HEADER SIGNALING PROTEIN 31-MAY-17 5W0P
TITLE CRYSTAL STRUCTURE OF RHODOPSIN BOUND TO VISUAL ARRESTIN DETERMINED BY
TITLE 2 X-RAY FREE ELECTRON LASER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOLYSIN,RHODOPSIN,S-ARRESTIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE,OPSIN-2,48 KDA PROTEIN,
COMPND 5 RETINAL S-ANTIGEN,S-AG,ROD PHOTORECEPTOR ARRESTIN;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ENDOLYSIN,RHODOPSIN,S-ARRESTIN;
COMPND 10 CHAIN: C, D;
COMPND 11 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE,OPSIN-2,48 KDA PROTEIN,
COMPND 12 RETINAL S-ANTIGEN,S-AG,ROD PHOTORECEPTOR ARRESTIN;
COMPND 13 EC: 3.2.1.17;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB55, HOMO SAPIENS, MUS
SOURCE 3 MUSCULUS;
SOURCE 4 ORGANISM_COMMON: HUMAN, MOUSE;
SOURCE 5 ORGANISM_TAXID: 697289, 9606, 10090;
SOURCE 6 GENE: E, RB55_P125, RHO, OPN2, SAG;
SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB55, HOMO SAPIENS, MUS
SOURCE 11 MUSCULUS;
SOURCE 12 ORGANISM_COMMON: HUMAN, MOUSE;
SOURCE 13 ORGANISM_TAXID: 697289, 9606, 10090;
SOURCE 14 GENE: E, RB55_P125, RHO, OPN2, SAG;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS RHODOPSIN, GPCR, ARRESTIN, GRK, PHOSPHORYLATION CODES, MEMBRANE
KEYWDS 2 PROTEINS, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,Y.HE,P.W.DE WAAL,X.GAO,Y.KANG,N.VAN EPS,Y.YIN,K.PAL,
AUTHOR 2 D.GOSWAMI,T.A.WHITE,A.BARTY,N.R.LATORRACA,H.N.CHAPMAN,W.L.HUBBELL,
AUTHOR 3 R.O.DROR,R.C.STEVENS,V.CHEREZOV,V.V.GUREVICH,P.R.GRIFFIN,O.P.ERNST,
AUTHOR 4 K.MELCHER,H.E.XU
REVDAT 6 04-OCT-23 5W0P 1 HETSYN
REVDAT 5 29-JUL-20 5W0P 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 11-DEC-19 5W0P 1 REMARK
REVDAT 3 21-NOV-18 5W0P 1 REMARK
REVDAT 2 27-SEP-17 5W0P 1 REMARK
REVDAT 1 09-AUG-17 5W0P 0
JRNL AUTH X.E.ZHOU,Y.HE,P.W.DE WAAL,X.GAO,Y.KANG,N.VAN EPS,Y.YIN,
JRNL AUTH 2 K.PAL,D.GOSWAMI,T.A.WHITE,A.BARTY,N.R.LATORRACA,H.N.CHAPMAN,
JRNL AUTH 3 W.L.HUBBELL,R.O.DROR,R.C.STEVENS,V.CHEREZOV,V.V.GUREVICH,
JRNL AUTH 4 P.R.GRIFFIN,O.P.ERNST,K.MELCHER,H.E.XU
JRNL TITL IDENTIFICATION OF PHOSPHORYLATION CODES FOR ARRESTIN
JRNL TITL 2 RECRUITMENT BY G PROTEIN-COUPLED RECEPTORS.
JRNL REF CELL V. 170 457 2017
JRNL REFN ISSN 1097-4172
JRNL PMID 28753425
JRNL DOI 10.1016/J.CELL.2017.07.002
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.7
REMARK 3 NUMBER OF REFLECTIONS : 76360
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 3761
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 30.0313 - 8.1602 0.95 5431 259 0.1766 0.2274
REMARK 3 2 8.1602 - 6.4985 0.94 5169 302 0.1988 0.2214
REMARK 3 3 6.4985 - 5.6834 0.95 5156 253 0.2398 0.2924
REMARK 3 4 5.6834 - 5.1666 0.95 5129 256 0.2372 0.3089
REMARK 3 5 5.1666 - 4.7979 0.95 5087 255 0.2153 0.2407
REMARK 3 6 4.7979 - 4.5160 0.95 5069 284 0.2242 0.2609
REMARK 3 7 4.5160 - 4.2905 0.95 5046 286 0.2541 0.2766
REMARK 3 8 4.2905 - 4.1042 0.95 5079 271 0.2634 0.2780
REMARK 3 9 4.1042 - 3.9466 0.95 5029 248 0.2934 0.3297
REMARK 3 10 3.9466 - 3.8107 0.95 5054 274 0.3094 0.3286
REMARK 3 11 3.8107 - 3.6917 0.95 5041 233 0.3342 0.3710
REMARK 3 12 3.6917 - 3.5864 0.93 4917 254 0.3704 0.4180
REMARK 3 13 3.5864 - 3.4921 0.64 3368 172 0.3679 0.3928
REMARK 3 14 3.4921 - 3.4070 0.46 2435 129 0.3794 0.3633
REMARK 3 15 3.4070 - 3.3297 0.35 1828 95 0.3674 0.3888
REMARK 3 16 3.3297 - 3.2589 0.26 1369 66 0.3786 0.4023
REMARK 3 17 3.2589 - 3.1938 0.19 992 65 0.3540 0.4258
REMARK 3 18 3.1938 - 3.1336 0.14 715 29 0.3492 0.2956
REMARK 3 19 3.1336 - 3.0777 0.09 459 21 0.3376 0.3521
REMARK 3 20 3.0777 - 3.0256 0.04 213 9 0.3534 0.2968
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 26612
REMARK 3 ANGLE : 0.845 36174
REMARK 3 CHIRALITY : 0.039 4154
REMARK 3 PLANARITY : 0.007 4544
REMARK 3 DIHEDRAL : 10.826 9700
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ -159:33 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0894 14.6447 187.6674
REMARK 3 T TENSOR
REMARK 3 T11: 2.7681 T22: 1.7211
REMARK 3 T33: 1.7467 T12: -0.6950
REMARK 3 T13: 0.0808 T23: -0.1495
REMARK 3 L TENSOR
REMARK 3 L11: 0.0691 L22: 0.0121
REMARK 3 L33: 0.0682 L12: 0.2004
REMARK 3 L13: 0.0807 L23: -0.0092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: -0.2864 S13: -0.1318
REMARK 3 S21: 0.2406 S22: -0.3905 S23: -0.0134
REMARK 3 S31: 0.1130 S32: -0.5020 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 34:277 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.1411 21.8835 227.1311
REMARK 3 T TENSOR
REMARK 3 T11: 1.5109 T22: 1.1283
REMARK 3 T33: 1.1107 T12: 0.4263
REMARK 3 T13: 0.0007 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 0.0713 L22: 0.0923
REMARK 3 L33: -0.0121 L12: 0.0984
REMARK 3 L13: 0.0458 L23: -0.0429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.5672 S13: -0.0760
REMARK 3 S21: -0.1465 S22: -0.0133 S23: -0.0150
REMARK 3 S31: -0.1690 S32: -0.1227 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 278:2362 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0772 32.5115 262.3119
REMARK 3 T TENSOR
REMARK 3 T11: 1.3358 T22: 1.2894
REMARK 3 T33: 1.3010 T12: 0.1916
REMARK 3 T13: -0.0688 T23: -0.0942
REMARK 3 L TENSOR
REMARK 3 L11: -0.5604 L22: -0.1759
REMARK 3 L33: 0.1678 L12: 0.2166
REMARK 3 L13: 0.1279 L23: 0.0068
REMARK 3 S TENSOR
REMARK 3 S11: -0.3519 S12: 0.1919 S13: 0.1340
REMARK 3 S21: -0.3379 S22: 0.2072 S23: 0.0699
REMARK 3 S31: -0.1565 S32: -0.1549 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESSEQ -159:14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5649 -14.5801 267.3997
REMARK 3 T TENSOR
REMARK 3 T11: 0.9142 T22: 1.5771
REMARK 3 T33: 1.7484 T12: 0.6712
REMARK 3 T13: 0.0295 T23: -0.3044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0787 L22: -0.1614
REMARK 3 L33: 0.0318 L12: -0.0880
REMARK 3 L13: -0.0006 L23: 0.0148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.0367 S13: 0.3811
REMARK 3 S21: 0.5292 S22: -0.3426 S23: -0.3667
REMARK 3 S31: 0.1952 S32: -0.1691 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESSEQ 15:277
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7386 -18.0170 226.8803
REMARK 3 T TENSOR
REMARK 3 T11: 1.8388 T22: 0.7859
REMARK 3 T33: 1.0011 T12: -0.1457
REMARK 3 T13: 0.0617 T23: 0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 0.1203 L22: 0.2575
REMARK 3 L33: 0.1012 L12: -0.1232
REMARK 3 L13: 0.2299 L23: 0.0297
REMARK 3 S TENSOR
REMARK 3 S11: 0.1220 S12: 0.3664 S13: -0.0061
REMARK 3 S21: 0.2271 S22: 0.2050 S23: -0.1667
REMARK 3 S31: -0.5291 S32: -0.3364 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESSEQ 278:2189
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0302 -14.4524 189.3309
REMARK 3 T TENSOR
REMARK 3 T11: 1.3510 T22: 1.3170
REMARK 3 T33: 1.0989 T12: 0.0707
REMARK 3 T13: 0.0363 T23: -0.0678
REMARK 3 L TENSOR
REMARK 3 L11: -0.1899 L22: 0.0324
REMARK 3 L33: 0.0416 L12: -0.3694
REMARK 3 L13: -0.0417 L23: -0.0453
REMARK 3 S TENSOR
REMARK 3 S11: -0.6371 S12: 0.1113 S13: -0.0151
REMARK 3 S21: 0.3026 S22: 0.5137 S23: -0.0128
REMARK 3 S31: 0.3079 S32: -0.0721 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND RESSEQ 2190:2361
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6341 -50.3089 189.2298
REMARK 3 T TENSOR
REMARK 3 T11: 1.7433 T22: 1.4834
REMARK 3 T33: 1.1811 T12: -0.3915
REMARK 3 T13: 0.2710 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 0.0631 L22: 0.1097
REMARK 3 L33: 0.0962 L12: 0.3120
REMARK 3 L13: -0.0657 L23: -0.0668
REMARK 3 S TENSOR
REMARK 3 S11: -0.4993 S12: -0.1718 S13: 0.0940
REMARK 3 S21: 0.1987 S22: 0.2757 S23: 0.5664
REMARK 3 S31: 0.5304 S32: 0.1266 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND RESSEQ -159:33
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8704 -45.1105 74.5022
REMARK 3 T TENSOR
REMARK 3 T11: 2.0384 T22: 2.1160
REMARK 3 T33: 1.5306 T12: 0.6571
REMARK 3 T13: -0.4805 T23: -0.1820
REMARK 3 L TENSOR
REMARK 3 L11: 0.0196 L22: 0.1137
REMARK 3 L33: 0.1022 L12: -0.2740
REMARK 3 L13: 0.0812 L23: 0.0766
REMARK 3 S TENSOR
REMARK 3 S11: -0.3164 S12: -0.2903 S13: 0.7403
REMARK 3 S21: 0.2159 S22: -0.1600 S23: -0.0634
REMARK 3 S31: 0.8073 S32: -0.2416 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND RESSEQ 34:277
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7698 -63.2714 114.2260
REMARK 3 T TENSOR
REMARK 3 T11: 1.0122 T22: 1.4134
REMARK 3 T33: 1.1819 T12: 0.0788
REMARK 3 T13: 0.1934 T23: 0.1447
REMARK 3 L TENSOR
REMARK 3 L11: 0.1362 L22: 0.0630
REMARK 3 L33: 0.0956 L12: -0.0249
REMARK 3 L13: 0.1231 L23: -0.0196
REMARK 3 S TENSOR
REMARK 3 S11: -0.1371 S12: 0.2119 S13: 0.4822
REMARK 3 S21: 0.3553 S22: 0.3250 S23: 0.0000
REMARK 3 S31: 0.1184 S32: -0.0449 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN C AND RESSEQ 278:2361
REMARK 3 ORIGIN FOR THE GROUP (A): -56.3460 -57.2722 149.5034
REMARK 3 T TENSOR
REMARK 3 T11: 0.8930 T22: 1.3638
REMARK 3 T33: 1.1961 T12: 0.0507
REMARK 3 T13: 0.0499 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: -0.1497 L22: -0.2533
REMARK 3 L33: -0.0602 L12: -0.3184
REMARK 3 L13: -0.0758 L23: 0.3211
REMARK 3 S TENSOR
REMARK 3 S11: 0.2310 S12: 0.0109 S13: 0.1010
REMARK 3 S21: 0.2154 S22: -0.0311 S23: -0.0337
REMARK 3 S31: -0.3114 S32: 0.0471 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN D AND RESSEQ -85:14
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7618 -43.5689 157.8005
REMARK 3 T TENSOR
REMARK 3 T11: 1.8855 T22: 2.6690
REMARK 3 T33: 1.7897 T12: -0.1190
REMARK 3 T13: 0.9875 T23: -0.6190
REMARK 3 L TENSOR
REMARK 3 L11: -0.1819 L22: 0.0305
REMARK 3 L33: 0.0150 L12: -0.0089
REMARK 3 L13: 0.0099 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1741 S12: -0.0610 S13: 0.5274
REMARK 3 S21: -0.1445 S22: 0.1073 S23: -0.0412
REMARK 3 S31: 0.0647 S32: -0.1297 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN D AND RESSEQ 15:277
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8363 -60.7774 113.9737
REMARK 3 T TENSOR
REMARK 3 T11: -2.0572 T22: -0.3641
REMARK 3 T33: 0.8840 T12: 2.3221
REMARK 3 T13: 0.3663 T23: -0.4836
REMARK 3 L TENSOR
REMARK 3 L11: 0.1406 L22: 0.1418
REMARK 3 L33: 0.0110 L12: -0.0770
REMARK 3 L13: -0.0696 L23: 0.1321
REMARK 3 S TENSOR
REMARK 3 S11: 0.9074 S12: -1.0534 S13: -0.1418
REMARK 3 S21: -0.0682 S22: -0.3112 S23: -0.1233
REMARK 3 S31: 0.2566 S32: -0.9667 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN D AND RESSEQ 278:2361
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3696 -55.1705 76.5168
REMARK 3 T TENSOR
REMARK 3 T11: 1.3440 T22: 0.9573
REMARK 3 T33: 0.8322 T12: 0.2674
REMARK 3 T13: 0.0789 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: -0.0143 L22: -0.1322
REMARK 3 L33: 0.4029 L12: 0.1186
REMARK 3 L13: -0.0405 L23: -0.3284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: -0.2067 S13: 0.1670
REMARK 3 S21: -0.1738 S22: -0.1088 S23: 0.0341
REMARK 3 S31: 0.1213 S32: 0.6587 S33: -0.0000
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 5W0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : CXI
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.33
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76360
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 72.4
REMARK 200 DATA REDUNDANCY : 287.0
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.5000
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) : 3.10
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4ZWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, MAGNESIUM ACETATE, SODIUM
REMARK 280 ACETATE., PH 5, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 54.62000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 226.32000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.62000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 226.32000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.62000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.62000
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, 3, 4
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 APPLY THE FOLLOWING TO CHAINS: A, E
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 APPLY THE FOLLOWING TO CHAINS: B, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 LYS A 325
REMARK 465 ASN A 326
REMARK 465 PRO A 327
REMARK 465 LEU A 328
REMARK 465 GLY A 329
REMARK 465 GLN A 1990
REMARK 465 VAL A 1991
REMARK 465 ALA A 1992
REMARK 465 PRO A 1993
REMARK 465 ALA A 1994
REMARK 465 GLY A 1995
REMARK 465 SER A 1996
REMARK 465 ALA A 1997
REMARK 465 GLY A 1998
REMARK 465 SER A 1999
REMARK 465 ALA A 2000
REMARK 465 GLY A 2001
REMARK 465 SER A 2002
REMARK 465 ALA A 2003
REMARK 465 GLY A 2004
REMARK 465 SER A 2005
REMARK 465 ALA A 2006
REMARK 465 GLY A 2007
REMARK 465 SER A 2008
REMARK 465 ALA A 2009
REMARK 465 SER A 2010
REMARK 465 HIS A 2011
REMARK 465 ASP A 2363
REMARK 465 PRO A 2364
REMARK 465 ALA A 2365
REMARK 465 LYS A 2366
REMARK 465 GLU A 2367
REMARK 465 SER A 2368
REMARK 465 VAL A 2369
REMARK 465 GLN A 2370
REMARK 465 ASP A 2371
REMARK 465 GLU A 2372
REMARK 465 ASN A 2373
REMARK 465 ALA A 2374
REMARK 465 ALA A 2375
REMARK 465 ALA A 2376
REMARK 465 GLU A 2377
REMARK 465 GLU A 2378
REMARK 465 PHE A 2379
REMARK 465 ALA A 2380
REMARK 465 ARG A 2381
REMARK 465 GLN A 2382
REMARK 465 ASN A 2383
REMARK 465 LEU A 2384
REMARK 465 LYS A 2385
REMARK 465 ASP A 2386
REMARK 465 THR A 2387
REMARK 465 GLY A 2388
REMARK 465 GLU A 2389
REMARK 465 ASN A 2390
REMARK 465 THR A 2391
REMARK 465 GLU A 2392
REMARK 465 LEU B -148
REMARK 465 ARG B -147
REMARK 465 LEU B -146
REMARK 465 LYS B -145
REMARK 465 ILE B -144
REMARK 465 TYR B -143
REMARK 465 LYS B -142
REMARK 465 ASP B -141
REMARK 465 THR B -140
REMARK 465 GLU B -139
REMARK 465 GLY B -138
REMARK 465 TYR B -137
REMARK 465 TYR B -136
REMARK 465 THR B -135
REMARK 465 ILE B -134
REMARK 465 GLY B -133
REMARK 465 ILE B -132
REMARK 465 GLY B -131
REMARK 465 HIS B -130
REMARK 465 LEU B -129
REMARK 465 LEU B -128
REMARK 465 THR B -127
REMARK 465 LYS B -126
REMARK 465 SER B -125
REMARK 465 PRO B -124
REMARK 465 SER B -123
REMARK 465 LEU B -122
REMARK 465 ASN B -121
REMARK 465 ALA B -120
REMARK 465 ALA B -119
REMARK 465 LYS B -118
REMARK 465 SER B -117
REMARK 465 GLU B -116
REMARK 465 LEU B -115
REMARK 465 ASP B -114
REMARK 465 LYS B -113
REMARK 465 ALA B -112
REMARK 465 ILE B -111
REMARK 465 GLY B -110
REMARK 465 ARG B -109
REMARK 465 ASN B -108
REMARK 465 THR B -107
REMARK 465 ASN B -106
REMARK 465 GLY B -105
REMARK 465 GLY B 324
REMARK 465 LYS B 325
REMARK 465 ASN B 326
REMARK 465 PRO B 327
REMARK 465 LEU B 328
REMARK 465 GLN B 1990
REMARK 465 VAL B 1991
REMARK 465 ALA B 1992
REMARK 465 PRO B 1993
REMARK 465 ALA B 1994
REMARK 465 GLY B 1995
REMARK 465 SER B 1996
REMARK 465 ALA B 1997
REMARK 465 GLY B 1998
REMARK 465 SER B 1999
REMARK 465 ALA B 2000
REMARK 465 GLY B 2001
REMARK 465 SER B 2002
REMARK 465 ALA B 2003
REMARK 465 GLY B 2004
REMARK 465 SER B 2005
REMARK 465 ALA B 2006
REMARK 465 GLY B 2007
REMARK 465 SER B 2008
REMARK 465 ALA B 2009
REMARK 465 SER B 2010
REMARK 465 HIS B 2011
REMARK 465 GLU B 2362
REMARK 465 ASP B 2363
REMARK 465 PRO B 2364
REMARK 465 ALA B 2365
REMARK 465 LYS B 2366
REMARK 465 GLU B 2367
REMARK 465 SER B 2368
REMARK 465 VAL B 2369
REMARK 465 GLN B 2370
REMARK 465 ASP B 2371
REMARK 465 GLU B 2372
REMARK 465 ASN B 2373
REMARK 465 ALA B 2374
REMARK 465 ALA B 2375
REMARK 465 ALA B 2376
REMARK 465 GLU B 2377
REMARK 465 GLU B 2378
REMARK 465 PHE B 2379
REMARK 465 ALA B 2380
REMARK 465 ARG B 2381
REMARK 465 GLN B 2382
REMARK 465 ASN B 2383
REMARK 465 LEU B 2384
REMARK 465 LYS B 2385
REMARK 465 ASP B 2386
REMARK 465 THR B 2387
REMARK 465 GLY B 2388
REMARK 465 GLU B 2389
REMARK 465 ASN B 2390
REMARK 465 THR B 2391
REMARK 465 GLU B 2392
REMARK 465 LYS C 325
REMARK 465 ASN C 326
REMARK 465 PRO C 327
REMARK 465 LEU C 328
REMARK 465 GLN C 1990
REMARK 465 VAL C 1991
REMARK 465 ALA C 1992
REMARK 465 PRO C 1993
REMARK 465 ALA C 1994
REMARK 465 GLY C 1995
REMARK 465 SER C 1996
REMARK 465 ALA C 1997
REMARK 465 GLY C 1998
REMARK 465 SER C 1999
REMARK 465 ALA C 2000
REMARK 465 GLY C 2001
REMARK 465 SER C 2002
REMARK 465 ALA C 2003
REMARK 465 GLY C 2004
REMARK 465 SER C 2005
REMARK 465 ALA C 2006
REMARK 465 GLY C 2007
REMARK 465 SER C 2008
REMARK 465 ALA C 2009
REMARK 465 SER C 2010
REMARK 465 GLU C 2362
REMARK 465 ASP C 2363
REMARK 465 PRO C 2364
REMARK 465 ALA C 2365
REMARK 465 LYS C 2366
REMARK 465 GLU C 2367
REMARK 465 SER C 2368
REMARK 465 VAL C 2369
REMARK 465 GLN C 2370
REMARK 465 ASP C 2371
REMARK 465 GLU C 2372
REMARK 465 ASN C 2373
REMARK 465 ALA C 2374
REMARK 465 ALA C 2375
REMARK 465 ALA C 2376
REMARK 465 GLU C 2377
REMARK 465 GLU C 2378
REMARK 465 PHE C 2379
REMARK 465 ALA C 2380
REMARK 465 ARG C 2381
REMARK 465 GLN C 2382
REMARK 465 ASN C 2383
REMARK 465 LEU C 2384
REMARK 465 LYS C 2385
REMARK 465 ASP C 2386
REMARK 465 THR C 2387
REMARK 465 GLY C 2388
REMARK 465 GLU C 2389
REMARK 465 ASN C 2390
REMARK 465 THR C 2391
REMARK 465 GLU C 2392
REMARK 465 ASN D -159
REMARK 465 ILE D -158
REMARK 465 PHE D -157
REMARK 465 GLU D -156
REMARK 465 MET D -155
REMARK 465 LEU D -154
REMARK 465 ARG D -153
REMARK 465 ILE D -152
REMARK 465 ASP D -151
REMARK 465 GLU D -150
REMARK 465 GLY D -149
REMARK 465 LEU D -148
REMARK 465 ARG D -147
REMARK 465 LEU D -146
REMARK 465 LYS D -145
REMARK 465 ILE D -144
REMARK 465 TYR D -143
REMARK 465 LYS D -142
REMARK 465 ASP D -141
REMARK 465 THR D -140
REMARK 465 GLU D -139
REMARK 465 GLY D -138
REMARK 465 TYR D -137
REMARK 465 TYR D -136
REMARK 465 THR D -135
REMARK 465 ILE D -134
REMARK 465 GLY D -133
REMARK 465 ILE D -132
REMARK 465 GLY D -131
REMARK 465 HIS D -130
REMARK 465 LEU D -129
REMARK 465 LEU D -128
REMARK 465 THR D -127
REMARK 465 LYS D -126
REMARK 465 SER D -125
REMARK 465 PRO D -124
REMARK 465 SER D -123
REMARK 465 LEU D -122
REMARK 465 ASN D -121
REMARK 465 ALA D -120
REMARK 465 ALA D -119
REMARK 465 LYS D -118
REMARK 465 SER D -117
REMARK 465 GLU D -116
REMARK 465 LEU D -115
REMARK 465 ASP D -114
REMARK 465 LYS D -113
REMARK 465 ALA D -112
REMARK 465 ILE D -111
REMARK 465 GLY D -110
REMARK 465 ARG D -109
REMARK 465 ASN D -108
REMARK 465 THR D -107
REMARK 465 ASN D -106
REMARK 465 GLY D -105
REMARK 465 VAL D -104
REMARK 465 ILE D -103
REMARK 465 THR D -102
REMARK 465 LYS D -101
REMARK 465 ASP D -100
REMARK 465 GLU D -99
REMARK 465 ALA D -98
REMARK 465 GLU D -97
REMARK 465 LYS D -96
REMARK 465 LEU D -95
REMARK 465 PHE D -94
REMARK 465 ASN D -93
REMARK 465 GLN D -92
REMARK 465 ASP D -91
REMARK 465 VAL D -90
REMARK 465 ASP D -89
REMARK 465 ALA D -88
REMARK 465 ALA D -87
REMARK 465 VAL D -86
REMARK 465 LYS D 325
REMARK 465 ASN D 326
REMARK 465 PRO D 327
REMARK 465 LEU D 328
REMARK 465 GLY D 329
REMARK 465 GLN D 1990
REMARK 465 VAL D 1991
REMARK 465 ALA D 1992
REMARK 465 PRO D 1993
REMARK 465 ALA D 1994
REMARK 465 GLY D 1995
REMARK 465 SER D 1996
REMARK 465 ALA D 1997
REMARK 465 GLY D 1998
REMARK 465 SER D 1999
REMARK 465 ALA D 2000
REMARK 465 GLY D 2001
REMARK 465 SER D 2002
REMARK 465 ALA D 2003
REMARK 465 GLY D 2004
REMARK 465 SER D 2005
REMARK 465 ALA D 2006
REMARK 465 GLY D 2007
REMARK 465 SER D 2008
REMARK 465 ALA D 2009
REMARK 465 SER D 2010
REMARK 465 HIS D 2011
REMARK 465 GLU D 2362
REMARK 465 ASP D 2363
REMARK 465 PRO D 2364
REMARK 465 ALA D 2365
REMARK 465 LYS D 2366
REMARK 465 GLU D 2367
REMARK 465 SER D 2368
REMARK 465 VAL D 2369
REMARK 465 GLN D 2370
REMARK 465 ASP D 2371
REMARK 465 GLU D 2372
REMARK 465 ASN D 2373
REMARK 465 ALA D 2374
REMARK 465 ALA D 2375
REMARK 465 ALA D 2376
REMARK 465 GLU D 2377
REMARK 465 GLU D 2378
REMARK 465 PHE D 2379
REMARK 465 ALA D 2380
REMARK 465 ARG D 2381
REMARK 465 GLN D 2382
REMARK 465 ASN D 2383
REMARK 465 LEU D 2384
REMARK 465 LYS D 2385
REMARK 465 ASP D 2386
REMARK 465 THR D 2387
REMARK 465 GLY D 2388
REMARK 465 GLU D 2389
REMARK 465 ASN D 2390
REMARK 465 THR D 2391
REMARK 465 GLU D 2392
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 VAL A2075 CG1 CG2
REMARK 470 PHE A2080 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B2075 CG1 CG2
REMARK 470 MET B2076 CG SD CE
REMARK 470 PHE B2080 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL C2075 CG1 CG2
REMARK 470 PHE C2080 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D2075 CG1 CG2
REMARK 470 MET D2076 CG SD CE
REMARK 470 PHE D2080 CG CD1 CD2 CE1 CE2 CZ
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 SER A 176 -144.62 54.79
REMARK 500 PHE A 212 -62.60 -132.30
REMARK 500 ILE A 300 -61.75 -104.59
REMARK 500 ALA A 333 -71.23 -74.20
REMARK 500 TPO A 336 83.73 -154.60
REMARK 500 LEU A2078 -11.68 86.14
REMARK 500 VAL A2140 -62.09 -104.74
REMARK 500 GLU A2162 -50.17 -126.57
REMARK 500 LEU A2250 -79.56 -125.71
REMARK 500 LYS A2301 -127.71 55.17
REMARK 500 SER B 176 -146.27 54.57
REMARK 500 PHE B 212 -62.61 -132.70
REMARK 500 ILE B 307 -61.38 -98.52
REMARK 500 ALA B 333 -70.08 -71.85
REMARK 500 LEU B2078 -9.55 77.77
REMARK 500 VAL B2140 -61.65 -105.15
REMARK 500 GLU B2162 -50.29 -125.34
REMARK 500 LEU B2250 -79.75 -124.01
REMARK 500 LYS B2301 -130.45 59.85
REMARK 500 SER C 176 -144.29 54.91
REMARK 500 PHE C 212 -62.07 -132.27
REMARK 500 ILE C 300 -62.14 -104.76
REMARK 500 ILE C 307 -60.73 -100.87
REMARK 500 SER C 334 -108.81 58.28
REMARK 500 LEU C2078 -14.26 81.51
REMARK 500 VAL C2140 -62.38 -106.56
REMARK 500 GLU C2162 -52.16 -123.12
REMARK 500 LEU C2250 -79.64 -125.17
REMARK 500 LYS C2301 -129.58 57.33
REMARK 500 SER D 176 -144.53 55.25
REMARK 500 PHE D 212 -62.22 -132.05
REMARK 500 ILE D 300 -61.50 -104.49
REMARK 500 ILE D 307 -61.43 -100.95
REMARK 500 LEU D2078 -7.21 81.78
REMARK 500 VAL D2140 -61.77 -104.30
REMARK 500 LEU D2250 -79.56 -124.59
REMARK 500 LYS D2301 -129.86 55.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZWJ RELATED DB: PDB
REMARK 900 REPICKED XFEL DATA IMAGES AND REPROCESSED DATA USING UPDATED
REMARK 900 PROGRAMS; LARGELY REBUILT AND RE-REFINED MODEL.
DBREF1 5W0P A -159 0 UNP A0A097J792_BPT4
DBREF2 5W0P A A0A097J792 2 161
DBREF 5W0P A 1 1994 UNP P08100 OPSD_HUMAN 1 348
DBREF 5W0P A 2010 2392 UNP P20443 ARRS_MOUSE 10 392
DBREF1 5W0P B -159 0 UNP A0A097J792_BPT4
DBREF2 5W0P B A0A097J792 2 161
DBREF 5W0P B 1 1994 UNP P08100 OPSD_HUMAN 1 348
DBREF 5W0P B 2010 2392 UNP P20443 ARRS_MOUSE 10 392
DBREF1 5W0P C -159 0 UNP A0A097J792_BPT4
DBREF2 5W0P C A0A097J792 2 161
DBREF 5W0P C 1 1994 UNP P08100 OPSD_HUMAN 1 348
DBREF 5W0P C 2010 2392 UNP P20443 ARRS_MOUSE 10 392
DBREF1 5W0P D -159 0 UNP A0A097J792_BPT4
DBREF2 5W0P D A0A097J792 2 161
DBREF 5W0P D 1 1994 UNP P08100 OPSD_HUMAN 1 348
DBREF 5W0P D 2010 2392 UNP P20443 ARRS_MOUSE 10 392
SEQADV 5W0P THR A -107 UNP A0A097J79 CYS 54 ENGINEERED MUTATION
SEQADV 5W0P ALA A -64 UNP A0A097J79 CYS 97 ENGINEERED MUTATION
SEQADV 5W0P CYS A 2 UNP P08100 ASN 2 ENGINEERED MUTATION
SEQADV 5W0P GLN A 113 UNP P08100 GLU 113 ENGINEERED MUTATION
SEQADV 5W0P TYR A 257 UNP P08100 MET 257 ENGINEERED MUTATION
SEQADV 5W0P CYS A 282 UNP P08100 ASN 282 ENGINEERED MUTATION
SEQADV 5W0P GLY A 1995 UNP P08100 LINKER
SEQADV 5W0P SER A 1996 UNP P08100 LINKER
SEQADV 5W0P ALA A 1997 UNP P08100 LINKER
SEQADV 5W0P GLY A 1998 UNP P08100 LINKER
SEQADV 5W0P SER A 1999 UNP P08100 LINKER
SEQADV 5W0P ALA A 2000 UNP P08100 LINKER
SEQADV 5W0P GLY A 2001 UNP P08100 LINKER
SEQADV 5W0P SER A 2002 UNP P08100 LINKER
SEQADV 5W0P ALA A 2003 UNP P08100 LINKER
SEQADV 5W0P GLY A 2004 UNP P08100 LINKER
SEQADV 5W0P SER A 2005 UNP P08100 LINKER
SEQADV 5W0P ALA A 2006 UNP P08100 LINKER
SEQADV 5W0P GLY A 2007 UNP P08100 LINKER
SEQADV 5W0P SER A 2008 UNP P08100 LINKER
SEQADV 5W0P ALA A 2009 UNP P08100 LINKER
SEQADV 5W0P ALA A 2374 UNP P20443 LEU 374 ENGINEERED MUTATION
SEQADV 5W0P ALA A 2375 UNP P20443 VAL 375 ENGINEERED MUTATION
SEQADV 5W0P ALA A 2376 UNP P20443 PHE 376 ENGINEERED MUTATION
SEQADV 5W0P THR B -107 UNP A0A097J79 CYS 54 ENGINEERED MUTATION
SEQADV 5W0P ALA B -64 UNP A0A097J79 CYS 97 ENGINEERED MUTATION
SEQADV 5W0P CYS B 2 UNP P08100 ASN 2 ENGINEERED MUTATION
SEQADV 5W0P GLN B 113 UNP P08100 GLU 113 ENGINEERED MUTATION
SEQADV 5W0P TYR B 257 UNP P08100 MET 257 ENGINEERED MUTATION
SEQADV 5W0P CYS B 282 UNP P08100 ASN 282 ENGINEERED MUTATION
SEQADV 5W0P GLY B 1995 UNP P08100 LINKER
SEQADV 5W0P SER B 1996 UNP P08100 LINKER
SEQADV 5W0P ALA B 1997 UNP P08100 LINKER
SEQADV 5W0P GLY B 1998 UNP P08100 LINKER
SEQADV 5W0P SER B 1999 UNP P08100 LINKER
SEQADV 5W0P ALA B 2000 UNP P08100 LINKER
SEQADV 5W0P GLY B 2001 UNP P08100 LINKER
SEQADV 5W0P SER B 2002 UNP P08100 LINKER
SEQADV 5W0P ALA B 2003 UNP P08100 LINKER
SEQADV 5W0P GLY B 2004 UNP P08100 LINKER
SEQADV 5W0P SER B 2005 UNP P08100 LINKER
SEQADV 5W0P ALA B 2006 UNP P08100 LINKER
SEQADV 5W0P GLY B 2007 UNP P08100 LINKER
SEQADV 5W0P SER B 2008 UNP P08100 LINKER
SEQADV 5W0P ALA B 2009 UNP P08100 LINKER
SEQADV 5W0P ALA B 2374 UNP P20443 LEU 374 ENGINEERED MUTATION
SEQADV 5W0P ALA B 2375 UNP P20443 VAL 375 ENGINEERED MUTATION
SEQADV 5W0P ALA B 2376 UNP P20443 PHE 376 ENGINEERED MUTATION
SEQADV 5W0P THR C -107 UNP A0A097J79 CYS 54 ENGINEERED MUTATION
SEQADV 5W0P ALA C -64 UNP A0A097J79 CYS 97 ENGINEERED MUTATION
SEQADV 5W0P CYS C 2 UNP P08100 ASN 2 ENGINEERED MUTATION
SEQADV 5W0P GLN C 113 UNP P08100 GLU 113 ENGINEERED MUTATION
SEQADV 5W0P TYR C 257 UNP P08100 MET 257 ENGINEERED MUTATION
SEQADV 5W0P CYS C 282 UNP P08100 ASN 282 ENGINEERED MUTATION
SEQADV 5W0P GLY C 1995 UNP P08100 LINKER
SEQADV 5W0P SER C 1996 UNP P08100 LINKER
SEQADV 5W0P ALA C 1997 UNP P08100 LINKER
SEQADV 5W0P GLY C 1998 UNP P08100 LINKER
SEQADV 5W0P SER C 1999 UNP P08100 LINKER
SEQADV 5W0P ALA C 2000 UNP P08100 LINKER
SEQADV 5W0P GLY C 2001 UNP P08100 LINKER
SEQADV 5W0P SER C 2002 UNP P08100 LINKER
SEQADV 5W0P ALA C 2003 UNP P08100 LINKER
SEQADV 5W0P GLY C 2004 UNP P08100 LINKER
SEQADV 5W0P SER C 2005 UNP P08100 LINKER
SEQADV 5W0P ALA C 2006 UNP P08100 LINKER
SEQADV 5W0P GLY C 2007 UNP P08100 LINKER
SEQADV 5W0P SER C 2008 UNP P08100 LINKER
SEQADV 5W0P ALA C 2009 UNP P08100 LINKER
SEQADV 5W0P ALA C 2374 UNP P20443 LEU 374 ENGINEERED MUTATION
SEQADV 5W0P ALA C 2375 UNP P20443 VAL 375 ENGINEERED MUTATION
SEQADV 5W0P ALA C 2376 UNP P20443 PHE 376 ENGINEERED MUTATION
SEQADV 5W0P THR D -107 UNP A0A097J79 CYS 54 ENGINEERED MUTATION
SEQADV 5W0P ALA D -64 UNP A0A097J79 CYS 97 ENGINEERED MUTATION
SEQADV 5W0P CYS D 2 UNP P08100 ASN 2 ENGINEERED MUTATION
SEQADV 5W0P GLN D 113 UNP P08100 GLU 113 ENGINEERED MUTATION
SEQADV 5W0P TYR D 257 UNP P08100 MET 257 ENGINEERED MUTATION
SEQADV 5W0P CYS D 282 UNP P08100 ASN 282 ENGINEERED MUTATION
SEQADV 5W0P GLY D 1995 UNP P08100 LINKER
SEQADV 5W0P SER D 1996 UNP P08100 LINKER
SEQADV 5W0P ALA D 1997 UNP P08100 LINKER
SEQADV 5W0P GLY D 1998 UNP P08100 LINKER
SEQADV 5W0P SER D 1999 UNP P08100 LINKER
SEQADV 5W0P ALA D 2000 UNP P08100 LINKER
SEQADV 5W0P GLY D 2001 UNP P08100 LINKER
SEQADV 5W0P SER D 2002 UNP P08100 LINKER
SEQADV 5W0P ALA D 2003 UNP P08100 LINKER
SEQADV 5W0P GLY D 2004 UNP P08100 LINKER
SEQADV 5W0P SER D 2005 UNP P08100 LINKER
SEQADV 5W0P ALA D 2006 UNP P08100 LINKER
SEQADV 5W0P GLY D 2007 UNP P08100 LINKER
SEQADV 5W0P SER D 2008 UNP P08100 LINKER
SEQADV 5W0P ALA D 2009 UNP P08100 LINKER
SEQADV 5W0P ALA D 2374 UNP P20443 LEU 374 ENGINEERED MUTATION
SEQADV 5W0P ALA D 2375 UNP P20443 VAL 375 ENGINEERED MUTATION
SEQADV 5W0P ALA D 2376 UNP P20443 PHE 376 ENGINEERED MUTATION
SEQRES 1 A 906 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 2 A 906 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 3 A 906 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN
SEQRES 4 A 906 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 5 A 906 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 6 A 906 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 7 A 906 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 8 A 906 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 9 A 906 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 10 A 906 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 11 A 906 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 12 A 906 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 13 A 906 TRP ASP ALA TYR MET CYS GLY THR GLU GLY PRO ASN PHE
SEQRES 14 A 906 TYR VAL PRO PHE SER ASN ALA THR GLY VAL VAL ARG SER
SEQRES 15 A 906 PRO PHE GLU TYR PRO GLN TYR TYR LEU ALA GLU PRO TRP
SEQRES 16 A 906 GLN PHE SER MET LEU ALA ALA TYR MET PHE LEU LEU ILE
SEQRES 17 A 906 VAL LEU GLY PHE PRO ILE ASN PHE LEU THR LEU TYR VAL
SEQRES 18 A 906 THR VAL GLN HIS LYS LYS LEU ARG THR PRO LEU ASN TYR
SEQRES 19 A 906 ILE LEU LEU ASN LEU ALA VAL ALA ASP LEU PHE MET VAL
SEQRES 20 A 906 LEU GLY GLY PHE THR SER THR LEU TYR THR SER LEU HIS
SEQRES 21 A 906 GLY TYR PHE VAL PHE GLY PRO THR GLY CYS ASN LEU GLN
SEQRES 22 A 906 GLY PHE PHE ALA THR LEU GLY GLY GLU ILE ALA LEU TRP
SEQRES 23 A 906 SER LEU VAL VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL
SEQRES 24 A 906 CYS LYS PRO MET SER ASN PHE ARG PHE GLY GLU ASN HIS
SEQRES 25 A 906 ALA ILE MET GLY VAL ALA PHE THR TRP VAL MET ALA LEU
SEQRES 26 A 906 ALA CYS ALA ALA PRO PRO LEU ALA GLY TRP SER ARG TYR
SEQRES 27 A 906 ILE PRO GLU GLY LEU GLN CYS SER CYS GLY ILE ASP TYR
SEQRES 28 A 906 TYR THR LEU LYS PRO GLU VAL ASN ASN GLU SER PHE VAL
SEQRES 29 A 906 ILE TYR MET PHE VAL VAL HIS PHE THR ILE PRO MET ILE
SEQRES 30 A 906 ILE ILE PHE PHE CYS TYR GLY GLN LEU VAL PHE THR VAL
SEQRES 31 A 906 LYS GLU ALA ALA ALA GLN GLN GLN GLU SER ALA THR THR
SEQRES 32 A 906 GLN LYS ALA GLU LYS GLU VAL THR ARG MET VAL ILE ILE
SEQRES 33 A 906 TYR VAL ILE ALA PHE LEU ILE CYS TRP VAL PRO TYR ALA
SEQRES 34 A 906 SER VAL ALA PHE TYR ILE PHE THR HIS GLN GLY SER CYS
SEQRES 35 A 906 PHE GLY PRO ILE PHE MET THR ILE PRO ALA PHE PHE ALA
SEQRES 36 A 906 LYS SER ALA ALA ILE TYR ASN PRO VAL ILE TYR ILE MET
SEQRES 37 A 906 MET ASN LYS GLN PHE ARG ASN CYS MET LEU THR THR ILE
SEQRES 38 A 906 CYS CYS GLY LYS ASN PRO LEU GLY ASP ASP GLU ALA SER
SEQRES 39 A 906 ALA TPO VAL SEP LYS THR GLU THR SER GLN VAL ALA PRO
SEQRES 40 A 906 ALA GLY SER ALA GLY SER ALA GLY SER ALA GLY SER ALA
SEQRES 41 A 906 GLY SER ALA SER HIS VAL ILE PHE LYS LYS VAL SER ARG
SEQRES 42 A 906 ASP LYS SER VAL THR ILE TYR LEU GLY LYS ARG ASP TYR
SEQRES 43 A 906 VAL ASP HIS VAL SER GLN VAL GLU PRO VAL ASP GLY VAL
SEQRES 44 A 906 VAL LEU VAL ASP PRO GLU LEU VAL LYS GLY LYS LYS VAL
SEQRES 45 A 906 TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY GLN GLU
SEQRES 46 A 906 ASP ILE ASP VAL MET GLY LEU THR PHE ARG ARG ASP LEU
SEQRES 47 A 906 TYR PHE SER ARG VAL GLN VAL TYR PRO PRO VAL GLY ALA
SEQRES 48 A 906 MET SER VAL LEU THR GLN LEU GLN GLU SER LEU LEU LYS
SEQRES 49 A 906 LYS LEU GLY ASP ASN THR TYR PRO PHE LEU LEU THR PHE
SEQRES 50 A 906 PRO ASP TYR LEU PRO CYS SER VAL MET LEU GLN PRO ALA
SEQRES 51 A 906 PRO GLN ASP VAL GLY LYS SER CYS GLY VAL ASP PHE GLU
SEQRES 52 A 906 VAL LYS ALA PHE ALA SER ASP ILE THR ASP PRO GLU GLU
SEQRES 53 A 906 ASP LYS ILE PRO LYS LYS SER SER VAL ARG LEU LEU ILE
SEQRES 54 A 906 ARG LYS VAL GLN HIS ALA PRO PRO GLU MET GLY PRO GLN
SEQRES 55 A 906 PRO SER ALA GLU ALA SER TRP GLN PHE PHE MET SER ASP
SEQRES 56 A 906 LYS PRO LEU ASN LEU SER VAL SER LEU SER LYS GLU ILE
SEQRES 57 A 906 TYR PHE HIS GLY GLU PRO ILE PRO VAL THR VAL THR VAL
SEQRES 58 A 906 THR ASN ASN THR ASP LYS VAL VAL LYS LYS ILE LYS VAL
SEQRES 59 A 906 SER VAL GLU GLN ILE ALA ASN VAL VAL LEU TYR SER SER
SEQRES 60 A 906 ASP TYR TYR VAL LYS PRO VAL ALA SER GLU GLU THR GLN
SEQRES 61 A 906 GLU LYS VAL GLN PRO ASN SER THR LEU THR LYS THR LEU
SEQRES 62 A 906 VAL LEU VAL PRO LEU LEU ALA ASN ASN ARG GLU ARG ARG
SEQRES 63 A 906 GLY ILE ALA LEU ASP GLY LYS ILE LYS HIS GLU ASP THR
SEQRES 64 A 906 ASN LEU ALA SER SER THR ILE ILE LYS GLU GLY ILE ASP
SEQRES 65 A 906 ARG THR VAL MET GLY ILE LEU VAL SER TYR HIS ILE LYS
SEQRES 66 A 906 VAL LYS LEU THR VAL SER GLY PHE LEU GLY GLU LEU THR
SEQRES 67 A 906 SER SER GLU VAL ALA THR GLU VAL PRO PHE ARG LEU MET
SEQRES 68 A 906 HIS PRO GLN PRO GLU ASP PRO ALA LYS GLU SER VAL GLN
SEQRES 69 A 906 ASP GLU ASN ALA ALA ALA GLU GLU PHE ALA ARG GLN ASN
SEQRES 70 A 906 LEU LYS ASP THR GLY GLU ASN THR GLU
SEQRES 1 B 906 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 2 B 906 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 3 B 906 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN
SEQRES 4 B 906 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 5 B 906 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 6 B 906 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 7 B 906 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 8 B 906 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 9 B 906 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 10 B 906 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 11 B 906 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 12 B 906 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 13 B 906 TRP ASP ALA TYR MET CYS GLY THR GLU GLY PRO ASN PHE
SEQRES 14 B 906 TYR VAL PRO PHE SER ASN ALA THR GLY VAL VAL ARG SER
SEQRES 15 B 906 PRO PHE GLU TYR PRO GLN TYR TYR LEU ALA GLU PRO TRP
SEQRES 16 B 906 GLN PHE SER MET LEU ALA ALA TYR MET PHE LEU LEU ILE
SEQRES 17 B 906 VAL LEU GLY PHE PRO ILE ASN PHE LEU THR LEU TYR VAL
SEQRES 18 B 906 THR VAL GLN HIS LYS LYS LEU ARG THR PRO LEU ASN TYR
SEQRES 19 B 906 ILE LEU LEU ASN LEU ALA VAL ALA ASP LEU PHE MET VAL
SEQRES 20 B 906 LEU GLY GLY PHE THR SER THR LEU TYR THR SER LEU HIS
SEQRES 21 B 906 GLY TYR PHE VAL PHE GLY PRO THR GLY CYS ASN LEU GLN
SEQRES 22 B 906 GLY PHE PHE ALA THR LEU GLY GLY GLU ILE ALA LEU TRP
SEQRES 23 B 906 SER LEU VAL VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL
SEQRES 24 B 906 CYS LYS PRO MET SER ASN PHE ARG PHE GLY GLU ASN HIS
SEQRES 25 B 906 ALA ILE MET GLY VAL ALA PHE THR TRP VAL MET ALA LEU
SEQRES 26 B 906 ALA CYS ALA ALA PRO PRO LEU ALA GLY TRP SER ARG TYR
SEQRES 27 B 906 ILE PRO GLU GLY LEU GLN CYS SER CYS GLY ILE ASP TYR
SEQRES 28 B 906 TYR THR LEU LYS PRO GLU VAL ASN ASN GLU SER PHE VAL
SEQRES 29 B 906 ILE TYR MET PHE VAL VAL HIS PHE THR ILE PRO MET ILE
SEQRES 30 B 906 ILE ILE PHE PHE CYS TYR GLY GLN LEU VAL PHE THR VAL
SEQRES 31 B 906 LYS GLU ALA ALA ALA GLN GLN GLN GLU SER ALA THR THR
SEQRES 32 B 906 GLN LYS ALA GLU LYS GLU VAL THR ARG MET VAL ILE ILE
SEQRES 33 B 906 TYR VAL ILE ALA PHE LEU ILE CYS TRP VAL PRO TYR ALA
SEQRES 34 B 906 SER VAL ALA PHE TYR ILE PHE THR HIS GLN GLY SER CYS
SEQRES 35 B 906 PHE GLY PRO ILE PHE MET THR ILE PRO ALA PHE PHE ALA
SEQRES 36 B 906 LYS SER ALA ALA ILE TYR ASN PRO VAL ILE TYR ILE MET
SEQRES 37 B 906 MET ASN LYS GLN PHE ARG ASN CYS MET LEU THR THR ILE
SEQRES 38 B 906 CYS CYS GLY LYS ASN PRO LEU GLY ASP ASP GLU ALA SER
SEQRES 39 B 906 ALA TPO VAL SEP LYS THR GLU THR SER GLN VAL ALA PRO
SEQRES 40 B 906 ALA GLY SER ALA GLY SER ALA GLY SER ALA GLY SER ALA
SEQRES 41 B 906 GLY SER ALA SER HIS VAL ILE PHE LYS LYS VAL SER ARG
SEQRES 42 B 906 ASP LYS SER VAL THR ILE TYR LEU GLY LYS ARG ASP TYR
SEQRES 43 B 906 VAL ASP HIS VAL SER GLN VAL GLU PRO VAL ASP GLY VAL
SEQRES 44 B 906 VAL LEU VAL ASP PRO GLU LEU VAL LYS GLY LYS LYS VAL
SEQRES 45 B 906 TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY GLN GLU
SEQRES 46 B 906 ASP ILE ASP VAL MET GLY LEU THR PHE ARG ARG ASP LEU
SEQRES 47 B 906 TYR PHE SER ARG VAL GLN VAL TYR PRO PRO VAL GLY ALA
SEQRES 48 B 906 MET SER VAL LEU THR GLN LEU GLN GLU SER LEU LEU LYS
SEQRES 49 B 906 LYS LEU GLY ASP ASN THR TYR PRO PHE LEU LEU THR PHE
SEQRES 50 B 906 PRO ASP TYR LEU PRO CYS SER VAL MET LEU GLN PRO ALA
SEQRES 51 B 906 PRO GLN ASP VAL GLY LYS SER CYS GLY VAL ASP PHE GLU
SEQRES 52 B 906 VAL LYS ALA PHE ALA SER ASP ILE THR ASP PRO GLU GLU
SEQRES 53 B 906 ASP LYS ILE PRO LYS LYS SER SER VAL ARG LEU LEU ILE
SEQRES 54 B 906 ARG LYS VAL GLN HIS ALA PRO PRO GLU MET GLY PRO GLN
SEQRES 55 B 906 PRO SER ALA GLU ALA SER TRP GLN PHE PHE MET SER ASP
SEQRES 56 B 906 LYS PRO LEU ASN LEU SER VAL SER LEU SER LYS GLU ILE
SEQRES 57 B 906 TYR PHE HIS GLY GLU PRO ILE PRO VAL THR VAL THR VAL
SEQRES 58 B 906 THR ASN ASN THR ASP LYS VAL VAL LYS LYS ILE LYS VAL
SEQRES 59 B 906 SER VAL GLU GLN ILE ALA ASN VAL VAL LEU TYR SER SER
SEQRES 60 B 906 ASP TYR TYR VAL LYS PRO VAL ALA SER GLU GLU THR GLN
SEQRES 61 B 906 GLU LYS VAL GLN PRO ASN SER THR LEU THR LYS THR LEU
SEQRES 62 B 906 VAL LEU VAL PRO LEU LEU ALA ASN ASN ARG GLU ARG ARG
SEQRES 63 B 906 GLY ILE ALA LEU ASP GLY LYS ILE LYS HIS GLU ASP THR
SEQRES 64 B 906 ASN LEU ALA SER SER THR ILE ILE LYS GLU GLY ILE ASP
SEQRES 65 B 906 ARG THR VAL MET GLY ILE LEU VAL SER TYR HIS ILE LYS
SEQRES 66 B 906 VAL LYS LEU THR VAL SER GLY PHE LEU GLY GLU LEU THR
SEQRES 67 B 906 SER SER GLU VAL ALA THR GLU VAL PRO PHE ARG LEU MET
SEQRES 68 B 906 HIS PRO GLN PRO GLU ASP PRO ALA LYS GLU SER VAL GLN
SEQRES 69 B 906 ASP GLU ASN ALA ALA ALA GLU GLU PHE ALA ARG GLN ASN
SEQRES 70 B 906 LEU LYS ASP THR GLY GLU ASN THR GLU
SEQRES 1 C 906 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 2 C 906 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 3 C 906 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN
SEQRES 4 C 906 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 5 C 906 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 6 C 906 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 7 C 906 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 8 C 906 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 9 C 906 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 10 C 906 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 11 C 906 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 12 C 906 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 13 C 906 TRP ASP ALA TYR MET CYS GLY THR GLU GLY PRO ASN PHE
SEQRES 14 C 906 TYR VAL PRO PHE SER ASN ALA THR GLY VAL VAL ARG SER
SEQRES 15 C 906 PRO PHE GLU TYR PRO GLN TYR TYR LEU ALA GLU PRO TRP
SEQRES 16 C 906 GLN PHE SER MET LEU ALA ALA TYR MET PHE LEU LEU ILE
SEQRES 17 C 906 VAL LEU GLY PHE PRO ILE ASN PHE LEU THR LEU TYR VAL
SEQRES 18 C 906 THR VAL GLN HIS LYS LYS LEU ARG THR PRO LEU ASN TYR
SEQRES 19 C 906 ILE LEU LEU ASN LEU ALA VAL ALA ASP LEU PHE MET VAL
SEQRES 20 C 906 LEU GLY GLY PHE THR SER THR LEU TYR THR SER LEU HIS
SEQRES 21 C 906 GLY TYR PHE VAL PHE GLY PRO THR GLY CYS ASN LEU GLN
SEQRES 22 C 906 GLY PHE PHE ALA THR LEU GLY GLY GLU ILE ALA LEU TRP
SEQRES 23 C 906 SER LEU VAL VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL
SEQRES 24 C 906 CYS LYS PRO MET SER ASN PHE ARG PHE GLY GLU ASN HIS
SEQRES 25 C 906 ALA ILE MET GLY VAL ALA PHE THR TRP VAL MET ALA LEU
SEQRES 26 C 906 ALA CYS ALA ALA PRO PRO LEU ALA GLY TRP SER ARG TYR
SEQRES 27 C 906 ILE PRO GLU GLY LEU GLN CYS SER CYS GLY ILE ASP TYR
SEQRES 28 C 906 TYR THR LEU LYS PRO GLU VAL ASN ASN GLU SER PHE VAL
SEQRES 29 C 906 ILE TYR MET PHE VAL VAL HIS PHE THR ILE PRO MET ILE
SEQRES 30 C 906 ILE ILE PHE PHE CYS TYR GLY GLN LEU VAL PHE THR VAL
SEQRES 31 C 906 LYS GLU ALA ALA ALA GLN GLN GLN GLU SER ALA THR THR
SEQRES 32 C 906 GLN LYS ALA GLU LYS GLU VAL THR ARG MET VAL ILE ILE
SEQRES 33 C 906 TYR VAL ILE ALA PHE LEU ILE CYS TRP VAL PRO TYR ALA
SEQRES 34 C 906 SER VAL ALA PHE TYR ILE PHE THR HIS GLN GLY SER CYS
SEQRES 35 C 906 PHE GLY PRO ILE PHE MET THR ILE PRO ALA PHE PHE ALA
SEQRES 36 C 906 LYS SER ALA ALA ILE TYR ASN PRO VAL ILE TYR ILE MET
SEQRES 37 C 906 MET ASN LYS GLN PHE ARG ASN CYS MET LEU THR THR ILE
SEQRES 38 C 906 CYS CYS GLY LYS ASN PRO LEU GLY ASP ASP GLU ALA SER
SEQRES 39 C 906 ALA THR VAL SEP LYS THR GLU THR SER GLN VAL ALA PRO
SEQRES 40 C 906 ALA GLY SER ALA GLY SER ALA GLY SER ALA GLY SER ALA
SEQRES 41 C 906 GLY SER ALA SER HIS VAL ILE PHE LYS LYS VAL SER ARG
SEQRES 42 C 906 ASP LYS SER VAL THR ILE TYR LEU GLY LYS ARG ASP TYR
SEQRES 43 C 906 VAL ASP HIS VAL SER GLN VAL GLU PRO VAL ASP GLY VAL
SEQRES 44 C 906 VAL LEU VAL ASP PRO GLU LEU VAL LYS GLY LYS LYS VAL
SEQRES 45 C 906 TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY GLN GLU
SEQRES 46 C 906 ASP ILE ASP VAL MET GLY LEU THR PHE ARG ARG ASP LEU
SEQRES 47 C 906 TYR PHE SER ARG VAL GLN VAL TYR PRO PRO VAL GLY ALA
SEQRES 48 C 906 MET SER VAL LEU THR GLN LEU GLN GLU SER LEU LEU LYS
SEQRES 49 C 906 LYS LEU GLY ASP ASN THR TYR PRO PHE LEU LEU THR PHE
SEQRES 50 C 906 PRO ASP TYR LEU PRO CYS SER VAL MET LEU GLN PRO ALA
SEQRES 51 C 906 PRO GLN ASP VAL GLY LYS SER CYS GLY VAL ASP PHE GLU
SEQRES 52 C 906 VAL LYS ALA PHE ALA SER ASP ILE THR ASP PRO GLU GLU
SEQRES 53 C 906 ASP LYS ILE PRO LYS LYS SER SER VAL ARG LEU LEU ILE
SEQRES 54 C 906 ARG LYS VAL GLN HIS ALA PRO PRO GLU MET GLY PRO GLN
SEQRES 55 C 906 PRO SER ALA GLU ALA SER TRP GLN PHE PHE MET SER ASP
SEQRES 56 C 906 LYS PRO LEU ASN LEU SER VAL SER LEU SER LYS GLU ILE
SEQRES 57 C 906 TYR PHE HIS GLY GLU PRO ILE PRO VAL THR VAL THR VAL
SEQRES 58 C 906 THR ASN ASN THR ASP LYS VAL VAL LYS LYS ILE LYS VAL
SEQRES 59 C 906 SER VAL GLU GLN ILE ALA ASN VAL VAL LEU TYR SER SER
SEQRES 60 C 906 ASP TYR TYR VAL LYS PRO VAL ALA SER GLU GLU THR GLN
SEQRES 61 C 906 GLU LYS VAL GLN PRO ASN SER THR LEU THR LYS THR LEU
SEQRES 62 C 906 VAL LEU VAL PRO LEU LEU ALA ASN ASN ARG GLU ARG ARG
SEQRES 63 C 906 GLY ILE ALA LEU ASP GLY LYS ILE LYS HIS GLU ASP THR
SEQRES 64 C 906 ASN LEU ALA SER SER THR ILE ILE LYS GLU GLY ILE ASP
SEQRES 65 C 906 ARG THR VAL MET GLY ILE LEU VAL SER TYR HIS ILE LYS
SEQRES 66 C 906 VAL LYS LEU THR VAL SER GLY PHE LEU GLY GLU LEU THR
SEQRES 67 C 906 SER SER GLU VAL ALA THR GLU VAL PRO PHE ARG LEU MET
SEQRES 68 C 906 HIS PRO GLN PRO GLU ASP PRO ALA LYS GLU SER VAL GLN
SEQRES 69 C 906 ASP GLU ASN ALA ALA ALA GLU GLU PHE ALA ARG GLN ASN
SEQRES 70 C 906 LEU LYS ASP THR GLY GLU ASN THR GLU
SEQRES 1 D 906 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 2 D 906 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 3 D 906 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN
SEQRES 4 D 906 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 5 D 906 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 6 D 906 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 7 D 906 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 8 D 906 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 9 D 906 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 10 D 906 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 11 D 906 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 12 D 906 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 13 D 906 TRP ASP ALA TYR MET CYS GLY THR GLU GLY PRO ASN PHE
SEQRES 14 D 906 TYR VAL PRO PHE SER ASN ALA THR GLY VAL VAL ARG SER
SEQRES 15 D 906 PRO PHE GLU TYR PRO GLN TYR TYR LEU ALA GLU PRO TRP
SEQRES 16 D 906 GLN PHE SER MET LEU ALA ALA TYR MET PHE LEU LEU ILE
SEQRES 17 D 906 VAL LEU GLY PHE PRO ILE ASN PHE LEU THR LEU TYR VAL
SEQRES 18 D 906 THR VAL GLN HIS LYS LYS LEU ARG THR PRO LEU ASN TYR
SEQRES 19 D 906 ILE LEU LEU ASN LEU ALA VAL ALA ASP LEU PHE MET VAL
SEQRES 20 D 906 LEU GLY GLY PHE THR SER THR LEU TYR THR SER LEU HIS
SEQRES 21 D 906 GLY TYR PHE VAL PHE GLY PRO THR GLY CYS ASN LEU GLN
SEQRES 22 D 906 GLY PHE PHE ALA THR LEU GLY GLY GLU ILE ALA LEU TRP
SEQRES 23 D 906 SER LEU VAL VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL
SEQRES 24 D 906 CYS LYS PRO MET SER ASN PHE ARG PHE GLY GLU ASN HIS
SEQRES 25 D 906 ALA ILE MET GLY VAL ALA PHE THR TRP VAL MET ALA LEU
SEQRES 26 D 906 ALA CYS ALA ALA PRO PRO LEU ALA GLY TRP SER ARG TYR
SEQRES 27 D 906 ILE PRO GLU GLY LEU GLN CYS SER CYS GLY ILE ASP TYR
SEQRES 28 D 906 TYR THR LEU LYS PRO GLU VAL ASN ASN GLU SER PHE VAL
SEQRES 29 D 906 ILE TYR MET PHE VAL VAL HIS PHE THR ILE PRO MET ILE
SEQRES 30 D 906 ILE ILE PHE PHE CYS TYR GLY GLN LEU VAL PHE THR VAL
SEQRES 31 D 906 LYS GLU ALA ALA ALA GLN GLN GLN GLU SER ALA THR THR
SEQRES 32 D 906 GLN LYS ALA GLU LYS GLU VAL THR ARG MET VAL ILE ILE
SEQRES 33 D 906 TYR VAL ILE ALA PHE LEU ILE CYS TRP VAL PRO TYR ALA
SEQRES 34 D 906 SER VAL ALA PHE TYR ILE PHE THR HIS GLN GLY SER CYS
SEQRES 35 D 906 PHE GLY PRO ILE PHE MET THR ILE PRO ALA PHE PHE ALA
SEQRES 36 D 906 LYS SER ALA ALA ILE TYR ASN PRO VAL ILE TYR ILE MET
SEQRES 37 D 906 MET ASN LYS GLN PHE ARG ASN CYS MET LEU THR THR ILE
SEQRES 38 D 906 CYS CYS GLY LYS ASN PRO LEU GLY ASP ASP GLU ALA SER
SEQRES 39 D 906 ALA THR VAL SEP LYS THR GLU THR SER GLN VAL ALA PRO
SEQRES 40 D 906 ALA GLY SER ALA GLY SER ALA GLY SER ALA GLY SER ALA
SEQRES 41 D 906 GLY SER ALA SER HIS VAL ILE PHE LYS LYS VAL SER ARG
SEQRES 42 D 906 ASP LYS SER VAL THR ILE TYR LEU GLY LYS ARG ASP TYR
SEQRES 43 D 906 VAL ASP HIS VAL SER GLN VAL GLU PRO VAL ASP GLY VAL
SEQRES 44 D 906 VAL LEU VAL ASP PRO GLU LEU VAL LYS GLY LYS LYS VAL
SEQRES 45 D 906 TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY GLN GLU
SEQRES 46 D 906 ASP ILE ASP VAL MET GLY LEU THR PHE ARG ARG ASP LEU
SEQRES 47 D 906 TYR PHE SER ARG VAL GLN VAL TYR PRO PRO VAL GLY ALA
SEQRES 48 D 906 MET SER VAL LEU THR GLN LEU GLN GLU SER LEU LEU LYS
SEQRES 49 D 906 LYS LEU GLY ASP ASN THR TYR PRO PHE LEU LEU THR PHE
SEQRES 50 D 906 PRO ASP TYR LEU PRO CYS SER VAL MET LEU GLN PRO ALA
SEQRES 51 D 906 PRO GLN ASP VAL GLY LYS SER CYS GLY VAL ASP PHE GLU
SEQRES 52 D 906 VAL LYS ALA PHE ALA SER ASP ILE THR ASP PRO GLU GLU
SEQRES 53 D 906 ASP LYS ILE PRO LYS LYS SER SER VAL ARG LEU LEU ILE
SEQRES 54 D 906 ARG LYS VAL GLN HIS ALA PRO PRO GLU MET GLY PRO GLN
SEQRES 55 D 906 PRO SER ALA GLU ALA SER TRP GLN PHE PHE MET SER ASP
SEQRES 56 D 906 LYS PRO LEU ASN LEU SER VAL SER LEU SER LYS GLU ILE
SEQRES 57 D 906 TYR PHE HIS GLY GLU PRO ILE PRO VAL THR VAL THR VAL
SEQRES 58 D 906 THR ASN ASN THR ASP LYS VAL VAL LYS LYS ILE LYS VAL
SEQRES 59 D 906 SER VAL GLU GLN ILE ALA ASN VAL VAL LEU TYR SER SER
SEQRES 60 D 906 ASP TYR TYR VAL LYS PRO VAL ALA SER GLU GLU THR GLN
SEQRES 61 D 906 GLU LYS VAL GLN PRO ASN SER THR LEU THR LYS THR LEU
SEQRES 62 D 906 VAL LEU VAL PRO LEU LEU ALA ASN ASN ARG GLU ARG ARG
SEQRES 63 D 906 GLY ILE ALA LEU ASP GLY LYS ILE LYS HIS GLU ASP THR
SEQRES 64 D 906 ASN LEU ALA SER SER THR ILE ILE LYS GLU GLY ILE ASP
SEQRES 65 D 906 ARG THR VAL MET GLY ILE LEU VAL SER TYR HIS ILE LYS
SEQRES 66 D 906 VAL LYS LEU THR VAL SER GLY PHE LEU GLY GLU LEU THR
SEQRES 67 D 906 SER SER GLU VAL ALA THR GLU VAL PRO PHE ARG LEU MET
SEQRES 68 D 906 HIS PRO GLN PRO GLU ASP PRO ALA LYS GLU SER VAL GLN
SEQRES 69 D 906 ASP GLU ASN ALA ALA ALA GLU GLU PHE ALA ARG GLN ASN
SEQRES 70 D 906 LEU LYS ASP THR GLY GLU ASN THR GLU
MODRES 5W0P TPO A 336 THR MODIFIED RESIDUE
MODRES 5W0P SEP A 338 SER MODIFIED RESIDUE
MODRES 5W0P TPO B 336 THR MODIFIED RESIDUE
MODRES 5W0P SEP B 338 SER MODIFIED RESIDUE
MODRES 5W0P SEP C 338 SER MODIFIED RESIDUE
MODRES 5W0P SEP D 338 SER MODIFIED RESIDUE
HET TPO A 336 11
HET SEP A 338 10
HET TPO B 336 11
HET SEP B 338 10
HET SEP C 338 10
HET SEP D 338 10
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 1 SEP 4(C3 H8 N O6 P)
FORMUL 5 NAG 8(C8 H15 N O6)
HELIX 1 AA1 ASN A -159 GLY A -149 1 11
HELIX 2 AA2 SER A -123 GLY A -110 1 14
HELIX 3 AA3 THR A -102 ASN A -80 1 23
HELIX 4 AA4 LYS A -78 LEU A -70 1 9
HELIX 5 AA5 ASP A -69 GLY A -54 1 16
HELIX 6 AA6 GLY A -54 ALA A -49 1 6
HELIX 7 AA7 PHE A -47 GLN A -38 1 10
HELIX 8 AA8 ARG A -36 LYS A -26 1 11
HELIX 9 AA9 SER A -25 THR A -19 1 7
HELIX 10 AB1 THR A -19 GLY A -5 1 15
HELIX 11 AB2 PRO A 34 HIS A 65 1 32
HELIX 12 AB3 LYS A 66 ARG A 69 5 4
HELIX 13 AB4 ASN A 73 GLY A 89 1 17
HELIX 14 AB5 GLY A 89 GLY A 101 1 13
HELIX 15 AB6 PHE A 105 LYS A 141 1 37
HELIX 16 AB7 PRO A 142 PHE A 148 1 7
HELIX 17 AB8 GLY A 149 ALA A 169 1 21
HELIX 18 AB9 ALA A 169 GLY A 174 1 6
HELIX 19 AC1 ASN A 199 VAL A 210 1 12
HELIX 20 AC2 PHE A 212 GLN A 237 1 26
HELIX 21 AC3 SER A 240 HIS A 278 1 39
HELIX 22 AC4 GLY A 284 ILE A 307 1 24
HELIX 23 AC5 ASN A 310 CYS A 322 1 13
HELIX 24 AC6 GLN A 2070 GLY A 2077 1 8
HELIX 25 AC7 THR A 2102 LEU A 2112 1 11
HELIX 26 AC8 LEU A 2284 ARG A 2289 1 6
HELIX 27 AC9 ILE B -158 GLU B -150 1 9
HELIX 28 AD1 THR B -102 ASN B -80 1 23
HELIX 29 AD2 LYS B -78 LEU B -70 1 9
HELIX 30 AD3 ASP B -69 GLY B -54 1 16
HELIX 31 AD4 GLY B -54 ALA B -49 1 6
HELIX 32 AD5 THR B -46 GLN B -38 1 9
HELIX 33 AD6 ARG B -36 LYS B -26 1 11
HELIX 34 AD7 SER B -25 THR B -19 1 7
HELIX 35 AD8 THR B -19 GLY B -5 1 15
HELIX 36 AD9 PRO B 34 HIS B 65 1 32
HELIX 37 AE1 LYS B 66 ARG B 69 5 4
HELIX 38 AE2 THR B 70 LEU B 72 5 3
HELIX 39 AE3 ASN B 73 GLY B 89 1 17
HELIX 40 AE4 GLY B 89 GLY B 101 1 13
HELIX 41 AE5 PHE B 105 LYS B 141 1 37
HELIX 42 AE6 PRO B 142 PHE B 148 1 7
HELIX 43 AE7 GLY B 149 ALA B 169 1 21
HELIX 44 AE8 ALA B 169 GLY B 174 1 6
HELIX 45 AE9 ASN B 199 VAL B 210 1 12
HELIX 46 AF1 PHE B 212 GLN B 237 1 26
HELIX 47 AF2 SER B 240 HIS B 278 1 39
HELIX 48 AF3 PRO B 285 ILE B 307 1 23
HELIX 49 AF4 ASN B 310 CYS B 323 1 14
HELIX 50 AF5 ASP B 330 SER B 334 1 5
HELIX 51 AF6 GLN B 2070 GLY B 2077 1 8
HELIX 52 AF7 THR B 2102 LEU B 2112 1 11
HELIX 53 AF8 LEU B 2284 ARG B 2289 1 6
HELIX 54 AF9 ILE C -158 GLU C -150 1 9
HELIX 55 AG1 SER C -123 GLY C -110 1 14
HELIX 56 AG2 THR C -102 ASN C -80 1 23
HELIX 57 AG3 LYS C -78 LEU C -70 1 9
HELIX 58 AG4 ASP C -69 GLY C -54 1 16
HELIX 59 AG5 GLY C -54 ALA C -49 1 6
HELIX 60 AG6 PHE C -47 GLN C -38 1 10
HELIX 61 AG7 ARG C -36 LYS C -26 1 11
HELIX 62 AG8 SER C -25 THR C -19 1 7
HELIX 63 AG9 THR C -19 GLY C -5 1 15
HELIX 64 AH1 PRO C 34 HIS C 65 1 32
HELIX 65 AH2 THR C 70 LEU C 72 5 3
HELIX 66 AH3 ASN C 73 GLY C 89 1 17
HELIX 67 AH4 GLY C 89 GLY C 101 1 13
HELIX 68 AH5 PHE C 105 LYS C 141 1 37
HELIX 69 AH6 LYS C 141 PHE C 148 1 8
HELIX 70 AH7 GLY C 149 GLY C 174 1 26
HELIX 71 AH8 ASN C 199 HIS C 211 1 13
HELIX 72 AH9 PHE C 212 GLN C 237 1 26
HELIX 73 AI1 SER C 240 HIS C 278 1 39
HELIX 74 AI2 GLY C 284 ILE C 307 1 24
HELIX 75 AI3 ASN C 310 CYS C 322 1 13
HELIX 76 AI4 ASP C 330 SER C 334 1 5
HELIX 77 AI5 GLN C 2070 GLY C 2077 1 8
HELIX 78 AI6 THR C 2102 LEU C 2112 1 11
HELIX 79 AI7 LEU C 2284 ARG C 2289 1 6
HELIX 80 AI8 GLY D -84 ASN D -80 1 5
HELIX 81 AI9 LYS D -78 LEU D -70 1 9
HELIX 82 AJ1 ASP D -69 GLY D -54 1 16
HELIX 83 AJ2 GLY D -54 ALA D -49 1 6
HELIX 84 AJ3 THR D -46 GLN D -38 1 9
HELIX 85 AJ4 ARG D -36 LYS D -26 1 11
HELIX 86 AJ5 SER D -25 THR D -19 1 7
HELIX 87 AJ6 THR D -19 GLY D -5 1 15
HELIX 88 AJ7 PRO D 34 HIS D 65 1 32
HELIX 89 AJ8 LYS D 66 ARG D 69 5 4
HELIX 90 AJ9 THR D 70 LEU D 72 5 3
HELIX 91 AK1 ASN D 73 GLY D 89 1 17
HELIX 92 AK2 GLY D 89 GLY D 101 1 13
HELIX 93 AK3 PHE D 105 LYS D 141 1 37
HELIX 94 AK4 LYS D 141 PHE D 148 1 8
HELIX 95 AK5 GLY D 149 ALA D 169 1 21
HELIX 96 AK6 ALA D 169 GLY D 174 1 6
HELIX 97 AK7 ASN D 199 VAL D 210 1 12
HELIX 98 AK8 PHE D 212 GLN D 237 1 26
HELIX 99 AK9 SER D 240 HIS D 278 1 39
HELIX 100 AL1 GLY D 284 ILE D 307 1 24
HELIX 101 AL2 ASN D 310 CYS D 322 1 13
HELIX 102 AL3 GLN D 2070 GLY D 2077 1 8
HELIX 103 AL4 THR D 2102 LEU D 2112 1 11
SHEET 1 AA1 3 ARG A-147 LYS A-142 0
SHEET 2 AA1 3 TYR A-136 GLY A-133 -1 O THR A-135 N TYR A-143
SHEET 3 AA1 3 HIS A-130 LEU A-129 -1 O HIS A-130 N ILE A-134
SHEET 1 AA2 2 THR A 4 GLU A 5 0
SHEET 2 AA2 2 TYR A 10 VAL A 11 -1 O VAL A 11 N THR A 4
SHEET 1 AA3 2 TYR A 178 GLU A 181 0
SHEET 2 AA3 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181
SHEET 1 AA4 5 LYS A 339 GLU A 341 0
SHEET 2 AA4 5 ILE A2013 VAL A2017 -1 O ILE A2013 N GLU A 341
SHEET 3 AA4 5 VAL A2023 LEU A2027 -1 O ILE A2025 N LYS A2016
SHEET 4 AA4 5 VAL A2042 VAL A2048 -1 O LEU A2047 N THR A2024
SHEET 5 AA4 5 THR A2116 LEU A2121 -1 O LEU A2121 N VAL A2042
SHEET 1 AA5 5 ASP A2031 VAL A2033 0
SHEET 2 AA5 5 VAL A2171 VAL A2178 1 O ARG A2176 N TYR A2032
SHEET 3 AA5 5 CYS A2144 SER A2155 -1 N ALA A2152 O VAL A2171
SHEET 4 AA5 5 LYS A2057 TYR A2068 -1 N ARG A2067 O GLY A2145
SHEET 5 AA5 5 ASP A2083 TYR A2092 -1 O TYR A2085 N CYS A2064
SHEET 1 AA6 2 VAL A2131 LEU A2133 0
SHEET 2 AA6 2 ALA A2295 ASP A2297 -1 O LEU A2296 N MET A2132
SHEET 1 AA7 4 SER A2190 TRP A2195 0
SHEET 2 AA7 4 LEU A2204 LEU A2210 -1 O VAL A2208 N ALA A2191
SHEET 3 AA7 4 ILE A2221 ASN A2229 -1 O THR A2224 N SER A2209
SHEET 4 AA7 4 SER A2273 LEU A2281 -1 O LYS A2277 N VAL A2225
SHEET 1 AA8 5 ILE A2214 PHE A2216 0
SHEET 2 AA8 5 SER A2345 MET A2357 1 O ARG A2355 N TYR A2215
SHEET 3 AA8 5 GLY A2323 SER A2337 -1 N LEU A2334 O VAL A2348
SHEET 4 AA8 5 VAL A2235 VAL A2249 -1 N LYS A2239 O LYS A2333
SHEET 5 AA8 5 SER A2253 THR A2265 -1 O ALA A2261 N VAL A2242
SHEET 1 AA9 2 THR B 4 GLU B 5 0
SHEET 2 AA9 2 TYR B 10 VAL B 11 -1 O VAL B 11 N THR B 4
SHEET 1 AB1 2 TYR B 178 GLU B 181 0
SHEET 2 AB1 2 SER B 186 ILE B 189 -1 O SER B 186 N GLU B 181
SHEET 1 AB2 5 LYS B 339 GLU B 341 0
SHEET 2 AB2 5 ILE B2013 VAL B2017 -1 O LYS B2015 N LYS B 339
SHEET 3 AB2 5 VAL B2023 LEU B2027 -1 O LEU B2027 N PHE B2014
SHEET 4 AB2 5 VAL B2042 VAL B2048 -1 O LEU B2047 N THR B2024
SHEET 5 AB2 5 THR B2116 LEU B2121 -1 O TYR B2117 N VAL B2046
SHEET 1 AB3 5 ASP B2031 VAL B2033 0
SHEET 2 AB3 5 VAL B2171 VAL B2178 1 O ARG B2176 N TYR B2032
SHEET 3 AB3 5 CYS B2144 SER B2155 -1 N ALA B2152 O VAL B2171
SHEET 4 AB3 5 LYS B2057 TYR B2068 -1 N THR B2061 O LYS B2151
SHEET 5 AB3 5 ASP B2083 TYR B2092 -1 O TYR B2085 N CYS B2064
SHEET 1 AB4 2 VAL B2131 LEU B2133 0
SHEET 2 AB4 2 ALA B2295 ASP B2297 -1 O LEU B2296 N MET B2132
SHEET 1 AB5 4 SER B2190 TRP B2195 0
SHEET 2 AB5 4 LEU B2204 LEU B2210 -1 O VAL B2208 N ALA B2191
SHEET 3 AB5 4 ILE B2221 ASN B2229 -1 O THR B2224 N SER B2209
SHEET 4 AB5 4 SER B2273 LEU B2281 -1 O LEU B2275 N VAL B2227
SHEET 1 AB6 5 ILE B2214 PHE B2216 0
SHEET 2 AB6 5 SER B2345 MET B2357 1 O ARG B2355 N TYR B2215
SHEET 3 AB6 5 GLY B2323 SER B2337 -1 N ILE B2330 O VAL B2352
SHEET 4 AB6 5 VAL B2235 VAL B2249 -1 N LYS B2239 O LYS B2333
SHEET 5 AB6 5 SER B2253 THR B2265 -1 O GLU B2263 N VAL B2240
SHEET 1 AB7 3 ARG C-147 LYS C-142 0
SHEET 2 AB7 3 TYR C-136 GLY C-133 -1 O THR C-135 N TYR C-143
SHEET 3 AB7 3 HIS C-130 THR C-127 -1 O HIS C-130 N ILE C-134
SHEET 1 AB8 2 THR C 4 GLU C 5 0
SHEET 2 AB8 2 TYR C 10 VAL C 11 -1 O VAL C 11 N THR C 4
SHEET 1 AB9 2 TYR C 178 GLU C 181 0
SHEET 2 AB9 2 SER C 186 ILE C 189 -1 O SER C 186 N GLU C 181
SHEET 1 AC1 5 SEP C 338 GLU C 341 0
SHEET 2 AC1 5 ILE C2013 VAL C2017 -1 O ILE C2013 N GLU C 341
SHEET 3 AC1 5 VAL C2023 LEU C2027 -1 O LEU C2027 N PHE C2014
SHEET 4 AC1 5 VAL C2042 VAL C2048 -1 O LEU C2047 N THR C2024
SHEET 5 AC1 5 THR C2116 LEU C2121 -1 O TYR C2117 N VAL C2046
SHEET 1 AC2 5 ASP C2031 VAL C2033 0
SHEET 2 AC2 5 VAL C2171 VAL C2178 1 O ARG C2176 N TYR C2032
SHEET 3 AC2 5 CYS C2144 SER C2155 -1 N ALA C2152 O VAL C2171
SHEET 4 AC2 5 LYS C2057 TYR C2068 -1 N ARG C2067 O GLY C2145
SHEET 5 AC2 5 ASP C2083 TYR C2092 -1 O TYR C2085 N CYS C2064
SHEET 1 AC3 2 VAL C2131 LEU C2133 0
SHEET 2 AC3 2 ALA C2295 ASP C2297 -1 O LEU C2296 N MET C2132
SHEET 1 AC4 4 SER C2190 TRP C2195 0
SHEET 2 AC4 4 LEU C2204 LEU C2210 -1 O VAL C2208 N ALA C2191
SHEET 3 AC4 4 ILE C2221 ASN C2229 -1 O THR C2224 N SER C2209
SHEET 4 AC4 4 SER C2273 LEU C2281 -1 O LEU C2275 N VAL C2227
SHEET 1 AC5 5 ILE C2214 PHE C2216 0
SHEET 2 AC5 5 SER C2345 MET C2357 1 O ARG C2355 N TYR C2215
SHEET 3 AC5 5 GLY C2323 SER C2337 -1 N LEU C2334 O VAL C2348
SHEET 4 AC5 5 VAL C2235 VAL C2249 -1 N LYS C2239 O LYS C2333
SHEET 5 AC5 5 SER C2253 THR C2265 -1 O GLU C2263 N VAL C2240
SHEET 1 AC6 2 THR D 4 GLU D 5 0
SHEET 2 AC6 2 TYR D 10 VAL D 11 -1 O VAL D 11 N THR D 4
SHEET 1 AC7 2 TYR D 178 GLU D 181 0
SHEET 2 AC7 2 SER D 186 ILE D 189 -1 O SER D 186 N GLU D 181
SHEET 1 AC8 5 SEP D 338 GLU D 341 0
SHEET 2 AC8 5 ILE D2013 VAL D2017 -1 O ILE D2013 N GLU D 341
SHEET 3 AC8 5 VAL D2023 LEU D2027 -1 O LEU D2027 N PHE D2014
SHEET 4 AC8 5 VAL D2042 VAL D2048 -1 O LEU D2047 N THR D2024
SHEET 5 AC8 5 THR D2116 LEU D2121 -1 O TYR D2117 N VAL D2046
SHEET 1 AC9 5 ASP D2031 VAL D2033 0
SHEET 2 AC9 5 VAL D2171 VAL D2178 1 O ARG D2176 N TYR D2032
SHEET 3 AC9 5 CYS D2144 SER D2155 -1 N ALA D2152 O VAL D2171
SHEET 4 AC9 5 LYS D2057 TYR D2068 -1 N THR D2061 O LYS D2151
SHEET 5 AC9 5 ASP D2083 TYR D2092 -1 O TYR D2085 N CYS D2064
SHEET 1 AD1 2 VAL D2131 LEU D2133 0
SHEET 2 AD1 2 ALA D2295 ASP D2297 -1 O LEU D2296 N MET D2132
SHEET 1 AD2 4 SER D2190 TRP D2195 0
SHEET 2 AD2 4 LEU D2204 LEU D2210 -1 O VAL D2208 N ALA D2191
SHEET 3 AD2 4 ILE D2221 ASN D2229 -1 O THR D2224 N SER D2209
SHEET 4 AD2 4 SER D2273 LEU D2281 -1 O LEU D2275 N VAL D2227
SHEET 1 AD3 5 ILE D2214 PHE D2216 0
SHEET 2 AD3 5 SER D2345 MET D2357 1 O ARG D2355 N TYR D2215
SHEET 3 AD3 5 GLY D2323 SER D2337 -1 N ILE D2330 O VAL D2352
SHEET 4 AD3 5 VAL D2235 VAL D2249 -1 N LYS D2239 O LYS D2333
SHEET 5 AD3 5 SER D2253 THR D2265 -1 O GLU D2263 N VAL D2240
SSBOND 1 CYS A 2 CYS A 282 1555 1555 2.03
SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.03
SSBOND 3 CYS B 2 CYS B 282 1555 1555 2.03
SSBOND 4 CYS B 110 CYS B 187 1555 1555 2.03
SSBOND 5 CYS C 2 CYS C 282 1555 1555 2.03
SSBOND 6 CYS C 110 CYS C 187 1555 1555 2.03
SSBOND 7 CYS D 2 CYS D 282 1555 1555 2.03
SSBOND 8 CYS D 110 CYS D 187 1555 1555 2.03
LINK ND2 ASN A 15 C1 NAG E 1 1555 1555 1.47
LINK C ALA A 335 N TPO A 336 1555 1555 1.33
LINK C TPO A 336 N VAL A 337 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N LYS A 339 1555 1555 1.33
LINK ND2 ASN B 15 C1 NAG F 1 1555 1555 1.46
LINK C ALA B 335 N TPO B 336 1555 1555 1.33
LINK C TPO B 336 N VAL B 337 1555 1555 1.34
LINK C VAL B 337 N SEP B 338 1555 1555 1.33
LINK C SEP B 338 N LYS B 339 1555 1555 1.33
LINK ND2 ASN C 15 C1 NAG G 1 1555 1555 1.46
LINK C VAL C 337 N SEP C 338 1555 1555 1.33
LINK C SEP C 338 N LYS C 339 1555 1555 1.33
LINK ND2 ASN D 15 C1 NAG H 1 1555 1555 1.48
LINK C VAL D 337 N SEP D 338 1555 1555 1.33
LINK C SEP D 338 N LYS D 339 1555 1555 1.33
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.48
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
CISPEP 1 TYR A 2092 PRO A 2093 0 -6.57
CISPEP 2 TYR B 2092 PRO B 2093 0 -7.13
CISPEP 3 TYR C 2092 PRO C 2093 0 -8.27
CISPEP 4 TYR D 2092 PRO D 2093 0 -7.34
CRYST1 109.240 109.240 452.640 90.00 90.00 90.00 P 21 21 21 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 0.009154 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002209 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
