HEADER TRANSCRIPTION 28-MAR-17 5NJ8
TITLE STRUCTURAL BASIS FOR ARYL HYDROCARBON RECEPTOR MEDIATED GENE
TITLE 2 ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYL HYDROCARBON RECEPTOR;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: AHR,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 76,BHLHE76;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: ARNT PROTEIN,DIOXIN RECEPTOR,NUCLEAR TRANSLOCATOR,HYPOXIA-
COMPND 10 INDUCIBLE FACTOR 1-BETA,HIF1-BETA;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 OTHER_DETAILS: INTERNAL DELETION OF 274-301;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-D(*GP*GP*TP*CP*AP*CP*GP*CP*AP*AP*CP*C)-3');
COMPND 16 CHAIN: E, G;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: DIOXIN RESPONSE ELEMENT;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: DNA (5'-D(*GP*GP*TP*TP*GP*CP*GP*TP*GP*AP*CP*C)-3');
COMPND 21 CHAIN: F, H;
COMPND 22 ENGINEERED: YES;
COMPND 23 OTHER_DETAILS: DIOXIN RESPONSE ELEMENT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AHR, BHLHE76;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTE;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: ARNT;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 MOL_ID: 4;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606
KEYWDS BASIC HELIX LOOP HELIX PAS DOMAIN TRANSCRIPTION FACTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DAUMKE,K.W.SCHULTE
REVDAT 3 05-FEB-20 5NJ8 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQADV SEQRES SHEET LINK
REVDAT 3 3 1 SITE ATOM
REVDAT 2 19-JUL-17 5NJ8 1
REVDAT 1 28-JUN-17 5NJ8 0
JRNL AUTH K.W.SCHULTE,E.GREEN,A.WILZ,M.PLATTEN,O.DAUMKE
JRNL TITL STRUCTURAL BASIS FOR ARYL HYDROCARBON RECEPTOR-MEDIATED GENE
JRNL TITL 2 ACTIVATION.
JRNL REF STRUCTURE V. 25 1025 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28602820
JRNL DOI 10.1016/J.STR.2017.05.008
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 18323
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.294
REMARK 3 R VALUE (WORKING SET) : 0.292
REMARK 3 FREE R VALUE : 0.333
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 917
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 46.8351 - 6.3085 1.00 2751 145 0.2821 0.2952
REMARK 3 2 6.3085 - 5.0091 1.00 2536 134 0.2990 0.3318
REMARK 3 3 5.0091 - 4.3764 1.00 2479 130 0.2715 0.3325
REMARK 3 4 4.3764 - 3.9765 1.00 2452 129 0.2850 0.3353
REMARK 3 5 3.9765 - 3.6916 1.00 2451 130 0.3184 0.3985
REMARK 3 6 3.6916 - 3.4740 0.98 2385 125 0.3246 0.3621
REMARK 3 7 3.4740 - 3.3001 0.98 2352 124 0.3163 0.4147
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.160
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 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 : 0.005 6042
REMARK 3 ANGLE : 0.678 8337
REMARK 3 CHIRALITY : 0.042 981
REMARK 3 PLANARITY : 0.004 908
REMARK 3 DIHEDRAL : 16.888 3448
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 34 THROUGH 88)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5124 29.3907 200.4939
REMARK 3 T TENSOR
REMARK 3 T11: 1.4833 T22: 0.4494
REMARK 3 T33: 0.3373 T12: 0.1718
REMARK 3 T13: -0.0832 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.2699 L22: 0.9239
REMARK 3 L33: 0.0466 L12: -0.0621
REMARK 3 L13: -0.0438 L23: 0.1988
REMARK 3 S TENSOR
REMARK 3 S11: -0.2327 S12: -0.0669 S13: 0.1527
REMARK 3 S21: -0.1365 S22: -0.0351 S23: -0.3148
REMARK 3 S31: -0.0871 S32: 0.0586 S33: -0.0623
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 85 THROUGH 143)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9332 21.9640 200.0559
REMARK 3 T TENSOR
REMARK 3 T11: 1.2829 T22: 0.5549
REMARK 3 T33: 0.8809 T12: 0.2819
REMARK 3 T13: -0.1693 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 0.2473 L22: 0.0554
REMARK 3 L33: 0.1466 L12: -0.1243
REMARK 3 L13: 0.0911 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.2861 S12: -0.0100 S13: -0.1566
REMARK 3 S21: -0.0785 S22: 0.0042 S23: 0.3563
REMARK 3 S31: -0.1254 S32: 0.1546 S33: 0.0032
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 32 THROUGH 88)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9371 24.7156 229.6474
REMARK 3 T TENSOR
REMARK 3 T11: 0.3551 T22: 0.2080
REMARK 3 T33: 0.6653 T12: 0.0903
REMARK 3 T13: -0.0151 T23: 0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 0.0031 L22: 0.1833
REMARK 3 L33: 0.8193 L12: 0.0205
REMARK 3 L13: 0.0467 L23: 0.3670
REMARK 3 S TENSOR
REMARK 3 S11: -0.1827 S12: 0.0220 S13: 0.0576
REMARK 3 S21: -0.0635 S22: -0.2832 S23: -0.3442
REMARK 3 S31: -0.1078 S32: -0.0914 S33: -0.1862
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 84 THROUGH 144)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6089 15.0120 232.6177
REMARK 3 T TENSOR
REMARK 3 T11: 0.3010 T22: 0.2692
REMARK 3 T33: 0.3283 T12: 0.0017
REMARK 3 T13: -0.0436 T23: 0.0916
REMARK 3 L TENSOR
REMARK 3 L11: -0.0196 L22: 0.2110
REMARK 3 L33: 0.1016 L12: 0.0390
REMARK 3 L13: -0.0036 L23: -0.1124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0882 S12: -0.0731 S13: 0.1305
REMARK 3 S21: -0.1875 S22: -0.3340 S23: -0.2363
REMARK 3 S31: 0.1621 S32: 0.0418 S33: -0.0425
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 12)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1903 9.9676 197.5579
REMARK 3 T TENSOR
REMARK 3 T11: 1.4249 T22: 0.7188
REMARK 3 T33: 0.6163 T12: 0.1182
REMARK 3 T13: -0.2259 T23: -0.1332
REMARK 3 L TENSOR
REMARK 3 L11: -0.0005 L22: 0.0027
REMARK 3 L33: -0.0014 L12: 0.0108
REMARK 3 L13: -0.0009 L23: 0.0028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0539 S12: -0.1525 S13: -0.2233
REMARK 3 S21: -0.3816 S22: 0.2069 S23: -0.0485
REMARK 3 S31: 0.1315 S32: 0.0885 S33: 0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 12)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4227 9.7617 198.6716
REMARK 3 T TENSOR
REMARK 3 T11: 1.5450 T22: 0.8069
REMARK 3 T33: 0.6398 T12: 0.0689
REMARK 3 T13: -0.2587 T23: -0.0837
REMARK 3 L TENSOR
REMARK 3 L11: 0.0957 L22: 0.1435
REMARK 3 L33: 0.0879 L12: 0.1293
REMARK 3 L13: 0.0163 L23: 0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.1713 S12: 0.4695 S13: -0.6142
REMARK 3 S21: 0.0072 S22: 0.5784 S23: -0.3336
REMARK 3 S31: -0.0675 S32: -0.2281 S33: -0.0007
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 1 THROUGH 12)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9389 11.0616 237.1803
REMARK 3 T TENSOR
REMARK 3 T11: 0.7124 T22: 0.5325
REMARK 3 T33: 0.3354 T12: -0.0006
REMARK 3 T13: 0.1393 T23: 0.2054
REMARK 3 L TENSOR
REMARK 3 L11: 0.1755 L22: 0.4786
REMARK 3 L33: 0.3410 L12: -0.0410
REMARK 3 L13: 0.2277 L23: 0.1408
REMARK 3 S TENSOR
REMARK 3 S11: 0.5140 S12: 0.1867 S13: 0.2541
REMARK 3 S21: 0.2765 S22: 0.0035 S23: -0.1642
REMARK 3 S31: -0.1716 S32: -0.2954 S33: 0.7327
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 12)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0052 11.6430 236.3805
REMARK 3 T TENSOR
REMARK 3 T11: 0.8036 T22: 0.6394
REMARK 3 T33: 0.5958 T12: -0.0360
REMARK 3 T13: 0.0071 T23: 0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 0.0293 L22: 0.0661
REMARK 3 L33: 0.0225 L12: 0.0017
REMARK 3 L13: -0.0273 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.2187 S13: 0.1312
REMARK 3 S21: 0.4070 S22: -0.0128 S23: 0.0605
REMARK 3 S31: -0.1287 S32: -0.3221 S33: -0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 109 THROUGH 272)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0569 42.1127 218.9071
REMARK 3 T TENSOR
REMARK 3 T11: 0.4731 T22: -0.2680
REMARK 3 T33: 0.1554 T12: 0.3860
REMARK 3 T13: -0.0991 T23: 0.3090
REMARK 3 L TENSOR
REMARK 3 L11: 0.1233 L22: 0.1297
REMARK 3 L33: 0.2779 L12: -0.1351
REMARK 3 L13: 0.1955 L23: -0.1765
REMARK 3 S TENSOR
REMARK 3 S11: 0.3959 S12: -0.0544 S13: -0.0169
REMARK 3 S21: 0.1019 S22: 0.1504 S23: -0.0312
REMARK 3 S31: -0.0217 S32: 0.0157 S33: 0.7988
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 152 THROUGH 345)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0154 60.0065 220.0690
REMARK 3 T TENSOR
REMARK 3 T11: 0.5575 T22: -0.0410
REMARK 3 T33: 0.5296 T12: -0.0014
REMARK 3 T13: 0.1528 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.1961 L22: 0.0915
REMARK 3 L33: 0.1288 L12: 0.1619
REMARK 3 L13: 0.0515 L23: -0.0189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0585 S12: -0.0224 S13: 0.0896
REMARK 3 S21: -0.1199 S22: 0.0765 S23: 0.2342
REMARK 3 S31: -0.0943 S32: 0.0821 S33: 0.1120
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 107 THROUGH 271)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5148 19.5600 211.2753
REMARK 3 T TENSOR
REMARK 3 T11: 0.7918 T22: 0.2526
REMARK 3 T33: 0.3310 T12: 0.3221
REMARK 3 T13: 0.7203 T23: -0.0830
REMARK 3 L TENSOR
REMARK 3 L11: 0.0330 L22: 0.1529
REMARK 3 L33: 0.0217 L12: -0.0677
REMARK 3 L13: -0.0283 L23: 0.0442
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: -0.0116 S13: 0.1612
REMARK 3 S21: 0.0323 S22: -0.1037 S23: -0.1770
REMARK 3 S31: 0.1963 S32: 0.0377 S33: -0.3197
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 148 THROUGH 342)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7449 36.0055 207.7890
REMARK 3 T TENSOR
REMARK 3 T11: 0.5686 T22: 0.3876
REMARK 3 T33: 0.7282 T12: -0.0558
REMARK 3 T13: 0.5646 T23: 0.2661
REMARK 3 L TENSOR
REMARK 3 L11: 0.0687 L22: 0.0322
REMARK 3 L33: 0.0224 L12: 0.0377
REMARK 3 L13: 0.0334 L23: 0.0184
REMARK 3 S TENSOR
REMARK 3 S11: 0.2249 S12: -0.2769 S13: -0.1054
REMARK 3 S21: 0.0095 S22: 0.0376 S23: -0.3818
REMARK 3 S31: 0.0816 S32: -0.3589 S33: 0.2199
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 5NJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.476
REMARK 200 MONOCHROMATOR : SI111-DCM WITH SAGITAL BENDER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32653
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 18.00
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.09800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 16.50
REMARK 200 R MERGE FOR SHELL (I) : 0.66200
REMARK 200 R SYM FOR SHELL (I) : 0.68300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.110
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM HEPES/NAOH PH 6.8, 18% PEG3350,
REMARK 280 200 MM AMMONIUM FORMATE, PH 6.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 309.94267
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 154.97133
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 232.45700
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 77.48567
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 387.42833
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 309.94267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 154.97133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 77.48567
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 232.45700
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 387.42833
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ER ER3 H 101 LIES ON A SPECIAL POSITION.
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 20
REMARK 465 PRO A 21
REMARK 465 MET A 22
REMARK 465 VAL A 23
REMARK 465 LYS A 24
REMARK 465 PRO A 25
REMARK 465 ILE A 26
REMARK 465 PRO A 27
REMARK 465 ALA A 28
REMARK 465 GLU A 29
REMARK 465 GLY A 30
REMARK 465 ILE A 31
REMARK 465 LYS A 32
REMARK 465 SER A 33
REMARK 465 SER A 89
REMARK 465 SER A 90
REMARK 465 PRO A 91
REMARK 465 THR A 92
REMARK 465 GLU A 93
REMARK 465 ARG A 94
REMARK 465 ASN A 95
REMARK 465 GLY A 96
REMARK 465 GLY A 97
REMARK 465 GLN A 98
REMARK 465 ASP A 99
REMARK 465 ASN A 100
REMARK 465 CYS A 101
REMARK 465 ARG A 102
REMARK 465 ALA A 103
REMARK 465 ALA A 104
REMARK 465 ASN A 105
REMARK 465 PHE A 106
REMARK 465 ARG A 107
REMARK 465 GLU A 108
REMARK 465 ALA A 177
REMARK 465 LEU A 178
REMARK 465 ASN A 179
REMARK 465 PRO A 180
REMARK 465 SER A 181
REMARK 465 GLN A 182
REMARK 465 CYS A 183
REMARK 465 THR A 184
REMARK 465 GLU A 185
REMARK 465 SER A 186
REMARK 465 GLY A 187
REMARK 465 GLN A 188
REMARK 465 GLY A 189
REMARK 465 ILE A 190
REMARK 465 GLU A 191
REMARK 465 GLU A 192
REMARK 465 ALA A 193
REMARK 465 THR A 194
REMARK 465 GLY A 195
REMARK 465 LEU A 196
REMARK 465 PRO A 197
REMARK 465 GLN A 198
REMARK 465 THR A 199
REMARK 465 VAL A 200
REMARK 465 VAL A 201
REMARK 465 CYS A 202
REMARK 465 TYR A 203
REMARK 465 ASN A 204
REMARK 465 PRO A 205
REMARK 465 ASP A 206
REMARK 465 GLN A 207
REMARK 465 ILE A 208
REMARK 465 ASN A 230
REMARK 465 LYS A 251
REMARK 465 LYS A 252
REMARK 465 GLY A 253
REMARK 465 LYS A 254
REMARK 465 ASP A 255
REMARK 465 GLY A 256
REMARK 465 SER A 257
REMARK 465 ILE A 258
REMARK 465 LEU A 259
REMARK 465 PRO A 260
REMARK 465 GLN A 273
REMARK 465 GLY B 79
REMARK 465 PRO B 80
REMARK 465 GLY B 81
REMARK 465 SER B 82
REMARK 465 ASP B 83
REMARK 465 ALA B 84
REMARK 465 SER B 120
REMARK 465 ALA B 121
REMARK 465 LEU B 122
REMARK 465 ALA B 123
REMARK 465 ARG B 124
REMARK 465 LYS B 125
REMARK 465 GLY B 144
REMARK 465 THR B 145
REMARK 465 GLY B 146
REMARK 465 ASN B 147
REMARK 465 THR B 148
REMARK 465 SER B 149
REMARK 465 THR B 150
REMARK 465 ASP B 151
REMARK 465 GLU B 229
REMARK 465 ASN B 230
REMARK 465 ALA B 231
REMARK 465 LEU B 232
REMARK 465 THR B 233
REMARK 465 GLY B 234
REMARK 465 ARG B 235
REMARK 465 VAL B 236
REMARK 465 LEU B 237
REMARK 465 ASP B 238
REMARK 465 LEU B 239
REMARK 465 LYS B 240
REMARK 465 THR B 241
REMARK 465 GLY B 242
REMARK 465 THR B 243
REMARK 465 VAL B 244
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 GLU B 247
REMARK 465 GLY B 248
REMARK 465 GLN B 249
REMARK 465 GLN B 250
REMARK 465 SER B 251
REMARK 465 SER B 252
REMARK 465 MET B 253
REMARK 465 ARG B 254
REMARK 465 MET B 255
REMARK 465 SER B 256
REMARK 465 MET B 257
REMARK 465 GLY B 258
REMARK 465 GLY B 298
REMARK 465 THR B 299
REMARK 465 SER B 300
REMARK 465 SER B 301
REMARK 465 PRO B 317
REMARK 465 ALA B 318
REMARK 465 GLY B 319
REMARK 465 VAL B 320
REMARK 465 SER B 321
REMARK 465 LEU B 322
REMARK 465 PRO B 323
REMARK 465 GLY B 330
REMARK 465 GLN B 331
REMARK 465 GLY B 332
REMARK 465 SER B 333
REMARK 465 GLY C 20
REMARK 465 PRO C 21
REMARK 465 MET C 22
REMARK 465 VAL C 23
REMARK 465 LYS C 24
REMARK 465 PRO C 25
REMARK 465 ILE C 26
REMARK 465 PRO C 27
REMARK 465 ALA C 28
REMARK 465 GLU C 29
REMARK 465 GLY C 30
REMARK 465 ILE C 31
REMARK 465 SER C 89
REMARK 465 SER C 90
REMARK 465 PRO C 91
REMARK 465 THR C 92
REMARK 465 GLU C 93
REMARK 465 ARG C 94
REMARK 465 ASN C 95
REMARK 465 GLY C 96
REMARK 465 GLY C 97
REMARK 465 GLN C 98
REMARK 465 ASP C 99
REMARK 465 ASN C 100
REMARK 465 CYS C 101
REMARK 465 ARG C 102
REMARK 465 ALA C 103
REMARK 465 ALA C 104
REMARK 465 ASN C 105
REMARK 465 PHE C 106
REMARK 465 LEU C 174
REMARK 465 HIS C 175
REMARK 465 TRP C 176
REMARK 465 ALA C 177
REMARK 465 LEU C 178
REMARK 465 ASN C 179
REMARK 465 PRO C 180
REMARK 465 SER C 181
REMARK 465 GLN C 182
REMARK 465 CYS C 183
REMARK 465 THR C 184
REMARK 465 GLU C 185
REMARK 465 SER C 186
REMARK 465 GLY C 187
REMARK 465 GLN C 188
REMARK 465 GLY C 189
REMARK 465 ILE C 190
REMARK 465 GLU C 191
REMARK 465 GLU C 192
REMARK 465 ALA C 193
REMARK 465 THR C 194
REMARK 465 GLY C 195
REMARK 465 LEU C 196
REMARK 465 PRO C 197
REMARK 465 GLN C 198
REMARK 465 THR C 199
REMARK 465 VAL C 200
REMARK 465 VAL C 201
REMARK 465 CYS C 202
REMARK 465 TYR C 203
REMARK 465 ASN C 204
REMARK 465 PRO C 205
REMARK 465 ASP C 206
REMARK 465 GLN C 207
REMARK 465 ILE C 208
REMARK 465 PRO C 209
REMARK 465 PRO C 210
REMARK 465 LEU C 228
REMARK 465 ASP C 229
REMARK 465 ASN C 230
REMARK 465 SER C 231
REMARK 465 SER C 232
REMARK 465 GLY C 233
REMARK 465 LYS C 252
REMARK 465 GLY C 253
REMARK 465 LYS C 254
REMARK 465 LEU C 272
REMARK 465 GLN C 273
REMARK 465 GLY D 79
REMARK 465 PRO D 80
REMARK 465 GLY D 81
REMARK 465 SER D 82
REMARK 465 ASP D 83
REMARK 465 THR D 145
REMARK 465 GLY D 146
REMARK 465 ASN D 147
REMARK 465 GLY D 174
REMARK 465 ILE D 178
REMARK 465 VAL D 179
REMARK 465 SER D 180
REMARK 465 CYS D 181
REMARK 465 GLU D 182
REMARK 465 THR D 183
REMARK 465 GLY D 184
REMARK 465 ARG D 185
REMARK 465 VAL D 186
REMARK 465 VAL D 187
REMARK 465 LEU D 197
REMARK 465 ASN D 198
REMARK 465 TRP D 204
REMARK 465 PHE D 205
REMARK 465 GLY D 206
REMARK 465 GLN D 212
REMARK 465 VAL D 213
REMARK 465 HIS D 214
REMARK 465 PRO D 215
REMARK 465 ASP D 216
REMARK 465 ASP D 217
REMARK 465 VAL D 218
REMARK 465 ASP D 219
REMARK 465 LYS D 220
REMARK 465 LEU D 221
REMARK 465 ARG D 222
REMARK 465 GLU D 223
REMARK 465 GLN D 224
REMARK 465 LEU D 225
REMARK 465 SER D 226
REMARK 465 THR D 227
REMARK 465 SER D 228
REMARK 465 GLU D 229
REMARK 465 ASN D 230
REMARK 465 ALA D 231
REMARK 465 LEU D 232
REMARK 465 THR D 233
REMARK 465 GLY D 234
REMARK 465 ARG D 235
REMARK 465 VAL D 236
REMARK 465 LEU D 237
REMARK 465 ASP D 238
REMARK 465 LEU D 239
REMARK 465 LYS D 240
REMARK 465 THR D 241
REMARK 465 GLY D 242
REMARK 465 THR D 243
REMARK 465 VAL D 244
REMARK 465 LYS D 245
REMARK 465 LYS D 246
REMARK 465 GLU D 247
REMARK 465 GLY D 248
REMARK 465 GLN D 249
REMARK 465 GLN D 250
REMARK 465 SER D 251
REMARK 465 SER D 252
REMARK 465 MET D 253
REMARK 465 ARG D 254
REMARK 465 MET D 255
REMARK 465 SER D 256
REMARK 465 MET D 257
REMARK 465 GLY D 258
REMARK 465 GLY D 298
REMARK 465 THR D 299
REMARK 465 SER D 300
REMARK 465 SER D 301
REMARK 465 HIS D 302
REMARK 465 PHE D 303
REMARK 465 VAL D 304
REMARK 465 VAL D 305
REMARK 465 VAL D 306
REMARK 465 TRP D 315
REMARK 465 PRO D 316
REMARK 465 PRO D 317
REMARK 465 ALA D 318
REMARK 465 GLY D 319
REMARK 465 VAL D 320
REMARK 465 SER D 321
REMARK 465 LEU D 322
REMARK 465 PRO D 323
REMARK 465 ASP D 324
REMARK 465 ASP D 325
REMARK 465 ASP D 326
REMARK 465 PRO D 327
REMARK 465 GLU D 328
REMARK 465 ALA D 329
REMARK 465 GLY D 330
REMARK 465 GLN D 331
REMARK 465 GLY D 332
REMARK 465 SER D 333
REMARK 465 LYS D 334
REMARK 465 PHE D 335
REMARK 465 CYS D 336
REMARK 465 LEU D 343
REMARK 465 GLN D 344
REMARK 465 VAL D 345
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 ARG A 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 88 CG CD CE NZ
REMARK 470 ASP A 132 CG OD1 OD2
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 ASP A 229 CG OD1 OD2
REMARK 470 GLN A 249 CG CD OE1 NE2
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 154 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 PHE B 205 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 324 CG OD1 OD2
REMARK 470 ASP B 325 CG OD1 OD2
REMARK 470 GLU B 328 CG CD OE1 OE2
REMARK 470 LYS B 334 CG CD CE NZ
REMARK 470 LYS C 32 CG CD CE NZ
REMARK 470 LYS C 80 CG CD CE NZ
REMARK 470 LYS C 88 CG CD CE NZ
REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 108 CG CD OE1 OE2
REMARK 470 GLN C 113 CG CD OE1 NE2
REMARK 470 LEU C 122 CG CD1 CD2
REMARK 470 ASN C 123 CG OD1 ND2
REMARK 470 SER C 157 OG
REMARK 470 ILE C 162 CG1 CG2 CD1
REMARK 470 THR C 164 OG1 CG2
REMARK 470 GLU C 165 CG CD OE1 OE2
REMARK 470 ASP C 166 CG OD1 OD2
REMARK 470 ARG C 167 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 170 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 171 CG CD OE1 NE2
REMARK 470 ARG C 172 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 211 CG CD OE1 OE2
REMARK 470 SER C 213 OG
REMARK 470 LEU C 215 CG CD1 CD2
REMARK 470 MET C 216 CG SD CE
REMARK 470 ARG C 218 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 220 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 221 CG1 CG2 CD1
REMARK 470 CYS C 222 SG
REMARK 470 ARG C 223 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 224 CG CD1 CD2
REMARK 470 PHE C 234 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 235 CG CD1 CD2
REMARK 470 MET C 237 CG SD CE
REMARK 470 ASN C 238 CG OD1 ND2
REMARK 470 PHE C 239 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 240 CG CD OE1 NE2
REMARK 470 LYS C 242 CG CD CE NZ
REMARK 470 LEU C 243 CG CD1 CD2
REMARK 470 LYS C 244 CG CD CE NZ
REMARK 470 TYR C 245 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS C 247 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 249 CG CD OE1 NE2
REMARK 470 LYS C 250 CG CD CE NZ
REMARK 470 LYS C 251 CG CD CE NZ
REMARK 470 ASP C 255 CG OD1 OD2
REMARK 470 SER C 257 OG
REMARK 470 ILE C 258 CG1 CG2 CD1
REMARK 470 LEU C 259 CG CD1 CD2
REMARK 470 LEU C 263 CG CD1 CD2
REMARK 470 ILE C 268 CG1 CG2 CD1
REMARK 470 THR C 270 OG1 CG2
REMARK 470 ASP D 85 CG OD1 OD2
REMARK 470 LYS D 86 CG CD CE NZ
REMARK 470 LEU D 89 CG CD1 CD2
REMARK 470 ARG D 100 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 124 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 125 CG CD CE NZ
REMARK 470 LYS D 140 CG CD CE NZ
REMARK 470 THR D 148 OG1 CG2
REMARK 470 SER D 149 OG
REMARK 470 THR D 150 OG1 CG2
REMARK 470 ASP D 151 CG OD1 OD2
REMARK 470 TYR D 154 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 155 CG CD CE NZ
REMARK 470 THR D 160 OG1 CG2
REMARK 470 GLN D 162 CG CD OE1 NE2
REMARK 470 GLU D 163 CG CD OE1 OE2
REMARK 470 LEU D 164 CG CD1 CD2
REMARK 470 LYS D 165 CG CD CE NZ
REMARK 470 LEU D 167 CG CD1 CD2
REMARK 470 ILE D 168 CG1 CG2 CD1
REMARK 470 LEU D 169 CG CD1 CD2
REMARK 470 PHE D 175 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 177 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR D 188 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL D 189 CG1 CG2
REMARK 470 SER D 190 OG
REMARK 470 ASP D 191 CG OD1 OD2
REMARK 470 SER D 192 OG
REMARK 470 VAL D 193 CG1 CG2
REMARK 470 THR D 194 OG1 CG2
REMARK 470 PRO D 195 CG CD
REMARK 470 VAL D 196 CG1 CG2
REMARK 470 GLN D 199 CG CD OE1 NE2
REMARK 470 GLN D 201 CG CD OE1 NE2
REMARK 470 SER D 202 OG
REMARK 470 GLU D 203 CG CD OE1 OE2
REMARK 470 SER D 207 OG
REMARK 470 THR D 208 OG1 CG2
REMARK 470 LEU D 209 CG CD1 CD2
REMARK 470 TYR D 210 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP D 211 CG OD1 OD2
REMARK 470 ARG D 260 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 261 CG CD NE CZ NH1 NH2
REMARK 470 SER D 262 OG
REMARK 470 PHE D 263 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D 264 CG1 CG2 CD1
REMARK 470 ARG D 266 CG CD NE CZ NH1 NH2
REMARK 470 MET D 267 CG SD CE
REMARK 470 ARG D 268 CG CD NE CZ NH1 NH2
REMARK 470 CYS D 269 SG
REMARK 470 HIS D 307 CG ND1 CD2 CE1 NE2
REMARK 470 CYS D 308 SG
REMARK 470 THR D 309 OG1 CG2
REMARK 470 TYR D 311 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE D 312 CG1 CG2 CD1
REMARK 470 LYS D 313 CG CD CE NZ
REMARK 470 LEU D 337 CG CD1 CD2
REMARK 470 VAL D 338 CG1 CG2
REMARK 470 ILE D 340 CG1 CG2 CD1
REMARK 470 ARG D 342 CG CD NE CZ NH1 NH2
REMARK 470 DG E 1 O5'
REMARK 470 DG F 1 O5'
REMARK 470 DG G 1 O5'
REMARK 470 DG H 1 O5'
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 HZ1 LYS B 128 OP2 DG F 5 1.40
REMARK 500 O LEU D 169 H ASP D 173 1.47
REMARK 500 OE2 GLU A 114 HH TYR B 188 1.49
REMARK 500 O TYR A 159 HH21 ARG A 167 1.56
REMARK 500 O2 DC E 11 H22 DG F 2 1.56
REMARK 500 O THR D 160 H LEU D 164 1.59
REMARK 500 HH21 ARG C 40 OP2 DC G 6 1.59
REMARK 500 O TYR B 108 H LEU B 112 1.60
REMARK 500 OD2 ASP D 173 ER ER3 D 401 1.83
REMARK 500 O LEU A 112 OD2 ASP B 161 1.90
REMARK 500 OG SER C 139 OG1 THR C 141 1.99
REMARK 500 O LEU D 169 N ASP D 173 2.05
REMARK 500 OD1 ASP C 65 OG SER C 68 2.06
REMARK 500 OD1 ASN A 62 NE2 GLN C 143 2.11
REMARK 500 O GLU B 92 OG SER B 95 2.12
REMARK 500 O LEU A 228 OG SER A 231 2.12
REMARK 500 NZ LYS B 128 OP2 DG F 5 2.15
REMARK 500 OE2 GLU A 114 OH TYR B 188 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH12 ARG D 88 OP1 DA G 9 8556 1.53
REMARK 500 NH1 ARG D 88 OP1 DA G 9 8556 2.16
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 DT F 3 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT F 4 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC G 11 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC H 11 O4' - C1' - N1 ANGL. DEV. = 2.2 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 55 47.05 -92.25
REMARK 500 ASN A 123 5.21 -69.06
REMARK 500 VAL A 135 99.73 -61.87
REMARK 500 ASN A 212 57.35 -114.01
REMARK 500 LEU A 215 178.45 -57.61
REMARK 500 MET A 216 45.93 39.69
REMARK 500 PHE A 234 70.22 43.10
REMARK 500 ALA A 264 149.51 -173.38
REMARK 500 GLU B 182 -77.40 -126.41
REMARK 500 ASN B 198 -166.81 -110.26
REMARK 500 SER B 202 -73.84 -131.06
REMARK 500 PRO B 327 -63.56 -106.82
REMARK 500 PRO C 55 41.10 -104.11
REMARK 500 LYS C 63 17.84 -145.69
REMARK 500 PHE C 125 -159.18 -113.34
REMARK 500 LEU C 146 -155.54 -103.24
REMARK 500 PRO C 214 2.00 -68.36
REMARK 500 ALA C 264 148.82 -170.96
REMARK 500 GLU D 92 -6.22 -55.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE C 268 ALA C 269 -141.83
REMARK 500 ALA C 269 THR C 270 -136.19
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 ER3 A 304 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 OD2
REMARK 620 2 DT E 3 OP1 64.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 A 302 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 112 O
REMARK 620 2 GLU A 116 OE1 64.4
REMARK 620 3 ASP B 161 OD1 83.0 124.8
REMARK 620 4 ASP B 161 OD2 41.8 78.6 49.4
REMARK 620 5 ACT A 303 OXT 149.1 97.5 127.0 164.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 A 301 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 165 OE1
REMARK 620 2 GLU A 165 OE2 48.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 B 403 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 87 OE1
REMARK 620 2 GLU B 87 OE2 47.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 B 402 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 173 OD1
REMARK 620 2 ASP B 173 OD2 49.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 B 404 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 326 OD1
REMARK 620 2 LEU C 112 O 77.3
REMARK 620 3 GLU C 116 OE1 178.1 103.0
REMARK 620 4 GLU C 116 OE2 132.5 131.4 48.7
REMARK 620 5 ASP D 161 OD1 83.0 93.5 95.1 123.2
REMARK 620 6 ASP D 161 OD2 48.6 57.3 129.9 170.5 48.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 C 302 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 65 OD2
REMARK 620 2 DT G 3 OP1 64.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 C 301 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 165 O
REMARK 620 2 GLU C 169 OE1 127.0
REMARK 620 3 GLU C 169 OE2 86.3 47.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER3 H 101 ER
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT H 8 OP1
REMARK 620 2 DT H 8 OP2 48.8
REMARK 620 3 DT H 8 OP1 0.0 48.8
REMARK 620 4 DT H 8 OP2 48.8 0.0 48.8
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 ER3 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER3 H 101
DBREF 5NJ8 A 23 273 UNP P35869 AHR_HUMAN 23 273
DBREF 5NJ8 B 85 345 UNP P53762 ARNT_MOUSE 85 345
DBREF 5NJ8 C 23 273 UNP P35869 AHR_HUMAN 23 273
DBREF 5NJ8 D 85 345 UNP P53762 ARNT_MOUSE 85 345
DBREF 5NJ8 E 1 12 PDB 5NJ8 5NJ8 1 12
DBREF 5NJ8 F 1 12 PDB 5NJ8 5NJ8 1 12
DBREF 5NJ8 G 1 12 PDB 5NJ8 5NJ8 1 12
DBREF 5NJ8 H 1 12 PDB 5NJ8 5NJ8 1 12
SEQADV 5NJ8 GLY A 20 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 PRO A 21 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 MET A 22 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 GLY B 79 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 PRO B 80 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 GLY B 81 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 SER B 82 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 ASP B 83 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 ALA B 84 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 SER B 256 UNP P53762 CYS 256 ENGINEERED MUTATION
SEQADV 5NJ8 B UNP P53762 VAL 274 DELETION
SEQADV 5NJ8 B UNP P53762 ASP 275 DELETION
SEQADV 5NJ8 B UNP P53762 PRO 276 DELETION
SEQADV 5NJ8 B UNP P53762 VAL 277 DELETION
SEQADV 5NJ8 B UNP P53762 SER 278 DELETION
SEQADV 5NJ8 B UNP P53762 MET 279 DELETION
SEQADV 5NJ8 B UNP P53762 ASN 280 DELETION
SEQADV 5NJ8 B UNP P53762 ARG 281 DELETION
SEQADV 5NJ8 B UNP P53762 LEU 282 DELETION
SEQADV 5NJ8 B UNP P53762 SER 283 DELETION
SEQADV 5NJ8 B UNP P53762 PHE 284 DELETION
SEQADV 5NJ8 B UNP P53762 LEU 285 DELETION
SEQADV 5NJ8 B UNP P53762 ARG 286 DELETION
SEQADV 5NJ8 B UNP P53762 ASN 287 DELETION
SEQADV 5NJ8 B UNP P53762 ARG 288 DELETION
SEQADV 5NJ8 B UNP P53762 CYS 289 DELETION
SEQADV 5NJ8 B UNP P53762 ARG 290 DELETION
SEQADV 5NJ8 B UNP P53762 ASN 291 DELETION
SEQADV 5NJ8 B UNP P53762 GLY 292 DELETION
SEQADV 5NJ8 B UNP P53762 LEU 293 DELETION
SEQADV 5NJ8 B UNP P53762 GLY 294 DELETION
SEQADV 5NJ8 B UNP P53762 SER 295 DELETION
SEQADV 5NJ8 B UNP P53762 VAL 296 DELETION
SEQADV 5NJ8 B UNP P53762 LYS 297 DELETION
SEQADV 5NJ8 B UNP P53762 GLU 298 DELETION
SEQADV 5NJ8 B UNP P53762 GLY 299 DELETION
SEQADV 5NJ8 B UNP P53762 GLU 300 DELETION
SEQADV 5NJ8 B UNP P53762 PRO 301 DELETION
SEQADV 5NJ8 GLY C 20 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 PRO C 21 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 MET C 22 UNP P35869 EXPRESSION TAG
SEQADV 5NJ8 GLY D 79 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 PRO D 80 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 GLY D 81 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 SER D 82 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 ASP D 83 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 ALA D 84 UNP P53762 EXPRESSION TAG
SEQADV 5NJ8 SER D 256 UNP P53762 CYS 256 ENGINEERED MUTATION
SEQADV 5NJ8 D UNP P53762 VAL 274 DELETION
SEQADV 5NJ8 D UNP P53762 ASP 275 DELETION
SEQADV 5NJ8 D UNP P53762 PRO 276 DELETION
SEQADV 5NJ8 D UNP P53762 VAL 277 DELETION
SEQADV 5NJ8 D UNP P53762 SER 278 DELETION
SEQADV 5NJ8 D UNP P53762 MET 279 DELETION
SEQADV 5NJ8 D UNP P53762 ASN 280 DELETION
SEQADV 5NJ8 D UNP P53762 ARG 281 DELETION
SEQADV 5NJ8 D UNP P53762 LEU 282 DELETION
SEQADV 5NJ8 D UNP P53762 SER 283 DELETION
SEQADV 5NJ8 D UNP P53762 PHE 284 DELETION
SEQADV 5NJ8 D UNP P53762 LEU 285 DELETION
SEQADV 5NJ8 D UNP P53762 ARG 286 DELETION
SEQADV 5NJ8 D UNP P53762 ASN 287 DELETION
SEQADV 5NJ8 D UNP P53762 ARG 288 DELETION
SEQADV 5NJ8 D UNP P53762 CYS 289 DELETION
SEQADV 5NJ8 D UNP P53762 ARG 290 DELETION
SEQADV 5NJ8 D UNP P53762 ASN 291 DELETION
SEQADV 5NJ8 D UNP P53762 GLY 292 DELETION
SEQADV 5NJ8 D UNP P53762 LEU 293 DELETION
SEQADV 5NJ8 D UNP P53762 GLY 294 DELETION
SEQADV 5NJ8 D UNP P53762 SER 295 DELETION
SEQADV 5NJ8 D UNP P53762 VAL 296 DELETION
SEQADV 5NJ8 D UNP P53762 LYS 297 DELETION
SEQADV 5NJ8 D UNP P53762 GLU 298 DELETION
SEQADV 5NJ8 D UNP P53762 GLY 299 DELETION
SEQADV 5NJ8 D UNP P53762 GLU 300 DELETION
SEQADV 5NJ8 D UNP P53762 PRO 301 DELETION
SEQRES 1 A 254 GLY PRO MET VAL LYS PRO ILE PRO ALA GLU GLY ILE LYS
SEQRES 2 A 254 SER ASN PRO SER LYS ARG HIS ARG ASP ARG LEU ASN THR
SEQRES 3 A 254 GLU LEU ASP ARG LEU ALA SER LEU LEU PRO PHE PRO GLN
SEQRES 4 A 254 ASP VAL ILE ASN LYS LEU ASP LYS LEU SER VAL LEU ARG
SEQRES 5 A 254 LEU SER VAL SER TYR LEU ARG ALA LYS SER PHE PHE ASP
SEQRES 6 A 254 VAL ALA LEU LYS SER SER PRO THR GLU ARG ASN GLY GLY
SEQRES 7 A 254 GLN ASP ASN CYS ARG ALA ALA ASN PHE ARG GLU GLY LEU
SEQRES 8 A 254 ASN LEU GLN GLU GLY GLU PHE LEU LEU GLN ALA LEU ASN
SEQRES 9 A 254 GLY PHE VAL LEU VAL VAL THR THR ASP ALA LEU VAL PHE
SEQRES 10 A 254 TYR ALA SER SER THR ILE GLN ASP TYR LEU GLY PHE GLN
SEQRES 11 A 254 GLN SER ASP VAL ILE HIS GLN SER VAL TYR GLU LEU ILE
SEQRES 12 A 254 HIS THR GLU ASP ARG ALA GLU PHE GLN ARG GLN LEU HIS
SEQRES 13 A 254 TRP ALA LEU ASN PRO SER GLN CYS THR GLU SER GLY GLN
SEQRES 14 A 254 GLY ILE GLU GLU ALA THR GLY LEU PRO GLN THR VAL VAL
SEQRES 15 A 254 CYS TYR ASN PRO ASP GLN ILE PRO PRO GLU ASN SER PRO
SEQRES 16 A 254 LEU MET GLU ARG CYS PHE ILE CYS ARG LEU ARG CYS LEU
SEQRES 17 A 254 LEU ASP ASN SER SER GLY PHE LEU ALA MET ASN PHE GLN
SEQRES 18 A 254 GLY LYS LEU LYS TYR LEU HIS GLY GLN LYS LYS LYS GLY
SEQRES 19 A 254 LYS ASP GLY SER ILE LEU PRO PRO GLN LEU ALA LEU PHE
SEQRES 20 A 254 ALA ILE ALA THR PRO LEU GLN
SEQRES 1 B 239 GLY PRO GLY SER ASP ALA ASP LYS GLU ARG LEU ALA ARG
SEQRES 2 B 239 GLU ASN HIS SER GLU ILE GLU ARG ARG ARG ARG ASN LYS
SEQRES 3 B 239 MET THR ALA TYR ILE THR GLU LEU SER ASP MET VAL PRO
SEQRES 4 B 239 THR CYS SER ALA LEU ALA ARG LYS PRO ASP LYS LEU THR
SEQRES 5 B 239 ILE LEU ARG MET ALA VAL SER HIS MET LYS SER LEU ARG
SEQRES 6 B 239 GLY THR GLY ASN THR SER THR ASP GLY SER TYR LYS PRO
SEQRES 7 B 239 SER PHE LEU THR ASP GLN GLU LEU LYS HIS LEU ILE LEU
SEQRES 8 B 239 GLU ALA ALA ASP GLY PHE LEU PHE ILE VAL SER CYS GLU
SEQRES 9 B 239 THR GLY ARG VAL VAL TYR VAL SER ASP SER VAL THR PRO
SEQRES 10 B 239 VAL LEU ASN GLN PRO GLN SER GLU TRP PHE GLY SER THR
SEQRES 11 B 239 LEU TYR ASP GLN VAL HIS PRO ASP ASP VAL ASP LYS LEU
SEQRES 12 B 239 ARG GLU GLN LEU SER THR SER GLU ASN ALA LEU THR GLY
SEQRES 13 B 239 ARG VAL LEU ASP LEU LYS THR GLY THR VAL LYS LYS GLU
SEQRES 14 B 239 GLY GLN GLN SER SER MET ARG MET SER MET GLY SER ARG
SEQRES 15 B 239 ARG SER PHE ILE CYS ARG MET ARG CYS GLY THR SER SER
SEQRES 16 B 239 HIS PHE VAL VAL VAL HIS CYS THR GLY TYR ILE LYS ALA
SEQRES 17 B 239 TRP PRO PRO ALA GLY VAL SER LEU PRO ASP ASP ASP PRO
SEQRES 18 B 239 GLU ALA GLY GLN GLY SER LYS PHE CYS LEU VAL ALA ILE
SEQRES 19 B 239 GLY ARG LEU GLN VAL
SEQRES 1 C 254 GLY PRO MET VAL LYS PRO ILE PRO ALA GLU GLY ILE LYS
SEQRES 2 C 254 SER ASN PRO SER LYS ARG HIS ARG ASP ARG LEU ASN THR
SEQRES 3 C 254 GLU LEU ASP ARG LEU ALA SER LEU LEU PRO PHE PRO GLN
SEQRES 4 C 254 ASP VAL ILE ASN LYS LEU ASP LYS LEU SER VAL LEU ARG
SEQRES 5 C 254 LEU SER VAL SER TYR LEU ARG ALA LYS SER PHE PHE ASP
SEQRES 6 C 254 VAL ALA LEU LYS SER SER PRO THR GLU ARG ASN GLY GLY
SEQRES 7 C 254 GLN ASP ASN CYS ARG ALA ALA ASN PHE ARG GLU GLY LEU
SEQRES 8 C 254 ASN LEU GLN GLU GLY GLU PHE LEU LEU GLN ALA LEU ASN
SEQRES 9 C 254 GLY PHE VAL LEU VAL VAL THR THR ASP ALA LEU VAL PHE
SEQRES 10 C 254 TYR ALA SER SER THR ILE GLN ASP TYR LEU GLY PHE GLN
SEQRES 11 C 254 GLN SER ASP VAL ILE HIS GLN SER VAL TYR GLU LEU ILE
SEQRES 12 C 254 HIS THR GLU ASP ARG ALA GLU PHE GLN ARG GLN LEU HIS
SEQRES 13 C 254 TRP ALA LEU ASN PRO SER GLN CYS THR GLU SER GLY GLN
SEQRES 14 C 254 GLY ILE GLU GLU ALA THR GLY LEU PRO GLN THR VAL VAL
SEQRES 15 C 254 CYS TYR ASN PRO ASP GLN ILE PRO PRO GLU ASN SER PRO
SEQRES 16 C 254 LEU MET GLU ARG CYS PHE ILE CYS ARG LEU ARG CYS LEU
SEQRES 17 C 254 LEU ASP ASN SER SER GLY PHE LEU ALA MET ASN PHE GLN
SEQRES 18 C 254 GLY LYS LEU LYS TYR LEU HIS GLY GLN LYS LYS LYS GLY
SEQRES 19 C 254 LYS ASP GLY SER ILE LEU PRO PRO GLN LEU ALA LEU PHE
SEQRES 20 C 254 ALA ILE ALA THR PRO LEU GLN
SEQRES 1 D 239 GLY PRO GLY SER ASP ALA ASP LYS GLU ARG LEU ALA ARG
SEQRES 2 D 239 GLU ASN HIS SER GLU ILE GLU ARG ARG ARG ARG ASN LYS
SEQRES 3 D 239 MET THR ALA TYR ILE THR GLU LEU SER ASP MET VAL PRO
SEQRES 4 D 239 THR CYS SER ALA LEU ALA ARG LYS PRO ASP LYS LEU THR
SEQRES 5 D 239 ILE LEU ARG MET ALA VAL SER HIS MET LYS SER LEU ARG
SEQRES 6 D 239 GLY THR GLY ASN THR SER THR ASP GLY SER TYR LYS PRO
SEQRES 7 D 239 SER PHE LEU THR ASP GLN GLU LEU LYS HIS LEU ILE LEU
SEQRES 8 D 239 GLU ALA ALA ASP GLY PHE LEU PHE ILE VAL SER CYS GLU
SEQRES 9 D 239 THR GLY ARG VAL VAL TYR VAL SER ASP SER VAL THR PRO
SEQRES 10 D 239 VAL LEU ASN GLN PRO GLN SER GLU TRP PHE GLY SER THR
SEQRES 11 D 239 LEU TYR ASP GLN VAL HIS PRO ASP ASP VAL ASP LYS LEU
SEQRES 12 D 239 ARG GLU GLN LEU SER THR SER GLU ASN ALA LEU THR GLY
SEQRES 13 D 239 ARG VAL LEU ASP LEU LYS THR GLY THR VAL LYS LYS GLU
SEQRES 14 D 239 GLY GLN GLN SER SER MET ARG MET SER MET GLY SER ARG
SEQRES 15 D 239 ARG SER PHE ILE CYS ARG MET ARG CYS GLY THR SER SER
SEQRES 16 D 239 HIS PHE VAL VAL VAL HIS CYS THR GLY TYR ILE LYS ALA
SEQRES 17 D 239 TRP PRO PRO ALA GLY VAL SER LEU PRO ASP ASP ASP PRO
SEQRES 18 D 239 GLU ALA GLY GLN GLY SER LYS PHE CYS LEU VAL ALA ILE
SEQRES 19 D 239 GLY ARG LEU GLN VAL
SEQRES 1 E 12 DG DG DT DC DA DC DG DC DA DA DC DC
SEQRES 1 F 12 DG DG DT DT DG DC DG DT DG DA DC DC
SEQRES 1 G 12 DG DG DT DC DA DC DG DC DA DA DC DC
SEQRES 1 H 12 DG DG DT DT DG DC DG DT DG DA DC DC
HET ER3 A 301 1
HET ER3 A 302 1
HET ACT A 303 7
HET ER3 A 304 1
HET ER3 B 401 1
HET ER3 B 402 1
HET ER3 B 403 1
HET ER3 B 404 1
HET ER3 C 301 1
HET ER3 C 302 1
HET ER3 D 401 1
HET ER3 D 402 1
HET ER3 H 101 1
HETNAM ER3 ERBIUM (III) ION
HETNAM ACT ACETATE ION
FORMUL 9 ER3 12(ER 3+)
FORMUL 11 ACT C2 H3 O2 1-
HELIX 1 AA1 ASN A 34 LEU A 53 1 20
HELIX 2 AA2 PRO A 57 ASN A 62 1 6
HELIX 3 AA3 ASP A 65 LEU A 87 1 23
HELIX 4 AA4 LEU A 112 LEU A 122 1 11
HELIX 5 AA5 THR A 141 GLY A 147 1 7
HELIX 6 AA6 GLN A 149 VAL A 153 5 5
HELIX 7 AA7 SER A 157 ILE A 162 5 6
HELIX 8 AA8 HIS A 163 HIS A 175 1 13
HELIX 9 AA9 LYS B 86 SER B 113 1 28
HELIX 10 AB1 ASP B 127 ARG B 143 1 17
HELIX 11 AB2 THR B 160 ALA B 172 1 13
HELIX 12 AB3 ASP B 191 THR B 194 5 4
HELIX 13 AB4 THR B 208 VAL B 213 5 6
HELIX 14 AB5 HIS B 214 ASP B 216 5 3
HELIX 15 AB6 ASP B 217 GLU B 223 1 7
HELIX 16 AB7 ASN C 34 LEU C 53 1 20
HELIX 17 AB8 PRO C 57 ASN C 62 1 6
HELIX 18 AB9 ASP C 65 LYS C 88 1 24
HELIX 19 AC1 GLY C 109 LEU C 122 1 14
HELIX 20 AC2 THR C 141 LEU C 146 1 6
HELIX 21 AC3 GLN C 149 ILE C 154 1 6
HELIX 22 AC4 SER C 157 ILE C 162 5 6
HELIX 23 AC5 HIS C 163 GLN C 173 1 11
HELIX 24 AC6 LYS D 86 VAL D 116 1 31
HELIX 25 AC7 VAL D 116 ALA D 121 1 6
HELIX 26 AC8 ASP D 127 ARG D 143 1 17
HELIX 27 AC9 THR D 160 ASP D 173 1 14
HELIX 28 AD1 SER D 190 THR D 194 5 5
SHEET 1 AA1 5 VAL A 135 ALA A 138 0
SHEET 2 AA1 5 VAL A 126 THR A 130 -1 N VAL A 128 O TYR A 137
SHEET 3 AA1 5 GLN A 262 THR A 270 -1 O ALA A 267 N LEU A 127
SHEET 4 AA1 5 LEU A 235 LEU A 246 -1 N LEU A 246 O GLN A 262
SHEET 5 AA1 5 GLU A 217 LEU A 224 -1 N CYS A 222 O MET A 237
SHEET 1 AA2 5 VAL B 186 VAL B 189 0
SHEET 2 AA2 5 GLY B 174 SER B 180 -1 N ILE B 178 O VAL B 187
SHEET 3 AA2 5 PHE B 335 LEU B 343 -1 O ALA B 339 N PHE B 177
SHEET 4 AA2 5 VAL B 304 ALA B 314 -1 N HIS B 307 O ARG B 342
SHEET 5 AA2 5 ARG B 260 MET B 267 -1 N CYS B 265 O VAL B 306
SHEET 1 AA3 4 VAL C 135 ALA C 138 0
SHEET 2 AA3 4 VAL C 126 THR C 130 -1 N VAL C 128 O PHE C 136
SHEET 3 AA3 4 LEU C 263 ILE C 268 -1 O LEU C 265 N VAL C 129
SHEET 4 AA3 4 GLN C 240 GLY C 241 -1 N GLN C 240 O ILE C 268
SHEET 1 AA4 4 VAL C 135 ALA C 138 0
SHEET 2 AA4 4 VAL C 126 THR C 130 -1 N VAL C 128 O PHE C 136
SHEET 3 AA4 4 LEU C 263 ILE C 268 -1 O LEU C 265 N VAL C 129
SHEET 4 AA4 4 LYS C 244 TYR C 245 -1 N LYS C 244 O ALA C 264
SHEET 1 AA5 2 ILE C 221 CYS C 222 0
SHEET 2 AA5 2 MET C 237 ASN C 238 -1 O MET C 237 N CYS C 222
SHEET 1 AA6 2 CYS D 308 TYR D 311 0
SHEET 2 AA6 2 VAL D 338 GLY D 341 -1 O ILE D 340 N THR D 309
LINK OD2 ASP A 65 ER ER3 A 304 1555 1555 2.76
LINK O LEU A 112 ER ER3 A 302 1555 1555 2.66
LINK OE1 GLU A 116 ER ER3 A 302 1555 1555 3.18
LINK OE1 GLU A 165 ER ER3 A 301 1555 1555 2.70
LINK OE2 GLU A 165 ER ER3 A 301 1555 1555 2.68
LINK OE1 GLU B 87 ER ER3 B 403 1555 1555 2.72
LINK OE2 GLU B 87 ER ER3 B 403 1555 1555 2.72
LINK OD1 ASP B 161 ER ER3 A 302 1555 1555 2.62
LINK OD2 ASP B 161 ER ER3 A 302 1555 1555 2.66
LINK OD1 ASP B 173 ER ER3 B 402 1555 1555 2.64
LINK OD2 ASP B 173 ER ER3 B 402 1555 1555 2.62
LINK OE1 GLU B 203 ER ER3 B 401 1555 1555 2.74
LINK OD1 ASP B 326 ER ER3 B 404 1555 1555 2.78
LINK OD2 ASP C 65 ER ER3 C 302 1555 1555 2.76
LINK O LEU C 112 ER ER3 B 404 1555 1555 2.66
LINK OE1 GLU C 116 ER ER3 B 404 1555 1555 2.61
LINK OE2 GLU C 116 ER ER3 B 404 1555 1555 2.71
LINK O GLU C 165 ER ER3 C 301 1555 1555 3.33
LINK OE1 GLU C 169 ER ER3 C 301 1555 1555 2.70
LINK OE2 GLU C 169 ER ER3 C 301 1555 1555 2.75
LINK OD1 ASP D 161 ER ER3 B 404 1555 1555 2.63
LINK OD2 ASP D 161 ER ER3 B 404 1555 1555 2.74
LINK OP1 DT E 3 ER ER3 A 304 1555 1555 2.74
LINK OP1 DT G 3 ER ER3 C 302 1555 1555 2.69
LINK OP1 DT H 8 ER ER3 H 101 1555 1555 2.63
LINK OP2 DT H 8 ER ER3 H 101 1555 1555 3.40
LINK ER ER3 A 302 OXT ACT A 303 1555 1555 2.76
LINK OP1 DT H 8 ER ER3 H 101 1555 8556 2.63
LINK OP2 DT H 8 ER ER3 H 101 1555 8556 3.40
SITE 1 AC1 1 GLU A 165
SITE 1 AC2 4 LEU A 112 GLU A 116 ACT A 303 ASP B 161
SITE 1 AC3 3 GLU A 116 ER3 A 302 LYS B 155
SITE 1 AC4 2 ASP A 65 DT E 3
SITE 1 AC5 1 GLU B 203
SITE 1 AC6 1 ASP B 173
SITE 1 AC7 1 GLU B 87
SITE 1 AC8 4 ASP B 326 LEU C 112 GLU C 116 ASP D 161
SITE 1 AC9 2 GLU C 165 GLU C 169
SITE 1 AD1 2 ASP C 65 DT G 3
SITE 1 AD2 1 ASP D 173
SITE 1 AD3 1 ASN D 93
SITE 1 AD4 1 DT H 8
CRYST1 91.321 91.321 464.914 90.00 90.00 120.00 P 65 2 2 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 0.010950 0.006322 0.000000 0.00000
SCALE2 0.000000 0.012644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
