 3VD1 G 500 511 PDB 3VD1 3VD1 500 511
DBREF 3VD1 H 512 523 PDB 3VD1 3VD1 512 523
DBREF 3VD1 M 600 611 PDB 3VD1 3VD1 600 611
DBREF 3VD1 N 612 623 PDB 3VD1 3VD1 612 623
DBREF 3VD1 O 700 711 PDB 3VD1 3VD1 700 711
DBREF 3VD1 P 712 723 PDB 3VD1 3VD1 712 723
SEQADV 3VD1 MET A 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY A 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS A 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU A 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE A 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET B 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY B 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS B 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU B 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE B 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET C 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY C 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS C 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU C 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE C 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET D 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY D 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS D 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU D 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE D 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET I 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY I 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS I 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU I 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE I 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET J 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY J 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS J 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU J 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE J 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET K 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY K 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS K 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU K 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE K 114 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 MET L 103 UNP O15350 INITIATING METHIONINE
SEQADV 3VD1 GLY L 104 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 105 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 106 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 107 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 108 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 109 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 110 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 111 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 HIS L 112 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 GLU L 113 UNP O15350 EXPRESSION TAG
SEQADV 3VD1 PHE L 114 UNP O15350 EXPRESSION TAG
SEQRES 1 A 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 A 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 A 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 A 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 A 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 A 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 A 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 A 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 A 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 A 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 A 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 A 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 A 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 A 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 A 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 A 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 A 210 GLU GLN
SEQRES 1 B 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 B 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 B 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 B 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 B 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 B 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 B 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 B 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 B 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 B 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 B 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 B 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 B 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 B 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 B 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 B 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 B 210 GLU GLN
SEQRES 1 C 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 C 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 C 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 C 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 C 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 C 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 C 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 C 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 C 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 C 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 C 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 C 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 C 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 C 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 C 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 C 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 C 210 GLU GLN
SEQRES 1 D 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 D 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 D 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 D 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 D 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 D 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 D 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 D 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 D 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 D 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 D 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 D 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 D 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 D 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 D 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 D 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 D 210 GLU GLN
SEQRES 1 I 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 I 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 I 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 I 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 I 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 I 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 I 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 I 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 I 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 I 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 I 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 I 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 I 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 I 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 I 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 I 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 I 210 GLU GLN
SEQRES 1 J 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 J 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 J 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 J 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 J 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 J 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 J 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 J 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 J 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 J 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 J 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 J 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 J 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 J 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 J 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 J 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 J 210 GLU GLN
SEQRES 1 K 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 K 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 K 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 K 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 K 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 K 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 K 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 K 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 K 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 K 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 K 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 K 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 K 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 K 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 K 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 K 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 K 210 GLU GLN
SEQRES 1 L 210 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE
SEQRES 2 L 210 PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU
SEQRES 3 L 210 VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR
SEQRES 4 L 210 TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN
SEQRES 5 L 210 ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR
SEQRES 6 L 210 PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL
SEQRES 7 L 210 TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG
SEQRES 8 L 210 CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY
SEQRES 9 L 210 GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY
SEQRES 10 L 210 ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY
SEQRES 11 L 210 ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL
SEQRES 12 L 210 GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS
SEQRES 13 L 210 ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE
SEQRES 14 L 210 LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL
SEQRES 15 L 210 LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS
SEQRES 16 L 210 PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG
SEQRES 17 L 210 GLU GLN
SEQRES 1 E 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 F 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 G 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 H 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 M 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 N 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 O 12 DC DG DG DG DC DA DT DG DC DC DC DG
SEQRES 1 P 12 DC DG DG DG DC DA DT DG DC DC DC DG
HET ZN A 401 1
HET ZN B 401 1
HET ZN C 401 1
HET ZN D 401 1
HET ZN I 401 1
HET ZN J 401 1
HET ZN K 401 1
HET ZN L 401 1
HETNAM ZN ZINC ION
FORMUL 17 ZN 8(ZN 2+)
FORMUL 25 HOH *188(H2 O)
HELIX 1 1 LYS A 183 THR A 188 1 6
HELIX 2 2 CYS A 194 GLY A 200 1 7
HELIX 3 3 CYS A 297 ARG A 310 1 14
HELIX 4 4 LYS B 183 THR B 188 1 6
HELIX 5 5 CYS B 194 GLY B 200 1 7
HELIX 6 6 CYS B 297 GLN B 312 1 16
HELIX 7 7 CYS C 194 LEU C 199 1 6
HELIX 8 8 CYS C 297 GLN C 312 1 16
HELIX 9 9 GLU D 185 ASP D 189 5 5
HELIX 10 10 CYS D 194 LEU D 199 1 6
HELIX 11 11 CYS D 297 GLN D 312 1 16
HELIX 12 12 CYS I 194 LEU I 199 1 6
HELIX 13 13 CYS I 297 GLU I 311 1 15
HELIX 14 14 PRO J 122 HIS J 126 5 5
HELIX 15 15 LYS J 183 THR J 188 1 6
HELIX 16 16 CYS J 194 GLY J 200 1 7
HELIX 17 17 CYS J 297 GLN J 312 1 16
HELIX 18 18 CYS K 194 LEU K 199 1 6
HELIX 19 19 CYS K 297 GLU K 311 1 15
HELIX 20 20 LYS L 183 VAL L 187 5 5
HELIX 21 21 CYS L 194 GLY L 200 1 7
HELIX 22 22 GLY L 299 GLU L 311 1 13
SHEET 1 A 4 GLU A 128 THR A 130 0
SHEET 2 A 4 CYS A 159 LYS A 164 -1 O GLN A 162 N THR A 130
SHEET 3 A 4 THR A 250 PHE A 256 -1 O THR A 250 N ILE A 163
SHEET 4 A 4 ILE A 215 VAL A 217 -1 N ARG A 216 O ASN A 255
SHEET 1 B 7 TRP A 142 THR A 143 0
SHEET 2 B 7 LYS A 150 CYS A 153 -1 O TYR A 152 N THR A 143
SHEET 3 B 7 GLU A 291 ILE A 294 1 O ARG A 293 N CYS A 153
SHEET 4 B 7 ILE A 271 GLU A 278 -1 N ILE A 271 O GLY A 292
SHEET 5 B 7 ALA A 174 TYR A 181 -1 N VAL A 180 O LEU A 272
SHEET 6 B 7 ARG A 233 PRO A 239 -1 O VAL A 238 N ILE A 175
SHEET 7 B 7 GLN A 224 ASP A 228 -1 N GLN A 224 O VAL A 237
SHEET 1 C 5 TRP A 142 THR A 143 0
SHEET 2 C 5 LYS A 150 CYS A 153 -1 O TYR A 152 N THR A 143
SHEET 3 C 5 GLU A 291 ILE A 294 1 O ARG A 293 N CYS A 153
SHEET 4 C 5 ILE A 271 GLU A 278 -1 N ILE A 271 O GLY A 292
SHEET 5 C 5 GLY A 286 ARG A 288 -1 O GLY A 286 N LEU A 277
SHEET 1 D 4 PHE B 127 PHE B 131 0
SHEET 2 D 4 CYS B 159 VAL B 165 -1 O GLN B 162 N THR B 130
SHEET 3 D 4 THR B 250 PHE B 256 -1 O THR B 250 N ILE B 163
SHEET 4 D 4 ILE B 215 VAL B 217 -1 N ARG B 216 O ASN B 255
SHEET 1 E 7 TRP B 142 SER B 145 0
SHEET 2 E 7 LYS B 150 CYS B 153 -1 O TYR B 152 N THR B 143
SHEET 3 E 7 VAL B 284 ILE B 294 1 O ARG B 293 N CYS B 153
SHEET 4 E 7 ILE B 271 GLU B 278 -1 N ILE B 271 O GLY B 292
SHEET 5 E 7 ALA B 174 TYR B 181 -1 N VAL B 180 O LEU B 272
SHEET 6 E 7 GLN B 234 PRO B 239 -1 O VAL B 238 N ILE B 175
SHEET 7 E 7 GLN B 224 ASP B 227 -1 N VAL B 226 O SER B 235
SHEET 1 F 4 GLU C 128 THR C 130 0
SHEET 2 F 4 CYS C 159 LYS C 164 -1 O GLN C 162 N THR C 130
SHEET 3 F 4 THR C 250 PHE C 256 -1 O THR C 250 N ILE C 163
SHEET 4 F 4 ILE C 215 VAL C 217 -1 N ARG C 216 O ASN C 255
SHEET 1 G 7 TRP C 142 SER C 145 0
SHEET 2 G 7 LYS C 150 GLN C 154 -1 O TYR C 152 N THR C 143
SHEET 3 G 7 VAL C 284 CYS C 295 1 O GLU C 291 N LEU C 151
SHEET 4 G 7 ILE C 271 GLU C 278 -1 N LEU C 277 O LEU C 285
SHEET 5 G 7 ALA C 174 TYR C 181 -1 N ARG C 176 O THR C 276
SHEET 6 G 7 GLN C 234 PRO C 239 -1 O VAL C 236 N ALA C 177
SHEET 7 G 7 GLN C 224 ASP C 227 -1 N VAL C 226 O SER C 235
SHEET 1 H 4 GLU D 128 THR D 130 0
SHEET 2 H 4 CYS D 159 LYS D 164 -1 O GLN D 162 N THR D 130
SHEET 3 H 4 THR D 250 PHE D 256 -1 O THR D 250 N ILE D 163
SHEET 4 H 4 ILE D 215 VAL D 217 -1 N ARG D 216 O ASN D 255
SHEET 1 I 7 TRP D 142 SER D 145 0
SHEET 2 I 7 LYS D 150 CYS D 153 -1 O TYR D 152 N THR D 143
SHEET 3 I 7 ARG D 288 ILE D 294 1 O GLU D 291 N LEU D 151
SHEET 4 I 7 ILE D 271 MET D 279 -1 N ILE D 271 O GLY D 292
SHEET 5 I 7 THR D 173 TYR D 181 -1 N MET D 178 O ILE D 274
SHEET 6 I 7 GLN D 234 PRO D 239 -1 O VAL D 238 N ILE D 175
SHEET 7 I 7 GLN D 224 ASP D 227 -1 N VAL D 226 O SER D 235
SHEET 1 J 4 GLU I 128 PHE I 131 0
SHEET 2 J 4 THR I 158 LYS I 164 -1 O LYS I 164 N GLU I 128
SHEET 3 J 4 THR I 250 PHE I 256 -1 O TYR I 254 N CYS I 159
SHEET 4 J 4 ILE I 215 VAL I 217 -1 N ARG I 216 O ASN I 255
SHEET 1 K 7 TRP I 142 SER I 145 0
SHEET 2 K 7 LYS I 150 CYS I 153 -1 O LYS I 150 N SER I 145
SHEET 3 K 7 VAL I 284 ILE I 294 1 O ARG I 293 N LEU I 151
SHEET 4 K 7 ILE I 271 GLU I 278 -1 N ILE I 273 O PHE I 290
SHEET 5 K 7 ALA I 174 TYR I 181 -1 N VAL I 180 O LEU I 272
SHEET 6 K 7 GLN I 234 PRO I 239 -1 O VAL I 236 N ALA I 177
SHEET 7 K 7 GLN I 224 ASP I 227 -1 N VAL I 226 O SER I 235
SHEET 1 L 4 GLU J 128 PHE J 131 0
SHEET 2 L 4 CYS J 159 LYS J 164 -1 N LYS J 164 O GLU J 128
SHEET 3 L 4 ILE J 252 PHE J 256 -1 O ILE J 252 N ILE J 161
SHEET 4 L 4 ILE J 215 VAL J 217 -1 N ARG J 216 O ASN J 255
SHEET 1 M 6 TRP J 142 SER J 145 0
SHEET 2 M 6 LYS J 150 CYS J 153 -1 O TYR J 152 N THR J 143
SHEET 3 M 6 VAL J 284 GLY J 292 1 O GLU J 291 N LEU J 151
SHEET 4 M 6 ILE J 271 MET J 279 -1 N ILE J 273 O PHE J 290
SHEET 5 M 6 THR J 173 TYR J 181 -1 N VAL J 180 O LEU J 272
SHEET 6 M 6 VAL J 236 VAL J 238 -1 O VAL J 238 N ILE J 175
SHEET 1 N 7 TRP K 142 SER K 145 0
SHEET 2 N 7 LYS K 150 GLN K 154 -1 O TYR K 152 N THR K 143
SHEET 3 N 7 ARG K 288 CYS K 295 1 O GLU K 291 N LEU K 151
SHEET 4 N 7 ILE K 271 GLU K 278 -1 N ILE K 273 O PHE K 290
SHEET 5 N 7 ALA K 174 TYR K 181 -1 N ALA K 174 O GLU K 278
SHEET 6 N 7 GLN K 234 PRO K 239 -1 O VAL K 238 N ILE K 175
SHEET 7 N 7 TYR K 225 ASP K 227 -1 N VAL K 226 O SER K 235
SHEET 1 O 3 CYS K 159 ILE K 163 0
SHEET 2 O 3 THR K 250 PHE K 256 -1 O TYR K 254 N CYS K 159
SHEET 3 O 3 ILE K 215 VAL K 217 -1 N ARG K 216 O ASN K 255
SHEET 1 P 4 GLU L 128 THR L 130 0
SHEET 2 P 4 CYS L 159 LYS L 164 -1 O LYS L 164 N GLU L 128
SHEET 3 P 4 THR L 250 PHE L 256 -1 O TYR L 254 N CYS L 159
SHEET 4 P 4 ILE L 215 VAL L 217 -1 N ARG L 216 O ASN L 255
SHEET 1 Q 7 TRP L 142 TYR L 144 0
SHEET 2 Q 7 LEU L 151 GLN L 154 -1 O TYR L 152 N THR L 143
SHEET 3 Q 7 VAL L 284 CYS L 295 1 O ARG L 293 N LEU L 151
SHEET 4 Q 7 ILE L 271 GLU L 278 -1 N LEU L 277 O GLY L 286
SHEET 5 Q 7 ALA L 174 TYR L 181 -1 N ALA L 174 O GLU L 278
SHEET 6 Q 7 GLN L 234 PRO L 239 -1 O VAL L 238 N ILE L 175
SHEET 7 Q 7 GLN L 224 ASP L 227 -1 N VAL L 226 O SER L 235
LINK SG CYS A 194 ZN ZN A 401 1555 1555 2.29
LINK ND1 HIS A 197 ZN ZN A 401 1555 1555 2.02
LINK SG CYS A 258 ZN ZN A 401 1555 1555 2.28
LINK SG CYS A 262 ZN ZN A 401 1555 1555 2.35
LINK SG CYS B 194 ZN ZN B 401 1555 1555 2.27
LINK ND1 HIS B 197 ZN ZN B 401 1555 1555 2.05
LINK SG CYS B 258 ZN ZN B 401 1555 1555 2.28
LINK SG CYS B 262 ZN ZN B 401 1555 1555 2.34
LINK SG CYS C 194 ZN ZN C 401 1555 1555 2.32
LINK ND1 HIS C 197 ZN ZN C 401 1555 1555 2.05
LINK SG CYS C 258 ZN ZN C 401 1555 1555 2.28
LINK SG CYS C 262 ZN ZN C 401 1555 1555 2.32
LINK SG CYS D 194 ZN ZN D 401 1555 1555 2.35
LINK ND1 HIS D 197 ZN ZN D 401 1555 1555 2.01
LINK SG CYS D 258 ZN ZN D 401 1555 1555 2.30
LINK SG CYS D 262 ZN ZN D 401 1555 1555 2.31
LINK SG CYS I 194 ZN ZN I 401 1555 1555 2.26
LINK ND1 HIS I 197 ZN ZN I 401 1555 1555 2.03
LINK SG CYS I 258 ZN ZN I 401 1555 1555 2.29
LINK SG CYS I 262 ZN ZN I 401 1555 1555 2.31
LINK SG CYS J 194 ZN ZN J 401 1555 1555 2.30
LINK ND1 HIS J 197 ZN ZN J 401 1555 1555 2.03
LINK SG CYS J 258 ZN ZN J 401 1555 1555 2.33
LINK SG CYS J 262 ZN ZN J 401 1555 1555 2.33
LINK SG CYS K 194 ZN ZN K 401 1555 1555 2.31
LINK ND1 HIS K 197 ZN ZN K 401 1555 1555 2.05
LINK SG CYS K 258 ZN ZN K 401 1555 1555 2.26
LINK SG CYS K 262 ZN ZN K 401 1555 1555 2.32
LINK SG CYS L 194 ZN ZN L 401 1555 1555 2.28
LINK ND1 HIS L 197 ZN ZN L 401 1555 1555 2.04
LINK SG CYS L 258 ZN ZN L 401 1555 1555 2.30
LINK SG CYS L 262 ZN ZN L 401 1555 1555 2.31
SITE 1 AC1 4 CYS A 194 HIS A 197 CYS A 258 CYS A 262
SITE 1 AC2 4 CYS B 194 HIS B 197 CYS B 258 CYS B 262
SITE 1 AC3 4 CYS C 194 HIS C 197 CYS C 258 CYS C 262
SITE 1 AC4 4 CYS D 194 HIS D 197 CYS D 258 CYS D 262
SITE 1 AC5 4 CYS I 194 HIS I 197 CYS I 258 CYS I 262
SITE 1 AC6 4 CYS J 194 HIS J 197 CYS J 258 CYS J 262
SITE 1 AC7 4 CYS K 194 HIS K 197 CYS K 258 CYS K 262
SITE 1 AC8 4 CYS L 194 HIS L 197 CYS L 258 CYS L 262
CRYST1 82.540 104.200 123.223 90.00 96.55 90.00 P 1 21 1 16
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 0.012115 0.000000 0.001391 0.00000
SCALE2 0.000000 0.009597 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008169 0.00000
(ATOM LINES ARE NOT SHOWN.)
END