HEADER TRANSFERASE 18-DEC-17 6BXI
TITLE X-RAY CRYSTAL STRUCTURE OF NDR1 KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 38;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NDR1 PROTEIN KINASE,NUCLEAR DBF2-RELATED KINASE 1;
COMPND 5 EC: 2.7.11.1;
COMPND 6 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: STK38, NDR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE FOLD WITH ATYPICALLY LONG ACTIVATION SEGMENT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XIONG,F.SICHERI
REVDAT 2 13-MAR-24 6BXI 1 LINK
REVDAT 1 29-AUG-18 6BXI 0
JRNL AUTH S.XIONG,K.LORENZEN,A.L.COUZENS,C.M.TEMPLETON,D.RAJENDRAN,
JRNL AUTH 2 D.Y.L.MAO,Y.C.JUANG,D.CHIOVITTI,I.KURINOV,S.GUETTLER,
JRNL AUTH 3 A.C.GINGRAS,F.SICHERI
JRNL TITL STRUCTURAL BASIS FOR AUTO-INHIBITION OF THE NDR1 KINASE
JRNL TITL 2 DOMAIN BY AN ATYPICALLY LONG ACTIVATION SEGMENT.
JRNL REF STRUCTURE V. 26 1101 2018
JRNL REFN ISSN 1878-4186
JRNL PMID 29983373
JRNL DOI 10.1016/J.STR.2018.05.014
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1951
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 50219
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2554
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 48.0827 - 5.7621 0.90 2607 136 0.1672 0.1945
REMARK 3 2 5.7621 - 4.5747 0.93 2655 131 0.1573 0.1938
REMARK 3 3 4.5747 - 3.9968 0.93 2678 128 0.1369 0.1787
REMARK 3 4 3.9968 - 3.6315 0.93 2620 155 0.1437 0.1924
REMARK 3 5 3.6315 - 3.3713 0.95 2696 144 0.1592 0.1732
REMARK 3 6 3.3713 - 3.1725 0.96 2749 131 0.1696 0.2242
REMARK 3 7 3.1725 - 3.0137 0.94 2679 129 0.1717 0.2241
REMARK 3 8 3.0137 - 2.8825 0.95 2670 150 0.1741 0.2349
REMARK 3 9 2.8825 - 2.7716 0.95 2698 151 0.1748 0.2376
REMARK 3 10 2.7716 - 2.6759 0.96 2723 159 0.1749 0.2123
REMARK 3 11 2.6759 - 2.5923 0.97 2755 129 0.1883 0.2090
REMARK 3 12 2.5923 - 2.5182 0.95 2647 152 0.1979 0.2423
REMARK 3 13 2.5182 - 2.4519 0.94 2654 150 0.1966 0.2511
REMARK 3 14 2.4519 - 2.3921 0.95 2677 167 0.2009 0.2487
REMARK 3 15 2.3921 - 2.3377 0.94 2669 145 0.2061 0.2337
REMARK 3 16 2.3377 - 2.2879 0.93 2626 145 0.2051 0.2314
REMARK 3 17 2.2879 - 2.2422 0.90 2521 139 0.2150 0.2735
REMARK 3 18 2.2422 - 2.1999 0.82 2341 113 0.2204 0.2656
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.580
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 : 0.008 5571
REMARK 3 ANGLE : 1.184 7540
REMARK 3 CHIRALITY : 0.055 817
REMARK 3 PLANARITY : 0.006 950
REMARK 3 DIHEDRAL : 14.664 2065
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): 174.1327 13.2140 30.4983
REMARK 3 T TENSOR
REMARK 3 T11: 0.2182 T22: 0.3058
REMARK 3 T33: 0.3507 T12: 0.0526
REMARK 3 T13: -0.0576 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 1.9283 L22: 1.1881
REMARK 3 L33: 1.0745 L12: -0.2803
REMARK 3 L13: -0.4282 L23: 0.1930
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: -0.0664 S13: 0.4671
REMARK 3 S21: 0.2427 S22: 0.0082 S23: -0.5319
REMARK 3 S31: -0.1327 S32: 0.2430 S33: 0.0032
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 159.1866 6.5180 27.5323
REMARK 3 T TENSOR
REMARK 3 T11: 0.2441 T22: 0.1693
REMARK 3 T33: 0.1747 T12: 0.0419
REMARK 3 T13: 0.0027 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.0295 L22: 1.1868
REMARK 3 L33: 1.4906 L12: 0.2267
REMARK 3 L13: 0.5811 L23: 0.3499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: -0.0795 S13: -0.0189
REMARK 3 S21: 0.1605 S22: -0.0018 S23: -0.0822
REMARK 3 S31: 0.1851 S32: 0.0554 S33: -0.0086
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 273 )
REMARK 3 ORIGIN FOR THE GROUP (A): 145.7179 19.5724 14.9037
REMARK 3 T TENSOR
REMARK 3 T11: 0.3116 T22: 0.3111
REMARK 3 T33: 0.3049 T12: 0.0139
REMARK 3 T13: -0.0582 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.5840 L22: 1.6463
REMARK 3 L33: 1.3724 L12: -0.2118
REMARK 3 L13: 0.2572 L23: 0.5017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0836 S12: 0.1924 S13: 0.2605
REMARK 3 S21: -0.3840 S22: -0.1593 S23: 0.2572
REMARK 3 S31: -0.3020 S32: -0.3465 S33: 0.1534
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 274 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 142.6352 7.9209 15.9862
REMARK 3 T TENSOR
REMARK 3 T11: 0.1696 T22: 0.2102
REMARK 3 T33: 0.1866 T12: -0.0043
REMARK 3 T13: 0.0035 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 1.0064 L22: 1.6357
REMARK 3 L33: 1.8523 L12: -0.0895
REMARK 3 L13: 0.2348 L23: 0.5206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: -0.0547 S13: 0.0638
REMARK 3 S21: -0.0192 S22: -0.1559 S23: 0.1739
REMARK 3 S31: 0.1093 S32: -0.2804 S33: 0.1197
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): 164.7050 -1.8779 16.9393
REMARK 3 T TENSOR
REMARK 3 T11: 0.3738 T22: 0.2502
REMARK 3 T33: 0.1980 T12: 0.1030
REMARK 3 T13: 0.0319 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.4894 L22: 1.3578
REMARK 3 L33: 1.3312 L12: 0.4083
REMARK 3 L13: 0.4528 L23: 0.0824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.3448 S13: -0.1721
REMARK 3 S21: 0.1052 S22: 0.0989 S23: -0.2259
REMARK 3 S31: 0.2946 S32: 0.1948 S33: -0.1490
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 167.0841 -16.9005 -33.6154
REMARK 3 T TENSOR
REMARK 3 T11: 0.2719 T22: 0.2653
REMARK 3 T33: 0.2886 T12: -0.0449
REMARK 3 T13: 0.0431 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.0251 L22: 1.8976
REMARK 3 L33: 1.6304 L12: 0.7202
REMARK 3 L13: 0.0221 L23: -0.0382
REMARK 3 S TENSOR
REMARK 3 S11: -0.0918 S12: 0.2090 S13: -0.3159
REMARK 3 S21: -0.2458 S22: 0.1749 S23: -0.3161
REMARK 3 S31: 0.1419 S32: 0.1821 S33: -0.0771
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 128 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 155.5648 -7.3689 -27.8354
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.1723
REMARK 3 T33: 0.1854 T12: -0.0403
REMARK 3 T13: -0.0070 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.8760 L22: 1.1391
REMARK 3 L33: 1.2778 L12: -0.2268
REMARK 3 L13: -0.4436 L23: 0.1897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: 0.0837 S13: 0.0091
REMARK 3 S21: -0.1264 S22: 0.0051 S23: -0.0603
REMARK 3 S31: -0.1430 S32: 0.0654 S33: -0.0190
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 256 )
REMARK 3 ORIGIN FOR THE GROUP (A): 141.6870 -23.2467 -23.0011
REMARK 3 T TENSOR
REMARK 3 T11: 0.2731 T22: 0.2782
REMARK 3 T33: 0.3127 T12: -0.0531
REMARK 3 T13: 0.0276 T23: -0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 1.7161 L22: 2.1123
REMARK 3 L33: 1.5124 L12: 0.5347
REMARK 3 L13: -0.5444 L23: -0.3453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: -0.0924 S13: -0.2321
REMARK 3 S21: 0.0608 S22: -0.2765 S23: 0.3687
REMARK 3 S31: 0.2864 S32: -0.2846 S33: 0.2062
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 257 THROUGH 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 148.7480 -20.4336 -9.7493
REMARK 3 T TENSOR
REMARK 3 T11: 0.2861 T22: 0.2135
REMARK 3 T33: 0.2060 T12: -0.0096
REMARK 3 T13: 0.0415 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 1.2867 L22: 2.3042
REMARK 3 L33: 2.5103 L12: -0.8053
REMARK 3 L13: 0.1984 L23: 1.0822
REMARK 3 S TENSOR
REMARK 3 S11: -0.3192 S12: -0.3169 S13: -0.2174
REMARK 3 S21: 0.6465 S22: 0.0410 S23: 0.1498
REMARK 3 S31: 0.1296 S32: -0.0690 S33: 0.2379
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 291 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 139.1598 -8.5524 -15.0149
REMARK 3 T TENSOR
REMARK 3 T11: 0.1791 T22: 0.2344
REMARK 3 T33: 0.1928 T12: 0.0087
REMARK 3 T13: -0.0051 T23: -0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.6731 L22: 1.4974
REMARK 3 L33: 1.3697 L12: -0.0916
REMARK 3 L13: -0.1747 L23: 0.4405
REMARK 3 S TENSOR
REMARK 3 S11: 0.0237 S12: 0.0118 S13: -0.0428
REMARK 3 S21: 0.0322 S22: -0.1739 S23: 0.2703
REMARK 3 S31: -0.1285 S32: -0.2720 S33: 0.1452
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): 162.8407 -0.7374 -19.1071
REMARK 3 T TENSOR
REMARK 3 T11: 0.3612 T22: 0.2576
REMARK 3 T33: 0.2269 T12: -0.0685
REMARK 3 T13: -0.0605 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.4352 L22: 0.9676
REMARK 3 L33: 1.3677 L12: 0.0400
REMARK 3 L13: -0.8715 L23: 0.8013
REMARK 3 S TENSOR
REMARK 3 S11: 0.2512 S12: -0.0507 S13: 0.0769
REMARK 3 S21: -0.3570 S22: 0.0926 S23: -0.1997
REMARK 3 S31: -0.1135 S32: 0.2565 S33: -0.2878
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 6BXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000231755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.071
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 64.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4 M AMMONIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.59550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.98350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.59550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.98350
REMARK 290 SMTRY3 4 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: 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 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 HOH B 776 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 THR B 82
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 THR A 82 OG1 CG2
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 GLN A 277 CG CD OE1 NE2
REMARK 470 GLN A 296 CG CD OE1 NE2
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 PRO A 414 CG CD
REMARK 470 ARG B 83 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 151 CG CD CE NZ
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 ARG B 273 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 277 CG CD OE1 NE2
REMARK 470 PHE B 280 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 296 CG CD OE1 NE2
REMARK 470 GLU B 325 CG CD OE1 OE2
REMARK 470 GLU B 383 CG CD OE1 OE2
REMARK 470 LYS B 402 CG CD CE NZ
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 NH2 ARG A 211 CG1 VAL A 293 1.85
REMARK 500 OE1 GLU B 127 O HOH B 601 2.07
REMARK 500 O HOH A 611 O HOH A 781 2.08
REMARK 500 O VAL B 226 NH1 ARG B 391 2.11
REMARK 500 NZ LYS B 272 O HOH B 602 2.12
REMARK 500 N ASN A 248 O HOH A 601 2.12
REMARK 500 OE1 GLN A 205 O HOH A 602 2.12
REMARK 500 O HOH A 757 O HOH A 807 2.13
REMARK 500 O HOH B 709 O HOH B 777 2.15
REMARK 500 O HOH A 774 O HOH A 811 2.15
REMARK 500 O HOH A 717 O HOH A 803 2.16
REMARK 500 O HOH B 747 O HOH B 790 2.17
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 O HOH A 601 O HOH B 669 4755 2.03
REMARK 500 O HOH A 615 O HOH A 748 2856 2.15
REMARK 500 O HOH A 619 O HOH A 795 2856 2.15
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 TRP A 387 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 TRP B 387 CB - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 GLU B 388 N - CA - CB ANGL. DEV. = 13.5 DEGREES
REMARK 500 GLU B 388 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG B 391 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 391 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO B 414 CA - C - O ANGL. DEV. = -15.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 158 -160.24 -120.54
REMARK 500 ASP A 182 -63.37 72.16
REMARK 500 ASP A 212 41.52 -147.93
REMARK 500 PRO A 254 -165.00 -58.87
REMARK 500 SER A 255 0.53 -151.38
REMARK 500 VAL A 283 -60.62 -99.60
REMARK 500 CYS A 361 59.46 -104.49
REMARK 500 TRP A 387 14.64 86.16
REMARK 500 GLU A 388 -31.28 -130.73
REMARK 500 ASP B 158 -164.81 -129.83
REMARK 500 ASP B 182 -62.76 69.96
REMARK 500 ASP B 212 39.48 -144.74
REMARK 500 VAL B 283 -63.08 -97.07
REMARK 500 CYS B 361 65.72 -104.83
REMARK 500 TRP B 387 15.12 86.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN B 409 0.07 SIDE CHAIN
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 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 217 OD1
REMARK 620 2 ANP A 501 O1G 82.2
REMARK 620 3 ANP A 501 O1B 170.9 88.9
REMARK 620 4 ANP A 501 O1A 91.6 83.0 85.5
REMARK 620 5 HOH A 700 O 83.3 84.3 97.8 166.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 217 OD1
REMARK 620 2 ANP B 501 O3G 86.1
REMARK 620 3 ANP B 501 O2B 172.3 87.7
REMARK 620 4 ANP B 501 O2A 96.4 86.4 87.7
REMARK 620 5 HOH B 620 O 97.2 173.0 88.6 99.3
REMARK 620 6 HOH B 659 O 85.9 83.7 89.0 169.7 90.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502
DBREF 6BXI A 82 414 UNP Q15208 STK38_HUMAN 82 414
DBREF 6BXI B 82 414 UNP Q15208 STK38_HUMAN 82 414
SEQRES 1 A 333 THR ARG LEU GLY LEU GLU ASP PHE GLU SER LEU LYS VAL
SEQRES 2 A 333 ILE GLY ARG GLY ALA PHE GLY GLU VAL ARG LEU VAL GLN
SEQRES 3 A 333 LYS LYS ASP THR GLY HIS VAL TYR ALA MET LYS ILE LEU
SEQRES 4 A 333 ARG LYS ALA ASP MET LEU GLU LYS GLU GLN VAL GLY HIS
SEQRES 5 A 333 ILE ARG ALA GLU ARG ASP ILE LEU VAL GLU ALA ASP SER
SEQRES 6 A 333 LEU TRP VAL VAL LYS MET PHE TYR SER PHE GLN ASP LYS
SEQRES 7 A 333 LEU ASN LEU TYR LEU ILE MET GLU PHE LEU PRO GLY GLY
SEQRES 8 A 333 ASP MET MET THR LEU LEU MET LYS LYS ASP THR LEU THR
SEQRES 9 A 333 GLU GLU GLU THR GLN PHE TYR ILE ALA GLU THR VAL LEU
SEQRES 10 A 333 ALA ILE ASP SER ILE HIS GLN LEU GLY PHE ILE HIS ARG
SEQRES 11 A 333 ASP ILE LYS PRO ASP ASN LEU LEU LEU ASP SER LYS GLY
SEQRES 12 A 333 HIS VAL LYS LEU SER ASP PHE GLY LEU CYS THR GLY LEU
SEQRES 13 A 333 LYS LYS ALA HIS ARG THR GLU PHE TYR ARG ASN LEU ASN
SEQRES 14 A 333 HIS SER LEU PRO SER ASP PHE THR PHE GLN ASN MET ASN
SEQRES 15 A 333 SER LYS ARG LYS ALA GLU THR TRP LYS ARG ASN ARG ARG
SEQRES 16 A 333 GLN LEU ALA PHE SER THR VAL GLY THR PRO ASP TYR ILE
SEQRES 17 A 333 ALA PRO GLU VAL PHE MET GLN THR GLY TYR ASN LYS LEU
SEQRES 18 A 333 CYS ASP TRP TRP SER LEU GLY VAL ILE MET TYR GLU MET
SEQRES 19 A 333 LEU ILE GLY TYR PRO PRO PHE CYS SER GLU THR PRO GLN
SEQRES 20 A 333 GLU THR TYR LYS LYS VAL MET ASN TRP LYS GLU THR LEU
SEQRES 21 A 333 THR PHE PRO PRO GLU VAL PRO ILE SER GLU LYS ALA LYS
SEQRES 22 A 333 ASP LEU ILE LEU ARG PHE CYS CYS GLU TRP GLU HIS ARG
SEQRES 23 A 333 ILE GLY ALA PRO GLY VAL GLU GLU ILE LYS SER ASN SER
SEQRES 24 A 333 PHE PHE GLU GLY VAL ASP TRP GLU HIS ILE ARG GLU ARG
SEQRES 25 A 333 PRO ALA ALA ILE SER ILE GLU ILE LYS SER ILE ASP ASP
SEQRES 26 A 333 THR SER ASN PHE ASP GLU PHE PRO
SEQRES 1 B 333 THR ARG LEU GLY LEU GLU ASP PHE GLU SER LEU LYS VAL
SEQRES 2 B 333 ILE GLY ARG GLY ALA PHE GLY GLU VAL ARG LEU VAL GLN
SEQRES 3 B 333 LYS LYS ASP THR GLY HIS VAL TYR ALA MET LYS ILE LEU
SEQRES 4 B 333 ARG LYS ALA ASP MET LEU GLU LYS GLU GLN VAL GLY HIS
SEQRES 5 B 333 ILE ARG ALA GLU ARG ASP ILE LEU VAL GLU ALA ASP SER
SEQRES 6 B 333 LEU TRP VAL VAL LYS MET PHE TYR SER PHE GLN ASP LYS
SEQRES 7 B 333 LEU ASN LEU TYR LEU ILE MET GLU PHE LEU PRO GLY GLY
SEQRES 8 B 333 ASP MET MET THR LEU LEU MET LYS LYS ASP THR LEU THR
SEQRES 9 B 333 GLU GLU GLU THR GLN PHE TYR ILE ALA GLU THR VAL LEU
SEQRES 10 B 333 ALA ILE ASP SER ILE HIS GLN LEU GLY PHE ILE HIS ARG
SEQRES 11 B 333 ASP ILE LYS PRO ASP ASN LEU LEU LEU ASP SER LYS GLY
SEQRES 12 B 333 HIS VAL LYS LEU SER ASP PHE GLY LEU CYS THR GLY LEU
SEQRES 13 B 333 LYS LYS ALA HIS ARG THR GLU PHE TYR ARG ASN LEU ASN
SEQRES 14 B 333 HIS SER LEU PRO SER ASP PHE THR PHE GLN ASN MET ASN
SEQRES 15 B 333 SER LYS ARG LYS ALA GLU THR TRP LYS ARG ASN ARG ARG
SEQRES 16 B 333 GLN LEU ALA PHE SER THR VAL GLY THR PRO ASP TYR ILE
SEQRES 17 B 333 ALA PRO GLU VAL PHE MET GLN THR GLY TYR ASN LYS LEU
SEQRES 18 B 333 CYS ASP TRP TRP SER LEU GLY VAL ILE MET TYR GLU MET
SEQRES 19 B 333 LEU ILE GLY TYR PRO PRO PHE CYS SER GLU THR PRO GLN
SEQRES 20 B 333 GLU THR TYR LYS LYS VAL MET ASN TRP LYS GLU THR LEU
SEQRES 21 B 333 THR PHE PRO PRO GLU VAL PRO ILE SER GLU LYS ALA LYS
SEQRES 22 B 333 ASP LEU ILE LEU ARG PHE CYS CYS GLU TRP GLU HIS ARG
SEQRES 23 B 333 ILE GLY ALA PRO GLY VAL GLU GLU ILE LYS SER ASN SER
SEQRES 24 B 333 PHE PHE GLU GLY VAL ASP TRP GLU HIS ILE ARG GLU ARG
SEQRES 25 B 333 PRO ALA ALA ILE SER ILE GLU ILE LYS SER ILE ASP ASP
SEQRES 26 B 333 THR SER ASN PHE ASP GLU PHE PRO
HET ANP A 501 31
HET MG A 502 1
HET ANP B 501 31
HET MG B 502 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *441(H2 O)
HELIX 1 AA1 GLY A 85 GLU A 87 5 3
HELIX 2 AA2 ALA A 123 MET A 125 5 3
HELIX 3 AA3 GLU A 127 ASP A 145 1 19
HELIX 4 AA4 MET A 174 ASP A 182 1 9
HELIX 5 AA5 THR A 185 LEU A 206 1 22
HELIX 6 AA6 LYS A 214 ASP A 216 5 3
HELIX 7 AA7 LYS A 238 ARG A 247 5 10
HELIX 8 AA8 ASP A 256 ASN A 261 1 6
HELIX 9 AA9 ASN A 263 ASN A 274 1 12
HELIX 10 AB1 ASN A 274 SER A 281 1 8
HELIX 11 AB2 ALA A 290 MET A 295 5 6
HELIX 12 AB3 LEU A 302 GLY A 318 1 17
HELIX 13 AB4 THR A 326 ASN A 336 1 11
HELIX 14 AB5 ASN A 336 LEU A 341 1 6
HELIX 15 AB6 SER A 350 CYS A 361 1 12
HELIX 16 AB7 GLU A 363 ARG A 367 5 5
HELIX 17 AB8 VAL A 373 SER A 378 1 6
HELIX 18 AB9 ASN A 379 GLU A 383 5 5
HELIX 19 AC1 HIS A 389 ARG A 393 5 5
HELIX 20 AC2 GLY B 85 GLU B 87 5 3
HELIX 21 AC3 ALA B 123 MET B 125 5 3
HELIX 22 AC4 GLU B 127 ASP B 145 1 19
HELIX 23 AC5 MET B 174 ASP B 182 1 9
HELIX 24 AC6 THR B 185 LEU B 206 1 22
HELIX 25 AC7 LYS B 214 ASP B 216 5 3
HELIX 26 AC8 LYS B 238 ARG B 247 5 10
HELIX 27 AC9 ASP B 256 ASN B 261 1 6
HELIX 28 AD1 ASN B 263 ASN B 274 1 12
HELIX 29 AD2 ASN B 274 SER B 281 1 8
HELIX 30 AD3 ALA B 290 MET B 295 5 6
HELIX 31 AD4 LEU B 302 GLY B 318 1 17
HELIX 32 AD5 THR B 326 ASN B 336 1 11
HELIX 33 AD6 ASN B 336 LEU B 341 1 6
HELIX 34 AD7 SER B 350 CYS B 361 1 12
HELIX 35 AD8 GLU B 363 ARG B 367 5 5
HELIX 36 AD9 GLY B 372 SER B 378 1 7
HELIX 37 AE1 ASN B 379 GLU B 383 5 5
HELIX 38 AE2 HIS B 389 ARG B 393 5 5
SHEET 1 AA1 5 PHE A 89 GLY A 98 0
SHEET 2 AA1 5 GLY A 101 LYS A 108 -1 O LEU A 105 N LEU A 92
SHEET 3 AA1 5 VAL A 114 ARG A 121 -1 O TYR A 115 N VAL A 106
SHEET 4 AA1 5 ASN A 161 MET A 166 -1 O LEU A 162 N LEU A 120
SHEET 5 AA1 5 MET A 152 GLN A 157 -1 N TYR A 154 O ILE A 165
SHEET 1 AA2 3 GLY A 172 ASP A 173 0
SHEET 2 AA2 3 LEU A 218 LEU A 220 -1 O LEU A 220 N GLY A 172
SHEET 3 AA2 3 VAL A 226 LEU A 228 -1 O LYS A 227 N LEU A 219
SHEET 1 AA3 5 PHE B 89 ARG B 97 0
SHEET 2 AA3 5 GLY B 101 LYS B 108 -1 O VAL B 103 N GLY B 96
SHEET 3 AA3 5 VAL B 114 ARG B 121 -1 O MET B 117 N ARG B 104
SHEET 4 AA3 5 ASN B 161 MET B 166 -1 O MET B 166 N ALA B 116
SHEET 5 AA3 5 MET B 152 GLN B 157 -1 N TYR B 154 O ILE B 165
SHEET 1 AA4 3 GLY B 172 ASP B 173 0
SHEET 2 AA4 3 LEU B 218 LEU B 220 -1 O LEU B 220 N GLY B 172
SHEET 3 AA4 3 VAL B 226 LEU B 228 -1 O LYS B 227 N LEU B 219
LINK OD1 ASN A 217 MG MG A 502 1555 1555 2.31
LINK O1G ANP A 501 MG MG A 502 1555 1555 2.17
LINK O1B ANP A 501 MG MG A 502 1555 1555 2.06
LINK O1A ANP A 501 MG MG A 502 1555 1555 1.92
LINK MG MG A 502 O HOH A 700 1555 1555 2.41
LINK OD1 ASN B 217 MG MG B 502 1555 1555 2.19
LINK O3G ANP B 501 MG MG B 502 1555 1555 2.13
LINK O2B ANP B 501 MG MG B 502 1555 1555 2.09
LINK O2A ANP B 501 MG MG B 502 1555 1555 1.82
LINK MG MG B 502 O HOH B 620 1555 1555 2.22
LINK MG MG B 502 O HOH B 659 1555 1555 2.31
SITE 1 AC1 28 GLY A 96 GLY A 98 VAL A 103 ALA A 116
SITE 2 AC1 28 LYS A 118 VAL A 150 MET A 166 GLU A 167
SITE 3 AC1 28 LEU A 169 ASP A 173 ASP A 216 ASN A 217
SITE 4 AC1 28 LEU A 219 SER A 229 ASP A 230 CYS A 234
SITE 5 AC1 28 PHE A 410 MG A 502 HOH A 608 HOH A 612
SITE 6 AC1 28 HOH A 626 HOH A 651 HOH A 681 HOH A 689
SITE 7 AC1 28 HOH A 696 HOH A 700 HOH A 705 HOH A 742
SITE 1 AC2 3 ASN A 217 ANP A 501 HOH A 700
SITE 1 AC3 31 ILE B 95 GLY B 96 GLY B 98 VAL B 103
SITE 2 AC3 31 ALA B 116 LYS B 118 VAL B 150 MET B 166
SITE 3 AC3 31 GLU B 167 LEU B 169 ASP B 173 ASP B 216
SITE 4 AC3 31 ASN B 217 LEU B 219 SER B 229 ASP B 230
SITE 5 AC3 31 CYS B 234 PHE B 410 MG B 502 HOH B 615
SITE 6 AC3 31 HOH B 619 HOH B 620 HOH B 625 HOH B 628
SITE 7 AC3 31 HOH B 647 HOH B 655 HOH B 659 HOH B 663
SITE 8 AC3 31 HOH B 679 HOH B 708 HOH B 711
SITE 1 AC4 4 ASN B 217 ANP B 501 HOH B 620 HOH B 659
CRYST1 117.191 117.967 95.044 90.00 124.88 90.00 C 1 2 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 0.008533 0.000000 0.005947 0.00000
SCALE2 0.000000 0.008477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012825 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
