HEADER TRANSPORT PROTEIN, MEMBRANE PROTEIN 09-NOV-11 3UKT
TITLE STRUCTURE OF THE C-LINKER/CNBHD OF ZELK CHANNELS IN P1 21 1 SPACE
TITLE 2 GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOVEL PROTEIN SIMILAR TO VERTEBRATE POTASSIUM VOLTAGE-GATED
COMPND 3 CHANNEL, SUBFAMILY H (EAG-RELATED) FAMILY;
COMPND 4 CHAIN: B, A, C, D;
COMPND 5 FRAGMENT: UNP RESIDUES 543-750;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 3 ORGANISM_COMMON: LEOPARD DANIO,ZEBRA DANIO,ZEBRA FISH;
SOURCE 4 ORGANISM_TAXID: 7955;
SOURCE 5 GENE: CH211-11O22.2-001, ELK, KCNH3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMALC2T
KEYWDS KCNH, ELK, ERG, EAG, CNBD, CNBHD, C-LINKER, ION CHANNEL, CYCLIC
KEYWDS 2 NUCLEOTIDE, CYCLIC NUCLEOTIDE-BINDING DOMAIN, ION TRANSPORT,
KEYWDS 3 TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.I.BRELIDZE
REVDAT 6 03-APR-24 3UKT 1 REMARK
REVDAT 5 28-FEB-24 3UKT 1 SEQADV
REVDAT 4 06-JUN-12 3UKT 1 JRNL
REVDAT 3 01-FEB-12 3UKT 1 JRNL
REVDAT 2 25-JAN-12 3UKT 1 JRNL
REVDAT 1 04-JAN-12 3UKT 0
JRNL AUTH T.I.BRELIDZE,A.E.CARLSON,B.SANKARAN,W.N.ZAGOTTA
JRNL TITL STRUCTURE OF THE CARBOXY-TERMINAL REGION OF A KCNH CHANNEL.
JRNL REF NATURE V. 481 530 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22230959
JRNL DOI 10.1038/NATURE10735
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 37513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1875
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 44.1556 - 4.9532 0.99 3860 202 0.1975 0.2548
REMARK 3 2 4.9532 - 3.9322 1.00 3855 204 0.1513 0.2022
REMARK 3 3 3.9322 - 3.4354 1.00 3823 200 0.1935 0.2359
REMARK 3 4 3.4354 - 3.1214 1.00 3846 203 0.2138 0.2604
REMARK 3 5 3.1214 - 2.8977 1.00 3812 200 0.2226 0.2908
REMARK 3 6 2.8977 - 2.7269 1.00 3835 203 0.2442 0.3119
REMARK 3 7 2.7269 - 2.5903 1.00 3791 199 0.2727 0.3405
REMARK 3 8 2.5903 - 2.4776 0.93 3549 187 0.2926 0.3398
REMARK 3 9 2.4776 - 2.3822 0.75 2881 152 0.3065 0.3478
REMARK 3 10 2.3822 - 2.3000 0.63 2386 125 0.3084 0.3494
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 46.08
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.220
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) : 4.84710
REMARK 3 B22 (A**2) : 1.99810
REMARK 3 B33 (A**2) : -6.84520
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.24500
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 : 0.008 5852
REMARK 3 ANGLE : 1.072 7944
REMARK 3 CHIRALITY : 0.067 965
REMARK 3 PLANARITY : 0.004 1003
REMARK 3 DIHEDRAL : 12.579 2069
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 549:640 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3177 14.7168 -3.9964
REMARK 3 T TENSOR
REMARK 3 T11: 0.2042 T22: 0.2212
REMARK 3 T33: 0.1778 T12: 0.0264
REMARK 3 T13: 0.0086 T23: 0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 2.2489 L22: 0.5777
REMARK 3 L33: 0.0012 L12: 0.3721
REMARK 3 L13: -0.1263 L23: 0.1094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.1205 S13: 0.1082
REMARK 3 S21: 0.0612 S22: 0.0261 S23: 0.1532
REMARK 3 S31: -0.1225 S32: 0.0028 S33: -0.0346
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 641:712 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8517 19.1563 -18.4439
REMARK 3 T TENSOR
REMARK 3 T11: 0.2739 T22: 0.3996
REMARK 3 T33: 0.4805 T12: -0.0299
REMARK 3 T13: -0.0646 T23: 0.1305
REMARK 3 L TENSOR
REMARK 3 L11: 1.3277 L22: 1.0684
REMARK 3 L33: 0.9780 L12: 1.0221
REMARK 3 L13: 0.0894 L23: -0.1151
REMARK 3 S TENSOR
REMARK 3 S11: -0.4336 S12: 0.4834 S13: 0.2755
REMARK 3 S21: -0.0909 S22: 0.1648 S23: 0.1749
REMARK 3 S31: 0.0056 S32: 0.1687 S33: 0.2230
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 713:744 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6005 4.8939 -18.4350
REMARK 3 T TENSOR
REMARK 3 T11: 0.3444 T22: 0.3152
REMARK 3 T33: 0.3282 T12: 0.0425
REMARK 3 T13: 0.0138 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 3.0769 L22: 1.6747
REMARK 3 L33: 0.7034 L12: 0.4630
REMARK 3 L13: 0.8662 L23: 0.9698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: 0.5507 S13: -0.2262
REMARK 3 S21: -0.2379 S22: 0.3205 S23: 0.0162
REMARK 3 S31: -0.1421 S32: 0.2414 S33: -0.2183
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 548:640 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9849 9.2550 1.9668
REMARK 3 T TENSOR
REMARK 3 T11: 0.2560 T22: 0.2475
REMARK 3 T33: 0.2646 T12: -0.0119
REMARK 3 T13: 0.0033 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 1.5897 L22: 0.1286
REMARK 3 L33: 0.2705 L12: 0.1633
REMARK 3 L13: -0.2306 L23: 0.0600
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: -0.1952 S13: -0.0371
REMARK 3 S21: 0.0256 S22: 0.0081 S23: 0.0216
REMARK 3 S31: 0.0135 S32: 0.0606 S33: 0.0160
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 641:712 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1678 -4.4879 8.7401
REMARK 3 T TENSOR
REMARK 3 T11: 0.3036 T22: 0.2606
REMARK 3 T33: 0.3195 T12: -0.0543
REMARK 3 T13: -0.0246 T23: 0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 1.4848 L22: 0.8344
REMARK 3 L33: 1.8168 L12: -0.1989
REMARK 3 L13: -0.8832 L23: 0.2048
REMARK 3 S TENSOR
REMARK 3 S11: -0.2119 S12: 0.0158 S13: -0.1419
REMARK 3 S21: 0.0947 S22: 0.1801 S23: 0.1432
REMARK 3 S31: 0.4464 S32: -0.0233 S33: 0.0563
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 713:745 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1437 -6.5198 -5.8526
REMARK 3 T TENSOR
REMARK 3 T11: 0.4979 T22: 0.2743
REMARK 3 T33: 0.3729 T12: -0.0050
REMARK 3 T13: 0.0366 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 2.3569 L22: 1.0823
REMARK 3 L33: 1.6567 L12: 1.3804
REMARK 3 L13: 0.1270 L23: 0.7631
REMARK 3 S TENSOR
REMARK 3 S11: -0.2812 S12: 0.3357 S13: -0.4841
REMARK 3 S21: -0.4494 S22: 0.0735 S23: 0.0019
REMARK 3 S31: 0.7678 S32: 0.0186 S33: 0.2092
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN C AND RESID 549:640 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3738 26.2216 30.4290
REMARK 3 T TENSOR
REMARK 3 T11: 0.2271 T22: 0.3227
REMARK 3 T33: 0.2178 T12: -0.0182
REMARK 3 T13: -0.0350 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 1.1844 L22: 0.5620
REMARK 3 L33: 2.1747 L12: 0.4395
REMARK 3 L13: -0.1914 L23: 0.7720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: -0.1708 S13: -0.1929
REMARK 3 S21: 0.0092 S22: -0.0038 S23: -0.0226
REMARK 3 S31: 0.2470 S32: -0.1400 S33: -0.0394
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN C AND RESID 641:712 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3773 23.2777 21.5071
REMARK 3 T TENSOR
REMARK 3 T11: 0.4072 T22: 0.3200
REMARK 3 T33: 0.2603 T12: -0.0252
REMARK 3 T13: 0.0601 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 2.0031 L22: 1.7137
REMARK 3 L33: 1.8900 L12: 0.5012
REMARK 3 L13: -0.1962 L23: 0.9922
REMARK 3 S TENSOR
REMARK 3 S11: 0.2731 S12: -0.1895 S13: 0.0719
REMARK 3 S21: 0.3647 S22: -0.2867 S23: 0.0307
REMARK 3 S31: -0.0365 S32: -0.3090 S33: -0.0277
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN C AND RESID 713:744 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8558 35.2105 13.7131
REMARK 3 T TENSOR
REMARK 3 T11: 0.3599 T22: 0.1794
REMARK 3 T33: 0.2823 T12: -0.0527
REMARK 3 T13: 0.0054 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.0707 L22: 1.2449
REMARK 3 L33: 1.3277 L12: -0.3805
REMARK 3 L13: -0.6577 L23: -0.6260
REMARK 3 S TENSOR
REMARK 3 S11: -0.1524 S12: 0.1029 S13: 0.3343
REMARK 3 S21: -0.0266 S22: 0.2337 S23: -0.1422
REMARK 3 S31: -0.4533 S32: -0.1060 S33: -0.0746
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN D AND RESID 551:640 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1355 33.1707 41.5922
REMARK 3 T TENSOR
REMARK 3 T11: 0.4617 T22: 0.3742
REMARK 3 T33: 0.4235 T12: -0.0518
REMARK 3 T13: 0.0211 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 0.5687 L22: 0.0983
REMARK 3 L33: 4.0745 L12: -0.0803
REMARK 3 L13: 0.6717 L23: 0.2445
REMARK 3 S TENSOR
REMARK 3 S11: 0.1017 S12: -0.3705 S13: 0.0135
REMARK 3 S21: 0.1047 S22: 0.0774 S23: 0.0721
REMARK 3 S31: 0.0299 S32: 0.1320 S33: -0.1858
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN D AND RESID 641:712 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5424 45.9349 45.4994
REMARK 3 T TENSOR
REMARK 3 T11: 0.7702 T22: 0.5254
REMARK 3 T33: 0.4517 T12: -0.1294
REMARK 3 T13: -0.0978 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 2.0656 L22: 0.2464
REMARK 3 L33: 0.4142 L12: 0.7141
REMARK 3 L13: 0.7463 L23: 0.2663
REMARK 3 S TENSOR
REMARK 3 S11: -0.6511 S12: 0.4762 S13: 0.2422
REMARK 3 S21: -0.4840 S22: 0.3846 S23: 0.0634
REMARK 3 S31: -0.6344 S32: -0.0303 S33: 0.2231
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN D AND RESID 713:742 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9347 50.2432 43.6618
REMARK 3 T TENSOR
REMARK 3 T11: 1.0413 T22: 0.5453
REMARK 3 T33: 0.7770 T12: -0.0035
REMARK 3 T13: -0.2728 T23: 0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 6.0797 L22: 0.3955
REMARK 3 L33: 0.4658 L12: 1.3705
REMARK 3 L13: 0.3488 L23: -0.0859
REMARK 3 S TENSOR
REMARK 3 S11: -0.8627 S12: 0.2308 S13: 1.4748
REMARK 3 S21: -0.3447 S22: 0.5752 S23: 0.5861
REMARK 3 S31: -0.0949 S32: 0.1386 S33: 0.4328
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 3UKT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37558
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 76.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: STRUCTURE OF THE CORRESPONDING SELENOMETHIONINE
REMARK 200 DERIVATIVE CRYSTAL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% (W/V) D-(+)-GALACTOSE, 180 MM
REMARK 280 AMMONIUM SULFATE, 22.5% (W/V) PEG 3350, 90 MM HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 53.90500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 B 539
REMARK 465 ALA B 540
REMARK 465 MET B 541
REMARK 465 ASP B 542
REMARK 465 GLN B 543
REMARK 465 ARG B 544
REMARK 465 MET B 545
REMARK 465 TYR B 546
REMARK 465 SER B 547
REMARK 465 SER B 746
REMARK 465 GLY B 747
REMARK 465 ALA B 748
REMARK 465 ASP B 749
REMARK 465 LEU B 750
REMARK 465 GLY A 539
REMARK 465 ALA A 540
REMARK 465 MET A 541
REMARK 465 ASP A 542
REMARK 465 GLN A 543
REMARK 465 ARG A 544
REMARK 465 MET A 545
REMARK 465 TYR A 546
REMARK 465 SER A 547
REMARK 465 ARG A 548
REMARK 465 GLY A 745
REMARK 465 SER A 746
REMARK 465 GLY A 747
REMARK 465 ALA A 748
REMARK 465 ASP A 749
REMARK 465 LEU A 750
REMARK 465 GLY C 539
REMARK 465 ALA C 540
REMARK 465 MET C 541
REMARK 465 ASP C 542
REMARK 465 GLN C 543
REMARK 465 ARG C 544
REMARK 465 MET C 545
REMARK 465 TYR C 546
REMARK 465 SER C 547
REMARK 465 ARG C 548
REMARK 465 GLY C 745
REMARK 465 SER C 746
REMARK 465 GLY C 747
REMARK 465 ALA C 748
REMARK 465 ASP C 749
REMARK 465 LEU C 750
REMARK 465 GLY D 539
REMARK 465 ALA D 540
REMARK 465 MET D 541
REMARK 465 ASP D 542
REMARK 465 GLN D 543
REMARK 465 ARG D 544
REMARK 465 MET D 545
REMARK 465 TYR D 546
REMARK 465 SER D 547
REMARK 465 ARG D 548
REMARK 465 ARG D 549
REMARK 465 SER D 550
REMARK 465 ARG D 721
REMARK 465 LEU D 722
REMARK 465 TYR D 723
REMARK 465 PRO D 724
REMARK 465 GLU D 725
REMARK 465 TYR D 726
REMARK 465 ALA D 727
REMARK 465 GLN D 728
REMARK 465 LYS D 729
REMARK 465 PHE D 730
REMARK 465 VAL D 731
REMARK 465 SER D 732
REMARK 465 GLU D 733
REMARK 465 ILE D 734
REMARK 465 GLN D 735
REMARK 465 ARG D 743
REMARK 465 GLU D 744
REMARK 465 GLY D 745
REMARK 465 SER D 746
REMARK 465 GLY D 747
REMARK 465 ALA D 748
REMARK 465 ASP D 749
REMARK 465 LEU D 750
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 B 548 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 557 CG CD CE NZ
REMARK 470 ARG B 567 CD NE CZ NH1 NH2
REMARK 470 LYS B 570 CE NZ
REMARK 470 GLN B 574 CG CD OE1 NE2
REMARK 470 LYS B 597 CE NZ
REMARK 470 ARG B 630 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 668 CD1 CD2
REMARK 470 LYS B 669 CG CD CE NZ
REMARK 470 ASN B 671 CG OD1 ND2
REMARK 470 SER B 687 OG
REMARK 470 LYS B 690 CG CD CE NZ
REMARK 470 GLU B 691 CG CD OE1 OE2
REMARK 470 GLN B 692 CG CD OE1 NE2
REMARK 470 VAL B 693 CG1 CG2
REMARK 470 LYS B 695 CD CE NZ
REMARK 470 GLN B 728 CG CD OE1 NE2
REMARK 470 GLN B 735 CG CD OE1 NE2
REMARK 470 HIS B 736 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 737 CG OD1 OD2
REMARK 470 GLU B 744 CG CD OE1 OE2
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 LEU A 595 CD1 CD2
REMARK 470 GLU A 602 CG CD OE1 OE2
REMARK 470 GLU A 614 CG CD OE1 OE2
REMARK 470 ARG A 630 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 666 CG CD OE1 OE2
REMARK 470 LEU A 668 CG CD1 CD2
REMARK 470 ASN A 671 CG OD1 ND2
REMARK 470 LYS A 690 CG CD CE NZ
REMARK 470 GLN A 692 CG CD OE1 NE2
REMARK 470 LYS A 695 CD CE NZ
REMARK 470 GLU A 718 OE1 OE2
REMARK 470 GLU A 725 CG CD OE1 OE2
REMARK 470 GLN A 735 CG CD OE1 NE2
REMARK 470 HIS A 736 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 743 CZ NH1 NH2
REMARK 470 GLU A 744 CG CD OE1 OE2
REMARK 470 ARG C 549 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 557 CG CD CE NZ
REMARK 470 ARG C 564 NE CZ NH1 NH2
REMARK 470 LYS C 570 CD CE NZ
REMARK 470 GLN C 581 CG CD OE1 NE2
REMARK 470 LEU C 595 CG CD1 CD2
REMARK 470 LYS C 597 CD CE NZ
REMARK 470 GLU C 602 CG CD OE1 OE2
REMARK 470 MET C 609 CG SD CE
REMARK 470 ASN C 612 CG OD1 ND2
REMARK 470 GLU C 614 CG CD OE1 OE2
REMARK 470 ARG C 626 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 630 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 671 CG OD1 ND2
REMARK 470 SER C 687 OG
REMARK 470 LYS C 690 CG CD CE NZ
REMARK 470 GLU C 691 OE1 OE2
REMARK 470 LYS C 695 CG CD CE NZ
REMARK 470 TYR C 705 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 714 CE NZ
REMARK 470 GLU C 725 CG CD OE1 OE2
REMARK 470 GLN C 728 CG CD OE1 NE2
REMARK 470 LYS C 729 CG CD CE NZ
REMARK 470 GLN C 735 CG CD OE1 NE2
REMARK 470 ARG C 743 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 557 CE NZ
REMARK 470 LYS D 560 CE NZ
REMARK 470 ARG D 567 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 570 CG CD CE NZ
REMARK 470 LEU D 577 CG CD1 CD2
REMARK 470 GLU D 594 CG CD OE1 OE2
REMARK 470 GLU D 602 CG CD OE1 OE2
REMARK 470 LEU D 611 CG CD1 CD2
REMARK 470 ASN D 612 CG OD1 ND2
REMARK 470 LYS D 613 CG CD CE NZ
REMARK 470 GLU D 614 CG CD OE1 OE2
REMARK 470 LEU D 616 CG CD1 CD2
REMARK 470 GLU D 622 CG CD OE1 OE2
REMARK 470 SER D 623 OG
REMARK 470 ARG D 626 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 630 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 650 CG CD OE1 NE2
REMARK 470 LYS D 669 CG CD CE NZ
REMARK 470 ASP D 670 CG OD1 OD2
REMARK 470 ASN D 671 CG OD1 ND2
REMARK 470 THR D 672 OG1 CG2
REMARK 470 LEU D 674 CG CD1 CD2
REMARK 470 LYS D 679 CG CD CE NZ
REMARK 470 SER D 685 OG
REMARK 470 ASP D 686 CG OD1 OD2
REMARK 470 SER D 687 OG
REMARK 470 LEU D 688 CG CD1 CD2
REMARK 470 LYS D 690 CG CD CE NZ
REMARK 470 GLU D 691 CG CD OE1 OE2
REMARK 470 GLN D 692 CG CD OE1 NE2
REMARK 470 LEU D 713 CG CD1 CD2
REMARK 470 LYS D 714 CG CD CE NZ
REMARK 470 ARG D 717 NH1 NH2
REMARK 470 GLU D 718 CG CD OE1 OE2
REMARK 470 LEU D 720 CG CD1 CD2
REMARK 470 HIS D 736 CG ND1 CD2 CE1 NE2
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 O HOH C 166 O HOH D 162 1.93
REMARK 500 O HOH A 47 O HOH A 56 1.96
REMARK 500 O HOH B 93 O HOH B 105 1.98
REMARK 500 O HOH A 82 O HOH A 83 2.01
REMARK 500 O HOH C 161 O HOH C 177 2.05
REMARK 500 OG1 THR C 739 O HOH C 22 2.06
REMARK 500 O HOH D 192 O HOH D 207 2.06
REMARK 500 O HOH A 33 O HOH A 38 2.07
REMARK 500 O HOH C 185 O HOH C 195 2.07
REMARK 500 O HOH A 131 O HOH A 137 2.10
REMARK 500 O HOH B 100 O HOH B 175 2.10
REMARK 500 O ILE D 590 O HOH D 138 2.14
REMARK 500 O HOH C 17 O HOH C 135 2.14
REMARK 500 O HOH B 63 O HOH A 45 2.15
REMARK 500 O HOH B 170 O HOH A 171 2.17
REMARK 500 O ARG A 567 O HOH A 60 2.18
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 MET A 576 CG - SD - CE ANGL. DEV. = -9.8 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 ASP B 670 -124.92 58.89
REMARK 500 LYS B 679 123.15 -33.43
REMARK 500 SER B 687 66.96 -118.60
REMARK 500 SER B 732 31.67 -88.30
REMARK 500 GLU B 733 -5.61 -152.03
REMARK 500 LEU B 738 109.62 -58.06
REMARK 500 ASP A 670 -104.03 58.77
REMARK 500 SER A 687 -81.28 -78.32
REMARK 500 LEU A 688 -60.91 68.87
REMARK 500 THR A 704 -169.05 -109.71
REMARK 500 SER C 687 68.23 -102.35
REMARK 500 ARG D 567 48.49 35.33
REMARK 500 ALA D 573 -39.46 -39.38
REMARK 500 ASN D 612 67.15 -152.35
REMARK 500 PRO D 619 -32.83 -37.50
REMARK 500 ASN D 671 -2.80 68.66
REMARK 500 VAL D 673 95.44 -69.00
REMARK 500 ALA D 675 170.41 177.31
REMARK 500 LEU D 688 -3.64 -140.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UK5 RELATED DB: PDB
REMARK 900 RELATED ID: 3UKN RELATED DB: PDB
REMARK 900 RELATED ID: 3UKV RELATED DB: PDB
DBREF 3UKT B 543 750 UNP A8WHX9 A8WHX9_DANRE 543 750
DBREF 3UKT A 543 750 UNP A8WHX9 A8WHX9_DANRE 543 750
DBREF 3UKT C 543 750 UNP A8WHX9 A8WHX9_DANRE 543 750
DBREF 3UKT D 543 750 UNP A8WHX9 A8WHX9_DANRE 543 750
SEQADV 3UKT GLY B 539 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ALA B 540 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT MET B 541 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ASP B 542 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT GLY A 539 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ALA A 540 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT MET A 541 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ASP A 542 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT GLY C 539 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ALA C 540 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT MET C 541 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ASP C 542 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT GLY D 539 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ALA D 540 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT MET D 541 UNP A8WHX9 EXPRESSION TAG
SEQADV 3UKT ASP D 542 UNP A8WHX9 EXPRESSION TAG
SEQRES 1 B 212 GLY ALA MET ASP GLN ARG MET TYR SER ARG ARG SER LEU
SEQRES 2 B 212 TYR HIS THR ARG THR LYS ASP LEU LYS ASP PHE ILE ARG
SEQRES 3 B 212 VAL HIS ARG LEU PRO LYS ALA LEU ALA GLN ARG MET LEU
SEQRES 4 B 212 GLU CYS PHE GLN THR THR TRP SER VAL ASN ASN GLY ILE
SEQRES 5 B 212 ASP VAL SER GLU LEU LEU LYS ASP PHE PRO ASP GLU LEU
SEQRES 6 B 212 ARG ALA ASP ILE ALA MET HIS LEU ASN LYS GLU LEU LEU
SEQRES 7 B 212 GLN LEU PRO LEU PHE GLU SER ALA SER ARG GLY CYS LEU
SEQRES 8 B 212 ARG SER LEU SER LEU ILE ILE LYS THR SER PHE CYS ALA
SEQRES 9 B 212 PRO GLY GLU PHE LEU ILE ARG GLN GLY ASP ALA LEU GLN
SEQRES 10 B 212 ALA ILE TYR PHE VAL CYS SER GLY SER MET GLU VAL LEU
SEQRES 11 B 212 LYS ASP ASN THR VAL LEU ALA ILE LEU GLY LYS GLY ASP
SEQRES 12 B 212 LEU ILE GLY SER ASP SER LEU THR LYS GLU GLN VAL ILE
SEQRES 13 B 212 LYS THR ASN ALA ASN VAL LYS ALA LEU THR TYR CYS ASP
SEQRES 14 B 212 LEU GLN TYR ILE SER LEU LYS GLY LEU ARG GLU VAL LEU
SEQRES 15 B 212 ARG LEU TYR PRO GLU TYR ALA GLN LYS PHE VAL SER GLU
SEQRES 16 B 212 ILE GLN HIS ASP LEU THR TYR ASN LEU ARG GLU GLY SER
SEQRES 17 B 212 GLY ALA ASP LEU
SEQRES 1 A 212 GLY ALA MET ASP GLN ARG MET TYR SER ARG ARG SER LEU
SEQRES 2 A 212 TYR HIS THR ARG THR LYS ASP LEU LYS ASP PHE ILE ARG
SEQRES 3 A 212 VAL HIS ARG LEU PRO LYS ALA LEU ALA GLN ARG MET LEU
SEQRES 4 A 212 GLU CYS PHE GLN THR THR TRP SER VAL ASN ASN GLY ILE
SEQRES 5 A 212 ASP VAL SER GLU LEU LEU LYS ASP PHE PRO ASP GLU LEU
SEQRES 6 A 212 ARG ALA ASP ILE ALA MET HIS LEU ASN LYS GLU LEU LEU
SEQRES 7 A 212 GLN LEU PRO LEU PHE GLU SER ALA SER ARG GLY CYS LEU
SEQRES 8 A 212 ARG SER LEU SER LEU ILE ILE LYS THR SER PHE CYS ALA
SEQRES 9 A 212 PRO GLY GLU PHE LEU ILE ARG GLN GLY ASP ALA LEU GLN
SEQRES 10 A 212 ALA ILE TYR PHE VAL CYS SER GLY SER MET GLU VAL LEU
SEQRES 11 A 212 LYS ASP ASN THR VAL LEU ALA ILE LEU GLY LYS GLY ASP
SEQRES 12 A 212 LEU ILE GLY SER ASP SER LEU THR LYS GLU GLN VAL ILE
SEQRES 13 A 212 LYS THR ASN ALA ASN VAL LYS ALA LEU THR TYR CYS ASP
SEQRES 14 A 212 LEU GLN TYR ILE SER LEU LYS GLY LEU ARG GLU VAL LEU
SEQRES 15 A 212 ARG LEU TYR PRO GLU TYR ALA GLN LYS PHE VAL SER GLU
SEQRES 16 A 212 ILE GLN HIS ASP LEU THR TYR ASN LEU ARG GLU GLY SER
SEQRES 17 A 212 GLY ALA ASP LEU
SEQRES 1 C 212 GLY ALA MET ASP GLN ARG MET TYR SER ARG ARG SER LEU
SEQRES 2 C 212 TYR HIS THR ARG THR LYS ASP LEU LYS ASP PHE ILE ARG
SEQRES 3 C 212 VAL HIS ARG LEU PRO LYS ALA LEU ALA GLN ARG MET LEU
SEQRES 4 C 212 GLU CYS PHE GLN THR THR TRP SER VAL ASN ASN GLY ILE
SEQRES 5 C 212 ASP VAL SER GLU LEU LEU LYS ASP PHE PRO ASP GLU LEU
SEQRES 6 C 212 ARG ALA ASP ILE ALA MET HIS LEU ASN LYS GLU LEU LEU
SEQRES 7 C 212 GLN LEU PRO LEU PHE GLU SER ALA SER ARG GLY CYS LEU
SEQRES 8 C 212 ARG SER LEU SER LEU ILE ILE LYS THR SER PHE CYS ALA
SEQRES 9 C 212 PRO GLY GLU PHE LEU ILE ARG GLN GLY ASP ALA LEU GLN
SEQRES 10 C 212 ALA ILE TYR PHE VAL CYS SER GLY SER MET GLU VAL LEU
SEQRES 11 C 212 LYS ASP ASN THR VAL LEU ALA ILE LEU GLY LYS GLY ASP
SEQRES 12 C 212 LEU ILE GLY SER ASP SER LEU THR LYS GLU GLN VAL ILE
SEQRES 13 C 212 LYS THR ASN ALA ASN VAL LYS ALA LEU THR TYR CYS ASP
SEQRES 14 C 212 LEU GLN TYR ILE SER LEU LYS GLY LEU ARG GLU VAL LEU
SEQRES 15 C 212 ARG LEU TYR PRO GLU TYR ALA GLN LYS PHE VAL SER GLU
SEQRES 16 C 212 ILE GLN HIS ASP LEU THR TYR ASN LEU ARG GLU GLY SER
SEQRES 17 C 212 GLY ALA ASP LEU
SEQRES 1 D 212 GLY ALA MET ASP GLN ARG MET TYR SER ARG ARG SER LEU
SEQRES 2 D 212 TYR HIS THR ARG THR LYS ASP LEU LYS ASP PHE ILE ARG
SEQRES 3 D 212 VAL HIS ARG LEU PRO LYS ALA LEU ALA GLN ARG MET LEU
SEQRES 4 D 212 GLU CYS PHE GLN THR THR TRP SER VAL ASN ASN GLY ILE
SEQRES 5 D 212 ASP VAL SER GLU LEU LEU LYS ASP PHE PRO ASP GLU LEU
SEQRES 6 D 212 ARG ALA ASP ILE ALA MET HIS LEU ASN LYS GLU LEU LEU
SEQRES 7 D 212 GLN LEU PRO LEU PHE GLU SER ALA SER ARG GLY CYS LEU
SEQRES 8 D 212 ARG SER LEU SER LEU ILE ILE LYS THR SER PHE CYS ALA
SEQRES 9 D 212 PRO GLY GLU PHE LEU ILE ARG GLN GLY ASP ALA LEU GLN
SEQRES 10 D 212 ALA ILE TYR PHE VAL CYS SER GLY SER MET GLU VAL LEU
SEQRES 11 D 212 LYS ASP ASN THR VAL LEU ALA ILE LEU GLY LYS GLY ASP
SEQRES 12 D 212 LEU ILE GLY SER ASP SER LEU THR LYS GLU GLN VAL ILE
SEQRES 13 D 212 LYS THR ASN ALA ASN VAL LYS ALA LEU THR TYR CYS ASP
SEQRES 14 D 212 LEU GLN TYR ILE SER LEU LYS GLY LEU ARG GLU VAL LEU
SEQRES 15 D 212 ARG LEU TYR PRO GLU TYR ALA GLN LYS PHE VAL SER GLU
SEQRES 16 D 212 ILE GLN HIS ASP LEU THR TYR ASN LEU ARG GLU GLY SER
SEQRES 17 D 212 GLY ALA ASP LEU
FORMUL 5 HOH *212(H2 O)
HELIX 1 1 SER B 550 HIS B 566 1 17
HELIX 2 2 PRO B 569 TRP B 584 1 16
HELIX 3 3 SER B 585 GLY B 589 5 5
HELIX 4 4 PRO B 600 HIS B 610 1 11
HELIX 5 5 LYS B 613 GLU B 622 5 10
HELIX 6 6 SER B 625 LEU B 634 1 10
HELIX 7 7 LEU B 713 TYR B 723 1 11
HELIX 8 8 TYR B 723 LEU B 738 1 16
HELIX 9 9 SER A 550 HIS A 566 1 17
HELIX 10 10 PRO A 569 TRP A 584 1 16
HELIX 11 11 SER A 585 GLY A 589 5 5
HELIX 12 12 PRO A 600 MET A 609 1 10
HELIX 13 13 LYS A 613 GLU A 622 5 10
HELIX 14 14 SER A 625 ILE A 635 1 11
HELIX 15 15 LEU A 713 TYR A 723 1 11
HELIX 16 16 TYR A 723 ASP A 737 1 15
HELIX 17 17 SER C 550 HIS C 566 1 17
HELIX 18 18 PRO C 569 TRP C 584 1 16
HELIX 19 19 VAL C 586 ILE C 590 5 5
HELIX 20 20 PRO C 600 HIS C 610 1 11
HELIX 21 21 LYS C 613 GLU C 622 5 10
HELIX 22 22 SER C 625 ILE C 635 1 11
HELIX 23 23 LEU C 713 TYR C 723 1 11
HELIX 24 24 TYR C 723 LEU C 738 1 16
HELIX 25 25 TYR D 552 HIS D 566 1 15
HELIX 26 26 PRO D 569 TRP D 584 1 16
HELIX 27 27 SER D 585 ILE D 590 5 6
HELIX 28 28 PRO D 600 HIS D 610 1 11
HELIX 29 29 LYS D 613 GLU D 622 5 10
HELIX 30 30 SER D 625 LEU D 634 1 10
HELIX 31 31 LEU D 713 LEU D 720 1 8
SHEET 1 A 5 LYS B 637 CYS B 641 0
SHEET 2 A 5 CYS B 706 SER B 712 -1 O CYS B 706 N CYS B 641
SHEET 3 A 5 ALA B 656 SER B 662 -1 N PHE B 659 O GLN B 709
SHEET 4 A 5 LEU B 682 GLY B 684 -1 O ILE B 683 N TYR B 658
SHEET 5 A 5 TYR B 740 ASN B 741 1 O TYR B 740 N GLY B 684
SHEET 1 B 4 PHE B 646 ILE B 648 0
SHEET 2 B 4 ASN B 699 ALA B 702 -1 O VAL B 700 N LEU B 647
SHEET 3 B 4 MET B 665 LYS B 669 -1 N LEU B 668 O ASN B 699
SHEET 4 B 4 THR B 672 LEU B 677 -1 O LEU B 677 N MET B 665
SHEET 1 C 5 LYS A 637 CYS A 641 0
SHEET 2 C 5 CYS A 706 SER A 712 -1 O TYR A 710 N LYS A 637
SHEET 3 C 5 ALA A 656 SER A 662 -1 N PHE A 659 O GLN A 709
SHEET 4 C 5 LEU A 682 GLY A 684 -1 O ILE A 683 N TYR A 658
SHEET 5 C 5 LEU A 738 ASN A 741 1 O TYR A 740 N GLY A 684
SHEET 1 D 4 PHE A 646 ILE A 648 0
SHEET 2 D 4 ASN A 699 ALA A 702 -1 O VAL A 700 N LEU A 647
SHEET 3 D 4 MET A 665 LYS A 669 -1 N LEU A 668 O ASN A 699
SHEET 4 D 4 THR A 672 LEU A 677 -1 O THR A 672 N LYS A 669
SHEET 1 E 5 LYS C 637 CYS C 641 0
SHEET 2 E 5 CYS C 706 SER C 712 -1 O CYS C 706 N CYS C 641
SHEET 3 E 5 ALA C 656 SER C 662 -1 N PHE C 659 O GLN C 709
SHEET 4 E 5 LEU C 682 GLY C 684 -1 O ILE C 683 N TYR C 658
SHEET 5 E 5 TYR C 740 ASN C 741 1 O TYR C 740 N GLY C 684
SHEET 1 F 4 PHE C 646 ILE C 648 0
SHEET 2 F 4 ASN C 699 ALA C 702 -1 O VAL C 700 N ILE C 648
SHEET 3 F 4 MET C 665 LYS C 669 -1 N LEU C 668 O ASN C 699
SHEET 4 F 4 THR C 672 LEU C 677 -1 O LEU C 677 N MET C 665
SHEET 1 G 5 LYS D 637 CYS D 641 0
SHEET 2 G 5 CYS D 706 SER D 712 -1 O LEU D 708 N SER D 639
SHEET 3 G 5 ALA D 656 SER D 662 -1 N PHE D 659 O GLN D 709
SHEET 4 G 5 LEU D 682 GLY D 684 -1 O ILE D 683 N TYR D 658
SHEET 5 G 5 TYR D 740 ASN D 741 1 O TYR D 740 N LEU D 682
SHEET 1 H 4 PHE D 646 ILE D 648 0
SHEET 2 H 4 ASN D 699 ALA D 702 -1 O VAL D 700 N LEU D 647
SHEET 3 H 4 MET D 665 LYS D 669 -1 N LEU D 668 O ASN D 699
SHEET 4 H 4 THR D 672 LEU D 677 -1 O LEU D 677 N MET D 665
CRYST1 55.660 107.810 77.580 90.00 97.38 90.00 P 1 21 1 8
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 0.017966 0.000000 0.002327 0.00000
SCALE2 0.000000 0.009276 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
