HEADER TRANSCRIPTION ACTIVATOR/DNA 22-NOV-11 3US0
TITLE STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR A/T
TITLE 2 RICH RESPONSE ELEMENT CONTAINING A TWO BASE PAIR "AT" SPACER BETWEEN
TITLE 3 HALF SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR PROTEIN 63;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN (UNP RESIDUES 166-362);
COMPND 5 SYNONYM: TP63, P63, CHRONIC ULCERATIVE STOMATITIS PROTEIN, CUSP,
COMPND 6 KERATINOCYTE TRANSCRIPTION FACTOR KET, TRANSFORMATION-RELATED PROTEIN
COMPND 7 63, TUMOR PROTEIN P73-LIKE, P73L, P40, P51;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 5'-D(*AP*AP*AP*CP*AP*TP*GP*TP*TP*TP*AP*TP*AP*AP*AP*CP*AP*TP
COMPND 11 *GP*TP*TP*T)-3';
COMPND 12 CHAIN: E, F;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: P63 RESPONSE ELEMENT WITH AT SPACER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KET, P63, P73H, P73L, TP63, TP73L;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS B-DNA DOUBLE HELIX, ZINC BINDING, BETA SANDWICH, GREEK KEY,
KEYWDS 2 TRANSCRIPTION FACTOR, NUCLEUS, TRANSCRIPTION ACTIVATOR-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHEN,O.HERZBERG
REVDAT 4 13-SEP-23 3US0 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3US0 1 REMARK
REVDAT 2 21-MAR-12 3US0 1 JRNL
REVDAT 1 01-FEB-12 3US0 0
JRNL AUTH C.CHEN,N.GORLATOVA,O.HERZBERG
JRNL TITL PLIABLE DNA CONFORMATION OF RESPONSE ELEMENTS BOUND TO
JRNL TITL 2 TRANSCRIPTION FACTOR P63.
JRNL REF J.BIOL.CHEM. V. 287 7477 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22247550
JRNL DOI 10.1074/JBC.M111.315820
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47224
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2424
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 59.8191 - 6.4257 1.00 2700 146 0.1705 0.2178
REMARK 3 2 6.4257 - 5.1012 1.00 2650 158 0.1497 0.1852
REMARK 3 3 5.1012 - 4.4566 1.00 2646 147 0.1389 0.1712
REMARK 3 4 4.4566 - 4.0492 1.00 2633 137 0.1525 0.1748
REMARK 3 5 4.0492 - 3.7590 1.00 2659 132 0.1879 0.2116
REMARK 3 6 3.7590 - 3.5374 1.00 2627 143 0.2002 0.2144
REMARK 3 7 3.5374 - 3.3603 1.00 2634 144 0.2186 0.2782
REMARK 3 8 3.3603 - 3.2140 1.00 2654 114 0.1862 0.2188
REMARK 3 9 3.2140 - 3.0903 1.00 2609 140 0.2286 0.2480
REMARK 3 10 3.0903 - 2.9837 1.00 2623 155 0.2577 0.2958
REMARK 3 11 2.9837 - 2.8904 1.00 2631 144 0.2856 0.3286
REMARK 3 12 2.8904 - 2.8078 1.00 2629 145 0.3044 0.2826
REMARK 3 13 2.8078 - 2.7338 1.00 2614 136 0.3297 0.3569
REMARK 3 14 2.7338 - 2.6671 1.00 2647 155 0.3430 0.4028
REMARK 3 15 2.6671 - 2.6065 1.00 2603 144 0.3564 0.3833
REMARK 3 16 2.6065 - 2.5510 1.00 2648 132 0.3585 0.3865
REMARK 3 17 2.5510 - 2.5000 1.00 2593 152 0.3841 0.4090
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 44.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.46190
REMARK 3 B22 (A**2) : 8.46190
REMARK 3 B33 (A**2) : -16.92370
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 7136
REMARK 3 ANGLE : 1.643 9894
REMARK 3 CHIRALITY : 0.102 1105
REMARK 3 PLANARITY : 0.007 1151
REMARK 3 DIHEDRAL : 20.344 2741
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -59.5023 6.3936 22.6970
REMARK 3 T TENSOR
REMARK 3 T11: 0.4795 T22: 0.3339
REMARK 3 T33: 0.3942 T12: 0.0834
REMARK 3 T13: -0.0829 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.3233 L22: 1.9618
REMARK 3 L33: 1.0346 L12: -0.7895
REMARK 3 L13: -0.4857 L23: 1.2166
REMARK 3 S TENSOR
REMARK 3 S11: 0.1244 S12: 0.1673 S13: 0.0185
REMARK 3 S21: -0.4610 S22: -0.2554 S23: 0.1854
REMARK 3 S31: -0.4676 S32: -0.2446 S33: -0.0096
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -49.0776 -19.9373 -10.3005
REMARK 3 T TENSOR
REMARK 3 T11: 0.3867 T22: 0.3590
REMARK 3 T33: 0.3896 T12: 0.0565
REMARK 3 T13: -0.0216 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.9242 L22: 1.3274
REMARK 3 L33: 1.7992 L12: -0.3418
REMARK 3 L13: -0.1141 L23: 0.5051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0782 S12: 0.1531 S13: -0.0466
REMARK 3 S21: -0.2589 S22: -0.2435 S23: 0.0165
REMARK 3 S31: -0.2100 S32: -0.0858 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -57.3275 20.3927 -43.4989
REMARK 3 T TENSOR
REMARK 3 T11: 0.5143 T22: 0.6061
REMARK 3 T33: 0.5374 T12: -0.1772
REMARK 3 T13: 0.1144 T23: -0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 1.2189 L22: 0.5266
REMARK 3 L33: 0.4326 L12: 0.7979
REMARK 3 L13: 0.2527 L23: 0.2818
REMARK 3 S TENSOR
REMARK 3 S11: 0.3692 S12: -0.5754 S13: 0.1146
REMARK 3 S21: 0.4752 S22: -0.3367 S23: 0.3738
REMARK 3 S31: 0.1902 S32: -0.3664 S33: 0.0715
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2543 39.5497 -10.1073
REMARK 3 T TENSOR
REMARK 3 T11: 0.5069 T22: 0.4718
REMARK 3 T33: 0.3283 T12: -0.1331
REMARK 3 T13: 0.0436 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.0813 L22: 1.2884
REMARK 3 L33: 1.1955 L12: 0.4056
REMARK 3 L13: 0.1126 L23: 0.6055
REMARK 3 S TENSOR
REMARK 3 S11: 0.2012 S12: -0.3891 S13: 0.0031
REMARK 3 S21: 0.4466 S22: -0.3031 S23: -0.0032
REMARK 3 S31: 0.2986 S32: -0.2738 S33: -0.0011
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E OR CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): -36.4120 8.2543 -10.1442
REMARK 3 T TENSOR
REMARK 3 T11: 0.8691 T22: 0.5263
REMARK 3 T33: 0.3928 T12: -0.1412
REMARK 3 T13: 0.0320 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: -0.3125 L22: 1.3089
REMARK 3 L33: 1.4612 L12: 0.4698
REMARK 3 L13: -0.8458 L23: -2.9506
REMARK 3 S TENSOR
REMARK 3 S11: 0.0855 S12: 0.0026 S13: -0.0516
REMARK 3 S21: -0.1963 S22: -0.0042 S23: -0.0275
REMARK 3 S31: 0.2337 S32: 0.6154 S33: 0.0503
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3US0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000069136.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320357
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47258
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.45100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 3QYN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 0.2 M AMMONIUM ACETATE,
REMARK 280 0.1 M BIS-TRIS, PH 6.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.80200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 59.80200
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.80200
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 GLY A 121
REMARK 465 SER A 122
REMARK 465 HIS A 123
REMARK 465 MET A 124
REMARK 465 ALA A 125
REMARK 465 ARG A 321
REMARK 465 LYS A 322
REMARK 465 GLN A 323
REMARK 465 GLY B 121
REMARK 465 SER B 122
REMARK 465 HIS B 123
REMARK 465 GLN B 144
REMARK 465 SER B 145
REMARK 465 SER B 146
REMARK 465 THR B 147
REMARK 465 ALA B 148
REMARK 465 LYS B 149
REMARK 465 GLN B 323
REMARK 465 GLY C 121
REMARK 465 SER C 122
REMARK 465 HIS C 123
REMARK 465 MET C 124
REMARK 465 ARG C 321
REMARK 465 LYS C 322
REMARK 465 GLN C 323
REMARK 465 GLY D 121
REMARK 465 SER D 122
REMARK 465 HIS D 123
REMARK 465 GLN D 144
REMARK 465 SER D 145
REMARK 465 SER D 146
REMARK 465 THR D 147
REMARK 465 ALA D 148
REMARK 465 LYS D 149
REMARK 465 SER D 150
REMARK 465 GLN D 323
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 LYS A 149 CE NZ
REMARK 470 LYS A 160 CD CE NZ
REMARK 470 GLN A 182 CG CD OE1 NE2
REMARK 470 LYS A 194 CD CE NZ
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 ILE A 219 CG1 CD1
REMARK 470 LYS A 314 CE NZ
REMARK 470 GLN B 182 CG CD OE1 NE2
REMARK 470 ARG B 212 NE CZ NH1 NH2
REMARK 470 ILE B 219 CG1 CD1
REMARK 470 GLN B 294 CD OE1 NE2
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 ARG B 321 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 149 CD CE NZ
REMARK 470 LYS C 194 CD CE NZ
REMARK 470 ARG C 212 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 218 CD OE1 NE2
REMARK 470 ARG C 279 NE CZ NH1 NH2
REMARK 470 LYS D 160 CE NZ
REMARK 470 LYS D 194 CD CE NZ
REMARK 470 ARG D 212 NE CZ NH1 NH2
REMARK 470 ILE D 219 CG1 CD1
REMARK 470 ARG D 291 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 314 CD CE NZ
REMARK 470 ARG D 321 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 OP2 DA F 11 O HOH F 373 1.81
REMARK 500 N GLN B 143 O HOH B 380 1.87
REMARK 500 O PRO B 133 O HOH B 368 1.91
REMARK 500 OG1 THR B 199 O HOH B 392 1.95
REMARK 500 O2 DT F 10 O HOH F 371 1.99
REMARK 500 N7 DA E 11 O HOH E 369 2.02
REMARK 500 O ILE A 166 O HOH A 383 2.04
REMARK 500 OE1 GLN B 143 O HOH B 380 2.06
REMARK 500 OG SER B 211 O HOH B 370 2.15
REMARK 500 O HOH B 97 O HOH B 392 2.16
REMARK 500 N6 DA E 11 O HOH E 369 2.17
REMARK 500 O LYS C 203 O HOH C 5 2.17
REMARK 500 OP2 DT F 12 O HOH F 374 2.18
REMARK 500 N SER C 128 O HOH C 377 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 A 181 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO C 127 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO C 181 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 DA E 5 O4' - C1' - N9 ANGL. DEV. = -5.6 DEGREES
REMARK 500 DT E 10 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DT E 18 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA F 5 O4' - C1' - N9 ANGL. DEV. = -5.3 DEGREES
REMARK 500 DT F 6 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DA F 15 O4' - C1' - C2' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DC F 16 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT F 18 P - O5' - C5' ANGL. DEV. = -11.7 DEGREES
REMARK 500 DT F 18 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DT F 21 O4' - C1' - N1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DT F 21 N3 - C4 - O4 ANGL. DEV. = 3.7 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 PRO A 135 -8.40 -54.70
REMARK 500 SER A 137 53.21 38.40
REMARK 500 SER A 146 97.74 -40.45
REMARK 500 THR A 147 13.42 -65.14
REMARK 500 ALA A 148 77.64 -69.04
REMARK 500 LYS A 149 -59.27 22.45
REMARK 500 SER A 150 37.28 -91.95
REMARK 500 ALA A 167 -29.53 68.33
REMARK 500 PRO A 181 -168.89 -53.72
REMARK 500 GLN A 182 -78.15 -46.58
REMARK 500 ALA A 184 163.13 -48.12
REMARK 500 VAL A 198 -27.64 -36.12
REMARK 500 SER A 211 160.08 -44.20
REMARK 500 PHE A 214 -17.31 76.98
REMARK 500 GLU A 216 -85.86 -1.50
REMARK 500 ILE A 219 23.68 -70.17
REMARK 500 PRO A 222 -8.37 -46.52
REMARK 500 SER A 271 32.68 -81.87
REMARK 500 SER A 272 13.01 -151.95
REMARK 500 ASN A 278 50.72 32.37
REMARK 500 ALA B 125 157.10 -37.02
REMARK 500 SER B 137 56.62 38.84
REMARK 500 ALA B 151 -173.03 -54.49
REMARK 500 THR B 154 148.45 -174.13
REMARK 500 ALA B 167 -16.59 61.98
REMARK 500 PRO B 181 -154.85 -56.20
REMARK 500 GLN B 182 -95.76 -63.67
REMARK 500 PHE B 214 -3.01 73.41
REMARK 500 GLU B 216 -91.34 -52.80
REMARK 500 GLN B 218 136.37 -171.72
REMARK 500 PRO B 253 170.44 -55.08
REMARK 500 ARG B 321 33.14 -71.45
REMARK 500 PRO C 127 138.69 -32.49
REMARK 500 SER C 146 22.40 30.09
REMARK 500 THR C 147 -66.49 18.18
REMARK 500 ALA C 148 -12.15 43.72
REMARK 500 LYS C 149 -21.54 78.50
REMARK 500 ALA C 167 -21.68 72.82
REMARK 500 PRO C 181 -156.58 -38.28
REMARK 500 GLN C 182 -80.75 -81.92
REMARK 500 ALA C 184 131.76 -37.48
REMARK 500 GLU C 196 -18.51 -47.33
REMARK 500 VAL C 198 -23.21 -37.42
REMARK 500 PHE C 214 -19.25 82.76
REMARK 500 GLU C 216 -75.16 -24.02
REMARK 500 SER C 272 0.46 -62.79
REMARK 500 ASN C 278 52.66 36.21
REMARK 500 LYS D 160 46.85 37.19
REMARK 500 ALA D 167 -22.89 57.89
REMARK 500 PRO D 181 -148.14 -57.52
REMARK 500
REMARK 500 THIS ENTRY HAS 55 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 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 205 SG
REMARK 620 2 HIS A 208 ND1 108.6
REMARK 620 3 CYS A 269 SG 107.7 115.6
REMARK 620 4 CYS A 273 SG 103.9 103.5 116.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 205 SG
REMARK 620 2 HIS B 208 ND1 102.6
REMARK 620 3 CYS B 269 SG 105.9 110.4
REMARK 620 4 CYS B 273 SG 121.5 105.6 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 205 SG
REMARK 620 2 HIS C 208 ND1 106.0
REMARK 620 3 CYS C 269 SG 112.7 111.9
REMARK 620 4 CYS C 273 SG 107.9 102.9 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 205 SG
REMARK 620 2 HIS D 208 ND1 100.5
REMARK 620 3 CYS D 269 SG 110.9 112.6
REMARK 620 4 CYS D 273 SG 117.7 100.8 113.2
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QYM RELATED DB: PDB
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 10 BASE PAIR
REMARK 900 A/T RICH RESPONSE ELEMENT HALF SITE
REMARK 900 RELATED ID: 3QYN RELATED DB: PDB
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR
REMARK 900 A/T RICH RESPONSE ELEMENT CONTAINING 2 BASE PAIR SPACER BETWEEN
REMARK 900 HALF SITES
REMARK 900 RELATED ID: 3US1 RELATED DB: PDB
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR
REMARK 900 RESPONSE ELEMENT CONTAINING A TWO BASE PAIR "GC" SPACER BETWEEN
REMARK 900 HALF SITES
REMARK 900 RELATED ID: 3US2 RELATED DB: PDB
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 19 BASE PAIR
REMARK 900 A/T RICH RESPONSE ELEMENT CONTAINING TWO HALF SITES WITH A SINGLE
REMARK 900 BASE PAIR OVERLAP
DBREF 3US0 A 127 323 UNP Q9H3D4 P63_HUMAN 166 362
DBREF 3US0 B 127 323 UNP Q9H3D4 P63_HUMAN 166 362
DBREF 3US0 C 127 323 UNP Q9H3D4 P63_HUMAN 166 362
DBREF 3US0 D 127 323 UNP Q9H3D4 P63_HUMAN 166 362
DBREF 3US0 E 1 22 PDB 3US0 3US0 1 22
DBREF 3US0 F 1 22 PDB 3US0 3US0 1 22
SEQADV 3US0 GLY A 121 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER A 122 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 HIS A 123 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 MET A 124 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 ALA A 125 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER A 126 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 GLY B 121 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER B 122 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 HIS B 123 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 MET B 124 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 ALA B 125 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER B 126 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 GLY C 121 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER C 122 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 HIS C 123 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 MET C 124 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 ALA C 125 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER C 126 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 GLY D 121 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER D 122 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 HIS D 123 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 MET D 124 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 ALA D 125 UNP Q9H3D4 EXPRESSION TAG
SEQADV 3US0 SER D 126 UNP Q9H3D4 EXPRESSION TAG
SEQRES 1 A 203 GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO
SEQRES 2 A 203 GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER
SEQRES 3 A 203 THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU
SEQRES 4 A 203 LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE
SEQRES 5 A 203 GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL
SEQRES 6 A 203 ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL
SEQRES 7 A 203 THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER
SEQRES 8 A 203 ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS
SEQRES 9 A 203 LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL
SEQRES 10 A 203 GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO
SEQRES 11 A 203 TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL
SEQRES 12 A 203 LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY
SEQRES 13 A 203 MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU
SEQRES 14 A 203 THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU
SEQRES 15 A 203 ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA
SEQRES 16 A 203 ASP GLU ASP SER ILE ARG LYS GLN
SEQRES 1 B 203 GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO
SEQRES 2 B 203 GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER
SEQRES 3 B 203 THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU
SEQRES 4 B 203 LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE
SEQRES 5 B 203 GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL
SEQRES 6 B 203 ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL
SEQRES 7 B 203 THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER
SEQRES 8 B 203 ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS
SEQRES 9 B 203 LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL
SEQRES 10 B 203 GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO
SEQRES 11 B 203 TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL
SEQRES 12 B 203 LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY
SEQRES 13 B 203 MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU
SEQRES 14 B 203 THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU
SEQRES 15 B 203 ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA
SEQRES 16 B 203 ASP GLU ASP SER ILE ARG LYS GLN
SEQRES 1 C 203 GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO
SEQRES 2 C 203 GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER
SEQRES 3 C 203 THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU
SEQRES 4 C 203 LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE
SEQRES 5 C 203 GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL
SEQRES 6 C 203 ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL
SEQRES 7 C 203 THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER
SEQRES 8 C 203 ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS
SEQRES 9 C 203 LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL
SEQRES 10 C 203 GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO
SEQRES 11 C 203 TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL
SEQRES 12 C 203 LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY
SEQRES 13 C 203 MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU
SEQRES 14 C 203 THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU
SEQRES 15 C 203 ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA
SEQRES 16 C 203 ASP GLU ASP SER ILE ARG LYS GLN
SEQRES 1 D 203 GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO
SEQRES 2 D 203 GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER
SEQRES 3 D 203 THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU
SEQRES 4 D 203 LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE
SEQRES 5 D 203 GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL
SEQRES 6 D 203 ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL
SEQRES 7 D 203 THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER
SEQRES 8 D 203 ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS
SEQRES 9 D 203 LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL
SEQRES 10 D 203 GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO
SEQRES 11 D 203 TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL
SEQRES 12 D 203 LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY
SEQRES 13 D 203 MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU
SEQRES 14 D 203 THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU
SEQRES 15 D 203 ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA
SEQRES 16 D 203 ASP GLU ASP SER ILE ARG LYS GLN
SEQRES 1 E 22 DA DA DA DC DA DT DG DT DT DT DA DT DA
SEQRES 2 E 22 DA DA DC DA DT DG DT DT DT
SEQRES 1 F 22 DA DA DA DC DA DT DG DT DT DT DA DT DA
SEQRES 2 F 22 DA DA DC DA DT DG DT DT DT
HET ZN A 901 1
HET ZN B 901 1
HET ZN C 901 1
HET ZN D 901 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 4(ZN 2+)
FORMUL 11 HOH *394(H2 O)
HELIX 1 1 PRO A 133 SER A 137 5 5
HELIX 2 2 CYS A 205 SER A 211 1 7
HELIX 3 3 CYS A 308 GLU A 317 1 10
HELIX 4 4 CYS B 205 SER B 211 1 7
HELIX 5 5 CYS B 308 ILE B 320 1 13
HELIX 6 6 CYS C 205 SER C 211 1 7
HELIX 7 7 CYS C 308 SER C 319 1 12
HELIX 8 8 CYS D 205 SER D 211 1 7
HELIX 9 9 CYS D 308 ARG D 321 1 14
SHEET 1 A 4 ASP A 139 SER A 141 0
SHEET 2 A 4 THR A 169 LYS A 175 -1 O GLN A 173 N SER A 141
SHEET 3 A 4 THR A 261 PHE A 267 -1 O VAL A 263 N ILE A 172
SHEET 4 A 4 ILE A 226 GLU A 229 -1 N ARG A 227 O ASN A 266
SHEET 1 B 7 TRP A 153 SER A 156 0
SHEET 2 B 7 LYS A 161 CYS A 164 -1 O TYR A 163 N THR A 154
SHEET 3 B 7 VAL A 295 ILE A 305 1 O ARG A 304 N LEU A 162
SHEET 4 B 7 ILE A 282 GLU A 289 -1 N LEU A 288 O GLY A 297
SHEET 5 B 7 VAL A 185 TYR A 192 -1 N VAL A 185 O GLU A 289
SHEET 6 B 7 GLN A 245 PRO A 250 -1 O VAL A 249 N ILE A 186
SHEET 7 B 7 GLN A 235 GLU A 238 -1 N GLN A 235 O LEU A 248
SHEET 1 C 4 ASP B 139 SER B 141 0
SHEET 2 C 4 THR B 169 LYS B 175 -1 O GLN B 173 N SER B 141
SHEET 3 C 4 THR B 261 PHE B 267 -1 O TYR B 265 N CYS B 170
SHEET 4 C 4 ILE B 226 VAL B 228 -1 N ARG B 227 O ASN B 266
SHEET 1 D 7 TRP B 153 SER B 156 0
SHEET 2 D 7 LYS B 161 CYS B 164 -1 O TYR B 163 N THR B 154
SHEET 3 D 7 VAL B 295 ILE B 305 1 O GLU B 302 N LEU B 162
SHEET 4 D 7 ILE B 282 GLU B 289 -1 N ILE B 284 O PHE B 301
SHEET 5 D 7 VAL B 185 TYR B 192 -1 N MET B 189 O ILE B 285
SHEET 6 D 7 GLN B 245 PRO B 250 -1 O VAL B 249 N ILE B 186
SHEET 7 D 7 GLN B 235 GLU B 238 -1 N GLN B 235 O LEU B 248
SHEET 1 E 4 ASP C 139 SER C 141 0
SHEET 2 E 4 THR C 169 LYS C 175 -1 O GLN C 173 N SER C 141
SHEET 3 E 4 THR C 261 PHE C 267 -1 O THR C 261 N ILE C 174
SHEET 4 E 4 ILE C 226 VAL C 228 -1 N ARG C 227 O ASN C 266
SHEET 1 F 7 TRP C 153 SER C 156 0
SHEET 2 F 7 LYS C 161 CYS C 164 -1 O TYR C 163 N THR C 154
SHEET 3 F 7 VAL C 295 ARG C 304 1 O GLU C 302 N LEU C 162
SHEET 4 F 7 ILE C 282 GLU C 289 -1 N LEU C 288 O LEU C 296
SHEET 5 F 7 VAL C 185 TYR C 192 -1 N VAL C 185 O GLU C 289
SHEET 6 F 7 GLN C 245 PRO C 250 -1 O VAL C 249 N ILE C 186
SHEET 7 F 7 GLN C 235 GLU C 238 -1 N VAL C 237 O SER C 246
SHEET 1 G 4 ASP D 139 SER D 141 0
SHEET 2 G 4 THR D 169 LYS D 175 -1 O GLN D 173 N SER D 141
SHEET 3 G 4 THR D 261 PHE D 267 -1 O TYR D 265 N CYS D 170
SHEET 4 G 4 ILE D 226 VAL D 228 -1 N ARG D 227 O ASN D 266
SHEET 1 H 7 TRP D 153 SER D 156 0
SHEET 2 H 7 LYS D 161 GLN D 165 -1 O TYR D 163 N THR D 154
SHEET 3 H 7 VAL D 295 CYS D 306 1 O ARG D 304 N LEU D 162
SHEET 4 H 7 ILE D 282 GLU D 289 -1 N ILE D 284 O PHE D 301
SHEET 5 H 7 VAL D 185 TYR D 192 -1 N ARG D 187 O THR D 287
SHEET 6 H 7 GLN D 245 PRO D 250 -1 O VAL D 249 N ILE D 186
SHEET 7 H 7 GLN D 235 GLU D 238 -1 N GLN D 235 O LEU D 248
LINK SG CYS A 205 ZN ZN A 901 1555 1555 2.38
LINK ND1 HIS A 208 ZN ZN A 901 1555 1555 2.09
LINK SG CYS A 269 ZN ZN A 901 1555 1555 2.31
LINK SG CYS A 273 ZN ZN A 901 1555 1555 2.30
LINK SG CYS B 205 ZN ZN B 901 1555 1555 2.31
LINK ND1 HIS B 208 ZN ZN B 901 1555 1555 2.12
LINK SG CYS B 269 ZN ZN B 901 1555 1555 2.36
LINK SG CYS B 273 ZN ZN B 901 1555 1555 2.35
LINK SG CYS C 205 ZN ZN C 901 1555 1555 2.36
LINK ND1 HIS C 208 ZN ZN C 901 1555 1555 2.12
LINK SG CYS C 269 ZN ZN C 901 1555 1555 2.35
LINK SG CYS C 273 ZN ZN C 901 1555 1555 2.31
LINK SG CYS D 205 ZN ZN D 901 1555 1555 2.32
LINK ND1 HIS D 208 ZN ZN D 901 1555 1555 2.15
LINK SG CYS D 269 ZN ZN D 901 1555 1555 2.34
LINK SG CYS D 273 ZN ZN D 901 1555 1555 2.32
SITE 1 AC1 4 CYS A 205 HIS A 208 CYS A 269 CYS A 273
SITE 1 AC2 4 CYS B 205 HIS B 208 CYS B 269 CYS B 273
SITE 1 AC3 4 CYS C 205 HIS C 208 CYS C 269 CYS C 273
SITE 1 AC4 4 CYS D 205 HIS D 208 CYS D 269 CYS D 273
CRYST1 141.806 141.806 119.604 90.00 90.00 120.00 P 63 24
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 0.007052 0.004071 0.000000 0.00000
SCALE2 0.000000 0.008143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008361 0.00000
(ATOM LINES ARE NOT SHOWN.)
END