HEADER HYDROLASE 06-FEB-13 4J4J
TITLE CRYSTAL STRUCTURE OF THE APOBEC3F VIF BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA DC->DU-EDITING ENZYME APOBEC-3F;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 218-373;
COMPND 5 SYNONYM: APOLIPOPROTEIN B MRNA-EDITING ENZYME CATALYTIC POLYPEPTIDE-
COMPND 6 LIKE 3F;
COMPND 7 EC: 3.5.4.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APOBEC3F;
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: PET46 EK/LIC
KEYWDS ALPHA/BETA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.SIU,A.SULTANA,J.E.LEE
REVDAT 3 28-FEB-24 4J4J 1 REMARK SEQADV LINK
REVDAT 2 20-NOV-13 4J4J 1 JRNL
REVDAT 1 06-NOV-13 4J4J 0
JRNL AUTH K.K.SIU,A.SULTANA,F.C.AZIMI,J.E.LEE
JRNL TITL STRUCTURAL DETERMINANTS OF HIV-1 VIF SUSCEPTIBILITY AND DNA
JRNL TITL 2 BINDING IN APOBEC3F.
JRNL REF NAT COMMUN V. 4 2593 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 24185281
JRNL DOI 10.1038/NCOMMS3593
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 16511
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1661
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 43.4900 - 7.0881 0.97 1338 148 0.1794 0.2008
REMARK 3 2 7.0881 - 5.6299 0.96 1265 141 0.2371 0.2721
REMARK 3 3 5.6299 - 4.9194 0.96 1250 139 0.2240 0.2697
REMARK 3 4 4.9194 - 4.4701 0.95 1209 135 0.2101 0.2587
REMARK 3 5 4.4701 - 4.1500 0.97 1247 139 0.2268 0.3249
REMARK 3 6 4.1500 - 3.9055 0.97 1224 136 0.2706 0.3535
REMARK 3 7 3.9055 - 3.7100 0.98 1239 137 0.2873 0.2968
REMARK 3 8 3.7100 - 3.5486 0.98 1220 137 0.3090 0.3496
REMARK 3 9 3.5486 - 3.4120 0.97 1243 140 0.3658 0.3834
REMARK 3 10 3.4120 - 3.2943 0.97 1217 137 0.3754 0.4704
REMARK 3 11 3.2943 - 3.1913 0.97 1198 138 0.3998 0.4148
REMARK 3 12 3.1913 - 3.1000 0.95 1200 134 0.4188 0.4751
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 99.20
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 : 0.011 3112
REMARK 3 ANGLE : 1.495 4247
REMARK 3 CHIRALITY : 0.084 428
REMARK 3 PLANARITY : 0.008 549
REMARK 3 DIHEDRAL : 18.693 1071
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 -26 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 181.6433 116.5010 58.1979
REMARK 3 T TENSOR
REMARK 3 T11: 0.8117 T22: 0.8051
REMARK 3 T33: 1.3602 T12: 0.0664
REMARK 3 T13: 0.5300 T23: -0.2172
REMARK 3 L TENSOR
REMARK 3 L11: 1.9256 L22: 0.6099
REMARK 3 L33: 2.8217 L12: -0.6276
REMARK 3 L13: -0.8427 L23: 1.2482
REMARK 3 S TENSOR
REMARK 3 S11: -0.4371 S12: -0.2404 S13: -0.7725
REMARK 3 S21: -0.1853 S22: 0.2088 S23: -0.4183
REMARK 3 S31: -0.0750 S32: -0.1311 S33: 0.1672
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 193.6435 117.6142 52.2656
REMARK 3 T TENSOR
REMARK 3 T11: 0.9710 T22: 0.8951
REMARK 3 T33: 1.6090 T12: 0.1696
REMARK 3 T13: 0.3978 T23: -0.1687
REMARK 3 L TENSOR
REMARK 3 L11: 1.4032 L22: 2.0491
REMARK 3 L33: 1.5221 L12: 0.2344
REMARK 3 L13: 1.3154 L23: -0.5457
REMARK 3 S TENSOR
REMARK 3 S11: 0.6365 S12: 0.6307 S13: 0.3126
REMARK 3 S21: -0.6021 S22: 0.2185 S23: -0.4504
REMARK 3 S31: -0.0015 S32: 0.4309 S33: -0.6054
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 198.9463 121.5121 49.8519
REMARK 3 T TENSOR
REMARK 3 T11: 0.8117 T22: 0.8443
REMARK 3 T33: 1.6496 T12: 0.5443
REMARK 3 T13: 1.2390 T23: -0.3582
REMARK 3 L TENSOR
REMARK 3 L11: 5.0826 L22: 3.5117
REMARK 3 L33: 6.0730 L12: -1.1534
REMARK 3 L13: 0.1364 L23: 1.3094
REMARK 3 S TENSOR
REMARK 3 S11: -0.0933 S12: -0.2509 S13: -0.0036
REMARK 3 S21: -0.1283 S22: 0.3142 S23: -0.5638
REMARK 3 S31: -0.0110 S32: 0.2506 S33: -0.0859
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 268 THROUGH 323 )
REMARK 3 ORIGIN FOR THE GROUP (A): 184.6315 124.3320 45.2894
REMARK 3 T TENSOR
REMARK 3 T11: 1.0340 T22: 0.6756
REMARK 3 T33: 1.3623 T12: 0.2630
REMARK 3 T13: 1.0155 T23: -0.7449
REMARK 3 L TENSOR
REMARK 3 L11: 1.3171 L22: 0.4359
REMARK 3 L33: 1.2368 L12: -0.1682
REMARK 3 L13: -0.8461 L23: 0.2371
REMARK 3 S TENSOR
REMARK 3 S11: 0.0745 S12: 0.3387 S13: -0.1678
REMARK 3 S21: -0.5754 S22: -0.0519 S23: -0.4297
REMARK 3 S31: -0.1403 S32: -0.0871 S33: -0.1179
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 324 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): 176.3005 111.3184 51.2306
REMARK 3 T TENSOR
REMARK 3 T11: 0.8918 T22: 0.8564
REMARK 3 T33: 1.7629 T12: -0.0025
REMARK 3 T13: 0.3538 T23: -0.4841
REMARK 3 L TENSOR
REMARK 3 L11: 1.4034 L22: 0.5348
REMARK 3 L33: 1.5953 L12: -0.1222
REMARK 3 L13: 0.6129 L23: 0.1590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0779 S12: 0.1549 S13: -0.7691
REMARK 3 S21: -0.0492 S22: 0.0869 S23: -0.1996
REMARK 3 S31: 0.1230 S32: -0.6759 S33: 0.0301
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -26 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 184.2623 116.0906 78.7740
REMARK 3 T TENSOR
REMARK 3 T11: 0.8251 T22: 0.8060
REMARK 3 T33: 1.5129 T12: 0.1112
REMARK 3 T13: 0.0734 T23: 0.6066
REMARK 3 L TENSOR
REMARK 3 L11: 0.8016 L22: 1.8349
REMARK 3 L33: 3.1535 L12: -0.6031
REMARK 3 L13: 1.2078 L23: 0.1019
REMARK 3 S TENSOR
REMARK 3 S11: -0.1026 S12: -0.2641 S13: -0.8509
REMARK 3 S21: 0.0741 S22: 0.1645 S23: -0.2239
REMARK 3 S31: -0.0507 S32: -0.0823 S33: 0.2680
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 175.8400 113.2044 80.0416
REMARK 3 T TENSOR
REMARK 3 T11: 0.7002 T22: 1.0385
REMARK 3 T33: 1.4731 T12: 0.0354
REMARK 3 T13: 0.3044 T23: 0.4229
REMARK 3 L TENSOR
REMARK 3 L11: 2.7402 L22: 0.7537
REMARK 3 L33: 4.2680 L12: 1.0045
REMARK 3 L13: -0.9246 L23: 0.8535
REMARK 3 S TENSOR
REMARK 3 S11: 0.1775 S12: -0.4893 S13: -0.6446
REMARK 3 S21: 0.1314 S22: 0.2187 S23: 0.0118
REMARK 3 S31: 0.7001 S32: 0.0224 S33: -0.0958
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 250 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 169.3882 109.1987 85.3976
REMARK 3 T TENSOR
REMARK 3 T11: 1.0775 T22: 0.7088
REMARK 3 T33: 1.4501 T12: -0.0307
REMARK 3 T13: 0.4451 T23: 1.2324
REMARK 3 L TENSOR
REMARK 3 L11: 6.4864 L22: 2.6228
REMARK 3 L33: 3.1726 L12: 0.5254
REMARK 3 L13: 0.4318 L23: 1.4407
REMARK 3 S TENSOR
REMARK 3 S11: -0.1077 S12: -0.4562 S13: -0.5541
REMARK 3 S21: 0.2038 S22: 0.0535 S23: 0.3969
REMARK 3 S31: -0.2700 S32: -0.1041 S33: 0.0656
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 268 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 175.9905 117.4696 88.8699
REMARK 3 T TENSOR
REMARK 3 T11: 0.9600 T22: 0.9193
REMARK 3 T33: 1.2780 T12: -0.0001
REMARK 3 T13: 0.5714 T23: 0.8374
REMARK 3 L TENSOR
REMARK 3 L11: 4.0412 L22: 3.6179
REMARK 3 L33: 2.4077 L12: 2.8303
REMARK 3 L13: -2.1922 L23: -1.6902
REMARK 3 S TENSOR
REMARK 3 S11: -0.1547 S12: -0.4791 S13: -0.6089
REMARK 3 S21: 0.7726 S22: -0.0722 S23: -0.0149
REMARK 3 S31: 0.0156 S32: -0.0044 S33: 0.1097
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 293 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 178.8455 124.1587 91.3108
REMARK 3 T TENSOR
REMARK 3 T11: 1.0894 T22: 1.3457
REMARK 3 T33: 1.1097 T12: 0.0292
REMARK 3 T13: 0.2278 T23: 0.8712
REMARK 3 L TENSOR
REMARK 3 L11: 0.7065 L22: 1.7704
REMARK 3 L33: 2.1137 L12: 1.0865
REMARK 3 L13: -0.7266 L23: -0.8942
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: -0.6982 S13: -0.2309
REMARK 3 S21: 0.7916 S22: -0.2923 S23: -0.1873
REMARK 3 S31: 0.1162 S32: -0.4329 S33: -0.0059
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 325 THROUGH 332 )
REMARK 3 ORIGIN FOR THE GROUP (A): 186.0002 118.9381 92.1410
REMARK 3 T TENSOR
REMARK 3 T11: 0.7216 T22: 0.9274
REMARK 3 T33: 1.4614 T12: 0.0026
REMARK 3 T13: -0.2822 T23: 0.4011
REMARK 3 L TENSOR
REMARK 3 L11: 1.6248 L22: 2.2347
REMARK 3 L33: 0.8742 L12: -0.8741
REMARK 3 L13: -0.6709 L23: 1.3876
REMARK 3 S TENSOR
REMARK 3 S11: -0.3820 S12: -0.9412 S13: -1.2147
REMARK 3 S21: 0.1848 S22: -0.2646 S23: -0.1651
REMARK 3 S31: 0.5500 S32: 0.2967 S33: 0.6193
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 333 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): 193.8829 118.1020 83.0232
REMARK 3 T TENSOR
REMARK 3 T11: 0.6783 T22: 1.0005
REMARK 3 T33: 1.9470 T12: 0.2275
REMARK 3 T13: -0.1631 T23: 0.7680
REMARK 3 L TENSOR
REMARK 3 L11: 0.6234 L22: 0.2840
REMARK 3 L33: 0.4419 L12: -0.2310
REMARK 3 L13: 0.5066 L23: -0.2858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0916 S12: 0.1504 S13: -0.6643
REMARK 3 S21: -0.1548 S22: -0.1502 S23: -0.3781
REMARK 3 S31: 0.2149 S32: 0.0927 S33: -0.0152
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 4J4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : ROTORY BEAM SHUTTERS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.9.9.1D
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.9.9.1D
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18499
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.45
REMARK 200 R MERGE FOR SHELL (I) : 0.83800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG 8000, 0.1 M CHES PH 9.0,
REMARK 280 25% (W/V) GLUCOSE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 82.02300
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.65750
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 82.02300
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 67.65750
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 82.02300
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 67.65750
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 82.02300
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 67.65750
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 82.02300
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 67.65750
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 82.02300
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 67.65750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 82.02300
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.65750
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 82.02300
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 82.02300
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.65750
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 -53
REMARK 465 ALA A -52
REMARK 465 HIS A -51
REMARK 465 HIS A -50
REMARK 465 HIS A -49
REMARK 465 HIS A -48
REMARK 465 HIS A -47
REMARK 465 HIS A -46
REMARK 465 VAL A -45
REMARK 465 ASP A -44
REMARK 465 ASP A -43
REMARK 465 ASP A -42
REMARK 465 ASP A -41
REMARK 465 LYS A -40
REMARK 465 MET A -39
REMARK 465 LEU A -38
REMARK 465 VAL A -37
REMARK 465 PRO A -36
REMARK 465 ARG A -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 GLU A -32
REMARK 465 ASN A -31
REMARK 465 LEU A -30
REMARK 465 TYR A -29
REMARK 465 PHE A -28
REMARK 465 MET B -53
REMARK 465 ALA B -52
REMARK 465 HIS B -51
REMARK 465 HIS B -50
REMARK 465 HIS B -49
REMARK 465 HIS B -48
REMARK 465 HIS B -47
REMARK 465 HIS B -46
REMARK 465 VAL B -45
REMARK 465 ASP B -44
REMARK 465 ASP B -43
REMARK 465 ASP B -42
REMARK 465 ASP B -41
REMARK 465 LYS B -40
REMARK 465 MET B -39
REMARK 465 LEU B -38
REMARK 465 VAL B -37
REMARK 465 PRO B -36
REMARK 465 ARG B -35
REMARK 465 GLY B -34
REMARK 465 SER B -33
REMARK 465 GLU B -32
REMARK 465 ASN B -31
REMARK 465 LEU B -30
REMARK 465 TYR B -29
REMARK 465 PHE B -28
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 -7 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 247 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 323 CG CD OE1 NE2
REMARK 470 ASP A 348 CG OD1 OD2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 LYS A 367 CG CD CE NZ
REMARK 470 GLN A 369 CG CD OE1 NE2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 ARG B -7 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 233 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 233 CZ3 CH2
REMARK 470 GLU B 245 CG CD OE1 OE2
REMARK 470 HIS B 247 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 323 CG CD OE1 NE2
REMARK 470 LYS B 355 CG CD CE NZ
REMARK 470 GLU B 373 CG CD OE1 OE2
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 OD1 ASP A -22 HH22 ARG B 239 1.51
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 ASN A -13 117.66 -33.53
REMARK 500 VAL A -8 156.89 -48.05
REMARK 500 ARG A -5 76.51 -100.02
REMARK 500 HIS A 228 -11.05 91.23
REMARK 500 PRO A 244 87.95 -55.89
REMARK 500 HIS A 247 45.58 29.65
REMARK 500 CYS A 248 51.37 -107.12
REMARK 500 ILE A 262 -106.45 -150.49
REMARK 500 LEU A 263 72.81 -3.33
REMARK 500 VAL A 287 -70.25 -79.45
REMARK 500 ALA A 288 -35.56 -39.85
REMARK 500 THR A 312 -38.76 -35.96
REMARK 500 GLU A 324 70.87 -114.64
REMARK 500 TYR A 345 73.16 -65.00
REMARK 500 ASN B -13 114.75 -35.16
REMARK 500 VAL B -8 157.25 -49.50
REMARK 500 ARG B -5 76.82 -101.52
REMARK 500 HIS B 228 -31.47 97.60
REMARK 500 SER B 232 159.63 129.32
REMARK 500 PRO B 244 90.17 -56.13
REMARK 500 THR B 246 123.60 -38.55
REMARK 500 HIS B 247 60.87 -167.68
REMARK 500 ILE B 262 -138.29 -157.83
REMARK 500 LEU B 263 68.01 33.37
REMARK 500 SER B 278 170.57 -59.02
REMARK 500 ALA B 288 -39.19 -35.08
REMARK 500 ASN B 296 11.96 -69.92
REMARK 500 THR B 312 -33.21 -36.08
REMARK 500 MET B 331 107.96 -50.41
REMARK 500 TYR B 345 77.78 -67.20
REMARK 500 ASP B 348 -20.76 76.76
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 PRO A 244 GLU A 245 144.61
REMARK 500 HIS A 247 CYS A 248 143.21
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 HIS A 249 ND1
REMARK 620 2 CYS A 280 SG 108.8
REMARK 620 3 CYS A 283 SG 81.8 87.8
REMARK 620 N 1 2
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 HIS B 249 ND1
REMARK 620 2 CYS B 280 SG 106.6
REMARK 620 3 CYS B 283 SG 87.9 88.4
REMARK 620 N 1 2
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
DBREF 4J4J A 218 373 UNP Q8IUX4 ABC3F_HUMAN 218 373
DBREF 4J4J B 218 373 UNP Q8IUX4 ABC3F_HUMAN 218 373
SEQADV 4J4J MET A -53 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ALA A -52 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -51 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -50 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -49 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -48 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -47 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -46 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL A -45 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP A -44 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP A -43 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP A -42 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP A -41 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LYS A -40 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J MET A -39 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LEU A -38 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL A -37 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO A -36 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG A -35 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY A -34 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J SER A -33 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU A -32 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN A -31 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LEU A -30 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TYR A -29 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE A -28 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLN A -27 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY A -26 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J SER A -25 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ALA A -24 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J MET A -23 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP A -22 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO A -21 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO A -20 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR A -19 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE A -18 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR A -17 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE A -16 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN A -15 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE A -14 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN A -13 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN A -12 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU A -11 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO A -10 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TRP A -9 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL A -8 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG A -7 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY A -6 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG A -5 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS A -4 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU A -3 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR A -2 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TYR A -1 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J MET B -53 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ALA B -52 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -51 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -50 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -49 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -48 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -47 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -46 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL B -45 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP B -44 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP B -43 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP B -42 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP B -41 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LYS B -40 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J MET B -39 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LEU B -38 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL B -37 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO B -36 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG B -35 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY B -34 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J SER B -33 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU B -32 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN B -31 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J LEU B -30 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TYR B -29 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE B -28 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLN B -27 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY B -26 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J SER B -25 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ALA B -24 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J MET B -23 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASP B -22 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO B -21 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO B -20 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR B -19 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE B -18 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR B -17 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE B -16 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN B -15 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PHE B -14 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN B -13 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ASN B -12 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU B -11 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J PRO B -10 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TRP B -9 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J VAL B -8 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG B -7 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLY B -6 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J ARG B -5 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J HIS B -4 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J GLU B -3 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J THR B -2 UNP Q8IUX4 EXPRESSION TAG
SEQADV 4J4J TYR B -1 UNP Q8IUX4 EXPRESSION TAG
SEQRES 1 A 209 MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP
SEQRES 2 A 209 LYS MET LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE
SEQRES 3 A 209 GLN GLY SER ALA MET ASP PRO PRO THR PHE THR PHE ASN
SEQRES 4 A 209 PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR
SEQRES 5 A 209 TYR LEU CYS PHE THR MET GLU VAL VAL LYS HIS HIS SER
SEQRES 6 A 209 PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL
SEQRES 7 A 209 ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU
SEQRES 8 A 209 SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN
SEQRES 9 A 209 TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO
SEQRES 10 A 209 GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS
SEQRES 11 A 209 SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR
SEQRES 12 A 209 TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER
SEQRES 13 A 209 LEU SER GLN GLU GLY ALA SER VAL GLU ILE MET GLY TYR
SEQRES 14 A 209 LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN
SEQRES 15 A 209 ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR
SEQRES 16 A 209 ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU
SEQRES 17 A 209 GLU
SEQRES 1 B 209 MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP
SEQRES 2 B 209 LYS MET LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE
SEQRES 3 B 209 GLN GLY SER ALA MET ASP PRO PRO THR PHE THR PHE ASN
SEQRES 4 B 209 PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR
SEQRES 5 B 209 TYR LEU CYS PHE THR MET GLU VAL VAL LYS HIS HIS SER
SEQRES 6 B 209 PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL
SEQRES 7 B 209 ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU
SEQRES 8 B 209 SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN
SEQRES 9 B 209 TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO
SEQRES 10 B 209 GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS
SEQRES 11 B 209 SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR
SEQRES 12 B 209 TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER
SEQRES 13 B 209 LEU SER GLN GLU GLY ALA SER VAL GLU ILE MET GLY TYR
SEQRES 14 B 209 LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN
SEQRES 15 B 209 ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR
SEQRES 16 B 209 ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU
SEQRES 17 B 209 GLU
HET ZN A 401 1
HET ZN B 401 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 ASP A -22 ASN A -13 1 10
HELIX 2 2 HIS A 249 ILE A 262 1 14
HELIX 3 3 CYS A 280 ARG A 293 1 14
HELIX 4 4 ASP A 311 GLU A 324 1 14
HELIX 5 5 GLY A 332 PHE A 343 1 12
HELIX 6 6 GLY A 356 GLU A 373 1 18
HELIX 7 7 ASP B -22 ASN B -13 1 10
HELIX 8 8 LYS B 226 SER B 229 5 4
HELIX 9 9 HIS B 249 ILE B 262 1 14
HELIX 10 10 CYS B 280 ARG B 293 1 14
HELIX 11 11 ASP B 311 GLN B 323 1 13
HELIX 12 12 GLY B 332 PHE B 343 1 12
HELIX 13 13 GLY B 356 GLU B 373 1 18
SHEET 1 A 5 SER A 229 GLN A 241 0
SHEET 2 A 5 GLU A -3 LYS A 226 -1 N MET A 222 O LYS A 234
SHEET 3 A 5 ASN A 268 THR A 275 -1 O THR A 272 N THR A 221
SHEET 4 A 5 VAL A 297 THR A 303 1 O PHE A 302 N TRP A 273
SHEET 5 A 5 ALA A 326 ILE A 330 1 O SER A 327 N ILE A 301
SHEET 1 B 5 TRP B 233 GLN B 241 0
SHEET 2 B 5 GLU B -3 VAL B 224 -1 N LEU B 218 O PHE B 238
SHEET 3 B 5 TYR B 269 TRP B 277 -1 O GLU B 270 N GLU B 223
SHEET 4 B 5 VAL B 297 ARG B 305 1 O PHE B 302 N TRP B 273
SHEET 5 B 5 ALA B 326 GLU B 329 1 O SER B 327 N ILE B 301
LINK ND1 HIS A 249 ZN ZN A 401 1555 1555 1.93
LINK SG CYS A 280 ZN ZN A 401 1555 1555 2.46
LINK SG CYS A 283 ZN ZN A 401 1555 1555 2.44
LINK ND1 HIS B 249 ZN ZN B 401 1555 1555 2.09
LINK SG CYS B 280 ZN ZN B 401 1555 1555 2.38
LINK SG CYS B 283 ZN ZN B 401 1555 1555 2.30
CISPEP 1 THR B 246 HIS B 247 0 -10.81
SITE 1 AC1 3 HIS A 249 CYS A 280 CYS A 283
SITE 1 AC2 4 HIS B 249 GLU B 251 CYS B 280 CYS B 283
CRYST1 164.046 164.046 135.315 90.00 90.00 90.00 I 4 2 2 32
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 0.006096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007390 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
