HEADER MEMBRANE PROTEIN 18-MAY-11 3S3X
TITLE STRUCTURE OF CHICKEN ACID-SENSING ION CHANNEL 1 AT 3.0 A RESOLUTION IN
TITLE 2 COMPLEX WITH PSALMOTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMILORIDE-SENSITIVE CATION CHANNEL 2, NEURONAL;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 26-463;
COMPND 5 SYNONYM: ACID-SENSING ION CHANNEL 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PSALMOTOXIN-1;
COMPND 9 CHAIN: D, E, F;
COMPND 10 SYNONYM: PI-TRTX-PC1A, PCTX1, PI-THERAPHOTOXIN-PC1A;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: ACCN2, ASIC1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: PSALMOPOEUS CAMBRIDGEI;
SOURCE 14 ORGANISM_COMMON: TRINIDAD CHEVRON TARANTULA;
SOURCE 15 ORGANISM_TAXID: 179874;
SOURCE 16 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS ACID-SENSING, ION CHANNEL, MEMBRANE PROTEIN, SODIUM CHANNEL, CELL
KEYWDS 2 MEMBRANE, GLYCOPROTEIN, ION TRANSPORT, MEMBRANE, SODIUM TRANSPORT,
KEYWDS 3 TRANSMEMBRANE, TRANSPORT, TRANSPORT PROTEIN, TOXIN, CYSTEINE KNOT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.P.DAWSON,J.BENZ,P.STOHLER,T.TETAZ,C.JOSEPH,S.HUBER,G.SCHMID,
AUTHOR 2 D.HUEGIN,P.PFLIMLIN,G.TRUBE,M.G.RUDOLPH,M.HENNIG,A.RUF
REVDAT 6 13-SEP-23 3S3X 1 HETSYN
REVDAT 5 29-JUL-20 3S3X 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 08-NOV-17 3S3X 1 REMARK
REVDAT 3 18-JUL-12 3S3X 1 JRNL
REVDAT 2 06-JUN-12 3S3X 1 AUTHOR
REVDAT 1 23-MAY-12 3S3X 0
JRNL AUTH R.J.DAWSON,J.BENZ,P.STOHLER,T.TETAZ,C.JOSEPH,S.HUBER,
JRNL AUTH 2 G.SCHMID,D.HUGIN,P.PFLIMLIN,G.TRUBE,M.G.RUDOLPH,M.HENNIG,
JRNL AUTH 3 A.RUF
JRNL TITL STRUCTURE OF THE ACID-SENSING ION CHANNEL 1 IN COMPLEX WITH
JRNL TITL 2 THE GATING MODIFIER PSALMOTOXIN 1.
JRNL REF NAT COMMUN V. 3 936 2012
JRNL REFN ESSN 2041-1723
JRNL PMID 22760635
JRNL DOI 10.1038/NCOMMS1917
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 55678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2823
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 29.9170 - 8.0655 0.99 2712 153 0.2298 0.2428
REMARK 3 2 8.0655 - 6.4226 0.99 2649 145 0.2104 0.2637
REMARK 3 3 6.4226 - 5.6169 0.99 2693 138 0.1966 0.2200
REMARK 3 4 5.6169 - 5.1061 1.00 2677 134 0.1685 0.2061
REMARK 3 5 5.1061 - 4.7416 1.00 2646 147 0.1482 0.2042
REMARK 3 6 4.7416 - 4.4630 0.99 2625 158 0.1511 0.1909
REMARK 3 7 4.4630 - 4.2402 0.99 2634 158 0.1566 0.1715
REMARK 3 8 4.2402 - 4.0561 0.99 2640 143 0.1771 0.2201
REMARK 3 9 4.0561 - 3.9003 0.99 2638 136 0.1909 0.2019
REMARK 3 10 3.9003 - 3.7659 0.99 2645 138 0.2135 0.2581
REMARK 3 11 3.7659 - 3.6484 0.99 2614 143 0.2333 0.2590
REMARK 3 12 3.6484 - 3.5443 0.99 2638 145 0.2395 0.2742
REMARK 3 13 3.5443 - 3.4511 0.99 2634 120 0.2562 0.2828
REMARK 3 14 3.4511 - 3.3670 0.99 2634 132 0.2810 0.2813
REMARK 3 15 3.3670 - 3.2906 0.99 2639 122 0.2838 0.3419
REMARK 3 16 3.2906 - 3.2206 1.00 2620 162 0.3195 0.3479
REMARK 3 17 3.2206 - 3.1563 0.99 2628 148 0.3444 0.3875
REMARK 3 18 3.1563 - 3.0968 0.99 2633 134 0.3702 0.3971
REMARK 3 19 3.0968 - 3.0415 0.99 2635 125 0.4110 0.4051
REMARK 3 20 3.0415 - 2.9900 0.99 2621 142 0.4470 0.5193
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 52.43
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.010
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.500
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) : 24.75240
REMARK 3 B22 (A**2) : -13.56650
REMARK 3 B33 (A**2) : -11.18600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -25.63940
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 10782
REMARK 3 ANGLE : 0.676 14544
REMARK 3 CHIRALITY : 0.040 1558
REMARK 3 PLANARITY : 0.003 1889
REMARK 3 DIHEDRAL : 11.284 4029
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 27
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 45:81)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1903 -7.0150 44.0137
REMARK 3 T TENSOR
REMARK 3 T11: 1.4397 T22: 1.8133
REMARK 3 T33: 1.4858 T12: 0.0240
REMARK 3 T13: 0.1722 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 2.1237 L22: 0.5965
REMARK 3 L33: 4.7494 L12: 1.3958
REMARK 3 L13: -6.8851 L23: -1.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.2306 S12: -0.5330 S13: 0.0154
REMARK 3 S21: 0.7041 S22: -0.4220 S23: 1.0576
REMARK 3 S31: -0.6470 S32: 0.0434 S33: 0.0574
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 82:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.6036 11.6534 13.1083
REMARK 3 T TENSOR
REMARK 3 T11: 0.8302 T22: 0.3892
REMARK 3 T33: 0.4200 T12: -0.0854
REMARK 3 T13: 0.0058 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 2.3232 L22: 3.6718
REMARK 3 L33: 2.0051 L12: 0.5100
REMARK 3 L13: 0.2709 L23: -0.0885
REMARK 3 S TENSOR
REMARK 3 S11: -0.1555 S12: 0.2203 S13: 0.3588
REMARK 3 S21: -0.6371 S22: 0.0197 S23: -0.2477
REMARK 3 S31: -0.5747 S32: 0.2925 S33: 0.1118
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 283:322)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4554 15.0881 29.5954
REMARK 3 T TENSOR
REMARK 3 T11: 0.9110 T22: 0.6073
REMARK 3 T33: 0.6993 T12: 0.0686
REMARK 3 T13: 0.0508 T23: -0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 8.0046 L22: 6.6440
REMARK 3 L33: 0.0908 L12: 6.3606
REMARK 3 L13: 0.2986 L23: -0.1065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: -0.2032 S13: 1.2173
REMARK 3 S21: 0.3378 S22: 0.0465 S23: 1.2040
REMARK 3 S31: -0.1064 S32: -0.4781 S33: -0.0739
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 323:448 OR RESSEQ 600
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0874 4.3338 22.2250
REMARK 3 T TENSOR
REMARK 3 T11: 0.7109 T22: 0.4288
REMARK 3 T33: 0.3683 T12: -0.0604
REMARK 3 T13: -0.0582 T23: 0.0857
REMARK 3 L TENSOR
REMARK 3 L11: 1.9916 L22: 2.6231
REMARK 3 L33: 1.2545 L12: -0.2261
REMARK 3 L13: -0.0931 L23: 0.8521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: -0.1059 S13: 0.0260
REMARK 3 S21: 0.1786 S22: -0.0328 S23: 0.3949
REMARK 3 S31: -0.0043 S32: -0.2663 S33: -0.0202
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 49:81)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9656 -12.9952 26.7771
REMARK 3 T TENSOR
REMARK 3 T11: 1.1795 T22: 1.3122
REMARK 3 T33: 2.0221 T12: -0.2448
REMARK 3 T13: 0.1964 T23: -0.1695
REMARK 3 L TENSOR
REMARK 3 L11: 9.0546 L22: 3.1987
REMARK 3 L33: 1.7572 L12: -5.4428
REMARK 3 L13: -3.9899 L23: 2.2194
REMARK 3 S TENSOR
REMARK 3 S11: -0.4721 S12: 1.7470 S13: -1.6671
REMARK 3 S21: 0.3856 S22: -0.4936 S23: 1.7342
REMARK 3 S31: 0.0871 S32: -1.1839 S33: 1.0635
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 82:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1773 -25.4024 1.4445
REMARK 3 T TENSOR
REMARK 3 T11: 0.9169 T22: 0.5114
REMARK 3 T33: 0.5668 T12: 0.0738
REMARK 3 T13: -0.0525 T23: -0.1210
REMARK 3 L TENSOR
REMARK 3 L11: 2.1078 L22: 2.8891
REMARK 3 L33: 4.9461 L12: 0.7018
REMARK 3 L13: -0.1791 L23: -0.7717
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.5838 S13: -0.2421
REMARK 3 S21: -0.8808 S22: 0.1445 S23: -0.4659
REMARK 3 S31: 0.7820 S32: 0.1373 S33: -0.0692
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 235:426 OR RESSEQ 600
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3320 -19.9981 8.6139
REMARK 3 T TENSOR
REMARK 3 T11: 0.7404 T22: 0.3680
REMARK 3 T33: 0.4640 T12: -0.0258
REMARK 3 T13: -0.0978 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 2.0467 L22: 2.1720
REMARK 3 L33: 2.2665 L12: -0.4826
REMARK 3 L13: 1.1341 L23: -0.0578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: 0.2471 S13: -0.1262
REMARK 3 S21: -0.5433 S22: -0.0089 S23: 0.4883
REMARK 3 S31: -0.0398 S32: -0.1677 S33: -0.0775
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 427:449)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1584 -19.1672 29.6429
REMARK 3 T TENSOR
REMARK 3 T11: 2.1585 T22: 2.8276
REMARK 3 T33: 2.0573 T12: -0.7309
REMARK 3 T13: 0.5227 T23: -0.1577
REMARK 3 L TENSOR
REMARK 3 L11: 1.1103 L22: 0.3890
REMARK 3 L33: 0.4842 L12: 0.6130
REMARK 3 L13: -0.1191 L23: -0.2161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0557 S12: 0.0318 S13: -0.0003
REMARK 3 S21: 0.2497 S22: 0.3843 S23: -0.3704
REMARK 3 S31: -0.8341 S32: -0.5952 S33: -0.4372
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 50:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1371 -25.7490 41.0988
REMARK 3 T TENSOR
REMARK 3 T11: 1.0999 T22: 2.4955
REMARK 3 T33: 2.6520 T12: -0.4584
REMARK 3 T13: 0.2434 T23: 0.1633
REMARK 3 L TENSOR
REMARK 3 L11: 5.2169 L22: 0.6599
REMARK 3 L33: 1.0786 L12: 1.7957
REMARK 3 L13: 0.6141 L23: -0.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.3386 S12: 0.2434 S13: -0.4474
REMARK 3 S21: 0.7736 S22: -1.1433 S23: 1.7472
REMARK 3 S31: -0.4005 S32: -1.2398 S33: 1.6564
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 72:396 OR RESSEQ 600 OR
REMARK 3 ORIGIN FOR THE GROUP (A): 77.6850 -15.9303 37.8998
REMARK 3 T TENSOR
REMARK 3 T11: 0.4207 T22: 0.3899
REMARK 3 T33: 0.3537 T12: -0.0549
REMARK 3 T13: -0.0496 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.3928 L22: 2.6216
REMARK 3 L33: 2.1822 L12: -1.0043
REMARK 3 L13: 0.6191 L23: -0.2159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0519 S12: -0.1989 S13: -0.1049
REMARK 3 S21: 0.1818 S22: 0.0671 S23: -0.0677
REMARK 3 S31: 0.1551 S32: 0.0508 S33: -0.1443
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 397:426)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1418 -6.4626 32.2900
REMARK 3 T TENSOR
REMARK 3 T11: 0.5149 T22: 0.5186
REMARK 3 T33: 0.3439 T12: -0.0683
REMARK 3 T13: -0.0631 T23: 0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 2.1258 L22: 3.8737
REMARK 3 L33: 1.9451 L12: 2.2609
REMARK 3 L13: -1.2080 L23: -0.7139
REMARK 3 S TENSOR
REMARK 3 S11: -0.2647 S12: -0.1320 S13: -0.1345
REMARK 3 S21: -0.2311 S22: 0.2238 S23: 0.3752
REMARK 3 S31: 0.0649 S32: -0.3519 S33: -0.0550
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 427:449)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2327 -17.7999 46.2433
REMARK 3 T TENSOR
REMARK 3 T11: 1.0715 T22: 2.1431
REMARK 3 T33: 2.3728 T12: -0.3346
REMARK 3 T13: 0.2375 T23: 0.4931
REMARK 3 L TENSOR
REMARK 3 L11: 1.7385 L22: 4.3655
REMARK 3 L33: 5.9198 L12: 1.3020
REMARK 3 L13: -2.5353 L23: 0.8609
REMARK 3 S TENSOR
REMARK 3 S11: 0.8260 S12: -0.6069 S13: 0.1040
REMARK 3 S21: -0.2634 S22: 1.2023 S23: 2.0828
REMARK 3 S31: 0.0637 S32: -1.3544 S33: -1.8764
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 2:6)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.6175 29.3773 42.5247
REMARK 3 T TENSOR
REMARK 3 T11: 1.7880 T22: 0.6193
REMARK 3 T33: 0.9362 T12: -0.6330
REMARK 3 T13: -0.5530 T23: -0.3150
REMARK 3 L TENSOR
REMARK 3 L11: 0.7327 L22: 8.7757
REMARK 3 L33: 3.4841 L12: -0.6202
REMARK 3 L13: -1.5955 L23: 1.0867
REMARK 3 S TENSOR
REMARK 3 S11: 0.6156 S12: -1.8670 S13: 1.5590
REMARK 3 S21: 1.6424 S22: -0.7051 S23: -0.6085
REMARK 3 S31: -0.3280 S32: 0.0515 S33: 0.0114
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 7:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 80.2529 23.2340 40.7776
REMARK 3 T TENSOR
REMARK 3 T11: 1.4972 T22: 0.7874
REMARK 3 T33: 0.7778 T12: -0.2992
REMARK 3 T13: -0.3453 T23: -0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 2.0044 L22: 2.3933
REMARK 3 L33: 6.5328 L12: -1.8654
REMARK 3 L13: 0.3430 L23: 2.5716
REMARK 3 S TENSOR
REMARK 3 S11: -0.1452 S12: -0.5483 S13: 0.6795
REMARK 3 S21: 1.0511 S22: -0.0585 S23: -0.9513
REMARK 3 S31: -0.3701 S32: 0.5840 S33: 0.0677
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 17:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.8130 22.0869 44.7708
REMARK 3 T TENSOR
REMARK 3 T11: 1.8267 T22: 0.9792
REMARK 3 T33: 0.7229 T12: -0.2287
REMARK 3 T13: -0.3015 T23: -0.1976
REMARK 3 L TENSOR
REMARK 3 L11: 7.7361 L22: 2.0066
REMARK 3 L33: 2.0056 L12: 4.8743
REMARK 3 L13: 5.2969 L23: 9.0807
REMARK 3 S TENSOR
REMARK 3 S11: 0.1653 S12: -1.7351 S13: 0.9736
REMARK 3 S21: 1.3102 S22: -0.1270 S23: -0.0922
REMARK 3 S31: -0.3074 S32: 0.0916 S33: -0.0142
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 25:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 77.2573 14.5200 34.0502
REMARK 3 T TENSOR
REMARK 3 T11: 0.7279 T22: 0.5390
REMARK 3 T33: 0.6233 T12: -0.1506
REMARK 3 T13: 0.0048 T23: 0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 9.3896 L22: 2.0008
REMARK 3 L33: 1.9988 L12: 1.9970
REMARK 3 L13: -2.1068 L23: 4.6903
REMARK 3 S TENSOR
REMARK 3 S11: 0.2913 S12: -0.1103 S13: -0.3611
REMARK 3 S21: 0.8671 S22: -0.1577 S23: 0.0354
REMARK 3 S31: 0.4262 S32: 0.0344 S33: -0.0040
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 32:38)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.0559 19.3606 43.9996
REMARK 3 T TENSOR
REMARK 3 T11: 1.7433 T22: 0.9222
REMARK 3 T33: 0.6456 T12: -0.1884
REMARK 3 T13: 0.0582 T23: -0.1481
REMARK 3 L TENSOR
REMARK 3 L11: 6.2282 L22: 2.0036
REMARK 3 L33: 2.0041 L12: -1.6546
REMARK 3 L13: 5.3941 L23: 6.0828
REMARK 3 S TENSOR
REMARK 3 S11: 0.3836 S12: -1.9997 S13: -0.3560
REMARK 3 S21: 2.4332 S22: -1.1981 S23: 0.9142
REMARK 3 S31: 1.2766 S32: -1.1419 S33: 0.8482
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 2:11)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9406 -7.9102 -20.1316
REMARK 3 T TENSOR
REMARK 3 T11: 2.2741 T22: 1.1265
REMARK 3 T33: 0.5155 T12: 0.2306
REMARK 3 T13: -0.0722 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 4.6251 L22: 3.2910
REMARK 3 L33: 4.2725 L12: 2.9896
REMARK 3 L13: -2.2526 L23: -3.5262
REMARK 3 S TENSOR
REMARK 3 S11: 0.5351 S12: 1.2950 S13: 0.2347
REMARK 3 S21: -1.6701 S22: 0.0069 S23: 0.0038
REMARK 3 S31: -0.5157 S32: 0.0487 S33: -0.7670
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 12:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6615 0.0251 -20.5418
REMARK 3 T TENSOR
REMARK 3 T11: 2.3257 T22: 1.1792
REMARK 3 T33: 0.7963 T12: 0.1278
REMARK 3 T13: -0.1490 T23: 0.2646
REMARK 3 L TENSOR
REMARK 3 L11: 2.0021 L22: 4.2980
REMARK 3 L33: 3.4293 L12: -3.2593
REMARK 3 L13: -3.5241 L23: 0.2756
REMARK 3 S TENSOR
REMARK 3 S11: 0.1019 S12: 1.6463 S13: 0.5093
REMARK 3 S21: -1.6506 S22: -0.5151 S23: -0.2328
REMARK 3 S31: 0.0253 S32: 0.6080 S33: 0.4275
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 17:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3636 -3.6953 -16.6916
REMARK 3 T TENSOR
REMARK 3 T11: 1.9832 T22: 0.9201
REMARK 3 T33: 0.5935 T12: -0.2679
REMARK 3 T13: -0.1678 T23: 0.1535
REMARK 3 L TENSOR
REMARK 3 L11: 4.9057 L22: 9.1880
REMARK 3 L33: 2.0021 L12: -6.3444
REMARK 3 L13: 7.5388 L23: 1.9975
REMARK 3 S TENSOR
REMARK 3 S11: 0.2178 S12: 1.3422 S13: 0.4481
REMARK 3 S21: -2.0379 S22: -0.7165 S23: 0.7772
REMARK 3 S31: -0.2382 S32: 0.0944 S33: 0.5289
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 25:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7826 -6.2050 -7.8303
REMARK 3 T TENSOR
REMARK 3 T11: 1.5499 T22: 0.7751
REMARK 3 T33: 0.5376 T12: -0.1309
REMARK 3 T13: -0.1471 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 8.7110 L22: 8.6188
REMARK 3 L33: 1.9996 L12: 0.6958
REMARK 3 L13: -5.9703 L23: 3.0305
REMARK 3 S TENSOR
REMARK 3 S11: 0.2698 S12: 0.6113 S13: 0.2255
REMARK 3 S21: -0.7222 S22: -0.2102 S23: -0.2518
REMARK 3 S31: -0.2998 S32: 0.1253 S33: -0.0412
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 32:38)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1594 -4.7619 -12.6746
REMARK 3 T TENSOR
REMARK 3 T11: 1.5837 T22: 0.7467
REMARK 3 T33: 0.7233 T12: 0.1549
REMARK 3 T13: -0.4607 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 5.1471 L22: 8.0069
REMARK 3 L33: 2.0020 L12: 1.1089
REMARK 3 L13: 8.3919 L23: 0.1854
REMARK 3 S TENSOR
REMARK 3 S11: 0.3135 S12: 0.7766 S13: 1.0442
REMARK 3 S21: -0.8706 S22: -0.3324 S23: 0.6769
REMARK 3 S31: -1.6911 S32: -1.5098 S33: 0.0937
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 2:6)
REMARK 3 ORIGIN FOR THE GROUP (A): 84.5914 -48.0940 37.5074
REMARK 3 T TENSOR
REMARK 3 T11: 1.3658 T22: 0.6032
REMARK 3 T33: 1.2340 T12: 0.1146
REMARK 3 T13: -0.4505 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.0931 L22: 6.0648
REMARK 3 L33: 6.6309 L12: 0.1592
REMARK 3 L13: 2.5665 L23: -1.5188
REMARK 3 S TENSOR
REMARK 3 S11: -0.2772 S12: 0.2564 S13: -2.7361
REMARK 3 S21: -0.1591 S22: 0.1005 S23: 0.1205
REMARK 3 S31: 1.6099 S32: 0.4087 S33: 0.1664
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 7:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.3493 -44.1647 31.3437
REMARK 3 T TENSOR
REMARK 3 T11: 1.4065 T22: 0.5897
REMARK 3 T33: 1.0478 T12: 0.2595
REMARK 3 T13: -0.3618 T23: -0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 4.7937 L22: 3.3823
REMARK 3 L33: 8.1284 L12: 0.8694
REMARK 3 L13: -4.6406 L23: 2.5822
REMARK 3 S TENSOR
REMARK 3 S11: 0.2441 S12: -0.0066 S13: -0.4806
REMARK 3 S21: -0.8226 S22: 0.7348 S23: -0.2827
REMARK 3 S31: 0.8198 S32: 0.4329 S33: -1.0009
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 17:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1292 -46.1461 32.9799
REMARK 3 T TENSOR
REMARK 3 T11: 1.2254 T22: 0.5514
REMARK 3 T33: 1.3124 T12: 0.1970
REMARK 3 T13: -0.5040 T23: -0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 2.0092 L22: 2.0045
REMARK 3 L33: 7.5927 L12: -9.5461
REMARK 3 L13: 3.4605 L23: -4.7018
REMARK 3 S TENSOR
REMARK 3 S11: 0.1022 S12: -0.6930 S13: -1.4114
REMARK 3 S21: -0.8667 S22: 0.4306 S23: -0.7368
REMARK 3 S31: 1.6764 S32: -0.2849 S33: -0.5149
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 25:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 81.8054 -33.5413 28.3990
REMARK 3 T TENSOR
REMARK 3 T11: 0.8621 T22: 0.5836
REMARK 3 T33: 0.7331 T12: 0.0810
REMARK 3 T13: -0.0006 T23: -0.1322
REMARK 3 L TENSOR
REMARK 3 L11: 2.0068 L22: 1.9996
REMARK 3 L33: 2.0051 L12: 1.9945
REMARK 3 L13: 6.1088 L23: -5.4962
REMARK 3 S TENSOR
REMARK 3 S11: 0.3678 S12: 0.6751 S13: -0.3220
REMARK 3 S21: -1.1548 S22: 0.0040 S23: -0.1960
REMARK 3 S31: -0.3126 S32: 0.2096 S33: -0.2971
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 32:38)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1713 -43.6322 33.3770
REMARK 3 T TENSOR
REMARK 3 T11: 1.0970 T22: 0.4955
REMARK 3 T33: 0.9074 T12: -0.2080
REMARK 3 T13: -0.2542 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 0.7205 L22: 2.0030
REMARK 3 L33: 2.0116 L12: -3.3337
REMARK 3 L13: 0.4746 L23: -2.7759
REMARK 3 S TENSOR
REMARK 3 S11: -0.2629 S12: 0.8239 S13: -1.4536
REMARK 3 S21: -0.9062 S22: 0.6738 S23: 0.9272
REMARK 3 S31: 1.1742 S32: -0.8329 S33: -0.3883
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 71:140 OR RESSEQ
REMARK 3 142:153 OR RESSEQ 155:183 OR RESSEQ 185:
REMARK 3 200 OR RESSEQ 205:291 OR RESSEQ 300:331
REMARK 3 OR RESSEQ 333:422 OR RESSEQ 600:600 OR
REMARK 3 RESSEQ 700:700 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 71:140 OR RESSEQ
REMARK 3 142:153 OR RESSEQ 155:183 OR RESSEQ 185:
REMARK 3 200 OR RESSEQ 205:291 OR RESSEQ 300:331
REMARK 3 OR RESSEQ 333:422 OR RESSEQ 600:600 OR
REMARK 3 RESSEQ 700:700 )
REMARK 3 ATOM PAIRS NUMBER : 2754
REMARK 3 RMSD : 0.053
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 71:140 OR RESSEQ
REMARK 3 142:153 OR RESSEQ 155:183 OR RESSEQ 185:
REMARK 3 200 OR RESSEQ 205:291 OR RESSEQ 300:331
REMARK 3 OR RESSEQ 333:422 OR RESSEQ 600:600 OR
REMARK 3 RESSEQ 700:700 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 71:140 OR RESSEQ
REMARK 3 142:153 OR RESSEQ 155:183 OR RESSEQ 185:
REMARK 3 200 OR RESSEQ 205:291 OR RESSEQ 300:331
REMARK 3 OR RESSEQ 333:422 OR RESSEQ 600:600 OR
REMARK 3 RESSEQ 700:700 )
REMARK 3 ATOM PAIRS NUMBER : 2754
REMARK 3 RMSD : 0.072
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 2:27 OR RESSEQ 29:38
REMARK 3 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 2:27 OR RESSEQ 29:38
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 288
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 2:27 OR RESSEQ 29:38
REMARK 3 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 2:27 OR RESSEQ 29:38
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 288
REMARK 3 RMSD : 0.005
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3S3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065729.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION MAY 10
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55842
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.380
REMARK 200 R MERGE (I) : 0.10830
REMARK 200 R SYM (I) : 0.10830
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.53
REMARK 200 R MERGE FOR SHELL (I) : 0.72500
REMARK 200 R SYM FOR SHELL (I) : 0.72500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.060
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: 3S3W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 5.5, 3 %
REMARK 280 GLYCEROL, 3% 1,6-HEXANEDIOL, 11 % PEG 6000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 286K
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 116.19800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.19800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.72100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 TYR A 7
REMARK 465 TYR A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 SER A 17
REMARK 465 LEU A 18
REMARK 465 VAL A 19
REMARK 465 PRO A 20
REMARK 465 ARG A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 HIS A 24
REMARK 465 MET A 25
REMARK 465 SER A 26
REMARK 465 THR A 27
REMARK 465 LEU A 28
REMARK 465 HIS A 29
REMARK 465 GLY A 30
REMARK 465 ILE A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 ILE A 34
REMARK 465 PHE A 35
REMARK 465 SER A 36
REMARK 465 TYR A 37
REMARK 465 GLU A 38
REMARK 465 ARG A 39
REMARK 465 LEU A 40
REMARK 465 SER A 41
REMARK 465 LEU A 42
REMARK 465 LYS A 43
REMARK 465 ARG A 44
REMARK 465 ALA A 293
REMARK 465 THR A 294
REMARK 465 THR A 295
REMARK 465 VAL A 449
REMARK 465 LEU A 450
REMARK 465 GLU A 451
REMARK 465 LEU A 452
REMARK 465 PHE A 453
REMARK 465 ASP A 454
REMARK 465 TYR A 455
REMARK 465 ALA A 456
REMARK 465 TYR A 457
REMARK 465 GLU A 458
REMARK 465 VAL A 459
REMARK 465 ILE A 460
REMARK 465 LYS A 461
REMARK 465 HIS A 462
REMARK 465 ARG A 463
REMARK 465 MET B 5
REMARK 465 SER B 6
REMARK 465 TYR B 7
REMARK 465 TYR B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 GLY B 15
REMARK 465 ALA B 16
REMARK 465 SER B 17
REMARK 465 LEU B 18
REMARK 465 VAL B 19
REMARK 465 PRO B 20
REMARK 465 ARG B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 HIS B 24
REMARK 465 MET B 25
REMARK 465 SER B 26
REMARK 465 THR B 27
REMARK 465 LEU B 28
REMARK 465 HIS B 29
REMARK 465 GLY B 30
REMARK 465 ILE B 31
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 ILE B 34
REMARK 465 PHE B 35
REMARK 465 SER B 36
REMARK 465 TYR B 37
REMARK 465 GLU B 38
REMARK 465 ARG B 39
REMARK 465 LEU B 40
REMARK 465 SER B 41
REMARK 465 LEU B 42
REMARK 465 LYS B 43
REMARK 465 ARG B 44
REMARK 465 VAL B 45
REMARK 465 VAL B 46
REMARK 465 TRP B 47
REMARK 465 ALA B 48
REMARK 465 GLY B 296
REMARK 465 ASP B 297
REMARK 465 SER B 298
REMARK 465 GLY B 443
REMARK 465 ALA B 444
REMARK 465 SER B 445
REMARK 465 ILE B 446
REMARK 465 LEU B 447
REMARK 465 THR B 448
REMARK 465 VAL B 449
REMARK 465 LEU B 450
REMARK 465 GLU B 451
REMARK 465 LEU B 452
REMARK 465 PHE B 453
REMARK 465 ASP B 454
REMARK 465 TYR B 455
REMARK 465 ALA B 456
REMARK 465 TYR B 457
REMARK 465 GLU B 458
REMARK 465 VAL B 459
REMARK 465 ILE B 460
REMARK 465 LYS B 461
REMARK 465 HIS B 462
REMARK 465 ARG B 463
REMARK 465 MET C 5
REMARK 465 SER C 6
REMARK 465 TYR C 7
REMARK 465 TYR C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 GLY C 15
REMARK 465 ALA C 16
REMARK 465 SER C 17
REMARK 465 LEU C 18
REMARK 465 VAL C 19
REMARK 465 PRO C 20
REMARK 465 ARG C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 HIS C 24
REMARK 465 MET C 25
REMARK 465 SER C 26
REMARK 465 THR C 27
REMARK 465 LEU C 28
REMARK 465 HIS C 29
REMARK 465 GLY C 30
REMARK 465 ILE C 31
REMARK 465 SER C 32
REMARK 465 HIS C 33
REMARK 465 ILE C 34
REMARK 465 PHE C 35
REMARK 465 SER C 36
REMARK 465 TYR C 37
REMARK 465 GLU C 38
REMARK 465 ARG C 39
REMARK 465 LEU C 40
REMARK 465 SER C 41
REMARK 465 LEU C 42
REMARK 465 LYS C 43
REMARK 465 ARG C 44
REMARK 465 VAL C 45
REMARK 465 VAL C 46
REMARK 465 TRP C 47
REMARK 465 ALA C 48
REMARK 465 LEU C 49
REMARK 465 THR C 294
REMARK 465 THR C 295
REMARK 465 GLY C 296
REMARK 465 ASP C 297
REMARK 465 LEU C 450
REMARK 465 GLU C 451
REMARK 465 LEU C 452
REMARK 465 PHE C 453
REMARK 465 ASP C 454
REMARK 465 TYR C 455
REMARK 465 ALA C 456
REMARK 465 TYR C 457
REMARK 465 GLU C 458
REMARK 465 VAL C 459
REMARK 465 ILE C 460
REMARK 465 LYS C 461
REMARK 465 HIS C 462
REMARK 465 ARG C 463
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 CB CYS B 94 SG CYS B 195 2.08
REMARK 500 O ILE C 442 OG SER C 445 2.10
REMARK 500 CB CYS A 94 SG CYS A 195 2.11
REMARK 500 CB CYS C 94 SG CYS C 195 2.11
REMARK 500 O SER C 445 OG1 THR C 448 2.14
REMARK 500 ND2 ASN B 394 C2 NAG B 700 2.15
REMARK 500 ND2 ASN C 394 C2 NAG C 700 2.15
REMARK 500 ND2 ASN A 394 C2 NAG A 700 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 357 CG ASN A 357 OD1 -0.154
REMARK 500 ASN A 357 CG ASN A 357 ND2 -0.185
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 ARG A 146 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 280 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 316 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 146 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 146 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 280 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 316 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 316 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG C 146 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG C 146 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG C 146 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG C 167 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG C 167 NE - CZ - NH1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG C 167 NE - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG C 280 NE - CZ - NH1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG C 280 NE - CZ - NH2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG C 316 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG C 316 NE - CZ - NH1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG C 316 NE - CZ - NH2 ANGL. DEV. = 7.5 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 79 108.38 -163.10
REMARK 500 ASN A 121 1.24 -68.48
REMARK 500 ASP A 203 -0.56 114.28
REMARK 500 GLN A 226 66.14 61.32
REMARK 500 ASP A 254 38.92 -96.08
REMARK 500 LEU A 258 64.42 -101.70
REMARK 500 PRO A 330 -159.18 -71.82
REMARK 500 ASP A 332 55.27 -141.94
REMARK 500 CYS A 344 -58.68 -142.88
REMARK 500 ALA A 413 -72.00 -48.80
REMARK 500 PHE B 70 6.26 -61.17
REMARK 500 ASP B 79 108.33 -163.19
REMARK 500 ASN B 121 1.51 -68.78
REMARK 500 ASP B 203 11.15 86.47
REMARK 500 GLN B 226 66.28 60.87
REMARK 500 ASP B 254 39.09 -95.79
REMARK 500 LEU B 258 64.49 -101.74
REMARK 500 PRO B 330 -159.58 -71.72
REMARK 500 ASP B 332 51.31 -141.73
REMARK 500 CYS B 344 -59.34 -143.19
REMARK 500 ALA B 413 -71.93 -49.11
REMARK 500 ASP C 79 108.24 -163.35
REMARK 500 ASN C 121 1.46 -68.78
REMARK 500 ASP C 203 2.84 110.77
REMARK 500 GLN C 226 66.28 61.00
REMARK 500 ASP C 254 38.72 -95.25
REMARK 500 LEU C 258 64.45 -101.63
REMARK 500 PRO C 330 -159.76 -71.34
REMARK 500 CYS C 344 -59.58 -142.78
REMARK 500 ALA C 413 -71.65 -48.74
REMARK 500 ASN D 12 13.96 59.18
REMARK 500 ARG D 13 57.69 -145.68
REMARK 500 ASN E 12 13.88 59.46
REMARK 500 ARG E 13 57.33 -145.66
REMARK 500 ASN F 12 14.18 59.32
REMARK 500 ARG F 13 57.61 -145.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 286 PRO A 287 79.08
REMARK 500 PRO B 286 PRO B 287 34.90
REMARK 500 PRO C 286 PRO C 287 35.07
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 K A 2 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 260 OD2
REMARK 620 2 GLU A 314 OE1 168.6
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S3W RELATED DB: PDB
DBREF 3S3X A 26 463 UNP Q1XA76 ACCN2_CHICK 26 463
DBREF 3S3X B 26 463 UNP Q1XA76 ACCN2_CHICK 26 463
DBREF 3S3X C 26 463 UNP Q1XA76 ACCN2_CHICK 26 463
DBREF 3S3X D 2 38 UNP P60514 TXP1_PSACA 2 38
DBREF 3S3X E 2 38 UNP P60514 TXP1_PSACA 2 38
DBREF 3S3X F 2 38 UNP P60514 TXP1_PSACA 2 38
SEQADV 3S3X MET A 5 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER A 6 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR A 7 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR A 8 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 9 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 10 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 11 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 12 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 13 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 14 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY A 15 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ALA A 16 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER A 17 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X LEU A 18 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X VAL A 19 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X PRO A 20 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ARG A 21 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY A 22 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER A 23 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS A 24 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X MET A 25 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X MET B 5 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER B 6 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR B 7 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR B 8 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 9 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 10 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 11 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 12 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 13 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 14 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY B 15 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ALA B 16 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER B 17 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X LEU B 18 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X VAL B 19 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X PRO B 20 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ARG B 21 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY B 22 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER B 23 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS B 24 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X MET B 25 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X MET C 5 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER C 6 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR C 7 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X TYR C 8 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 9 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 10 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 11 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 12 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 13 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 14 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY C 15 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ALA C 16 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER C 17 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X LEU C 18 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X VAL C 19 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X PRO C 20 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X ARG C 21 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X GLY C 22 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X SER C 23 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X HIS C 24 UNP Q1XA76 EXPRESSION TAG
SEQADV 3S3X MET C 25 UNP Q1XA76 EXPRESSION TAG
SEQRES 1 A 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS GLY ALA SER
SEQRES 2 A 459 LEU VAL PRO ARG GLY SER HIS MET SER THR LEU HIS GLY
SEQRES 3 A 459 ILE SER HIS ILE PHE SER TYR GLU ARG LEU SER LEU LYS
SEQRES 4 A 459 ARG VAL VAL TRP ALA LEU CYS PHE MET GLY SER LEU ALA
SEQRES 5 A 459 LEU LEU ALA LEU VAL CYS THR ASN ARG ILE GLN TYR TYR
SEQRES 6 A 459 PHE LEU TYR PRO HIS VAL THR LYS LEU ASP GLU VAL ALA
SEQRES 7 A 459 ALA THR ARG LEU THR PHE PRO ALA VAL THR PHE CYS ASN
SEQRES 8 A 459 LEU ASN GLU PHE ARG PHE SER ARG VAL THR LYS ASN ASP
SEQRES 9 A 459 LEU TYR HIS ALA GLY GLU LEU LEU ALA LEU LEU ASN ASN
SEQRES 10 A 459 ARG TYR GLU ILE PRO ASP THR GLN THR ALA ASP GLU LYS
SEQRES 11 A 459 GLN LEU GLU ILE LEU GLN ASP LYS ALA ASN PHE ARG ASN
SEQRES 12 A 459 PHE LYS PRO LYS PRO PHE ASN MET LEU GLU PHE TYR ASP
SEQRES 13 A 459 ARG ALA GLY HIS ASP ILE ARG GLU MET LEU LEU SER CYS
SEQRES 14 A 459 PHE PHE ARG GLY GLU GLN CYS SER PRO GLU ASP PHE LYS
SEQRES 15 A 459 VAL VAL PHE THR ARG TYR GLY LYS CYS TYR THR PHE ASN
SEQRES 16 A 459 ALA GLY GLN ASP GLY LYS PRO ARG LEU ILE THR MET LYS
SEQRES 17 A 459 GLY GLY THR GLY ASN GLY LEU GLU ILE MET LEU ASP ILE
SEQRES 18 A 459 GLN GLN ASP GLU TYR LEU PRO VAL TRP GLY GLU THR ASP
SEQRES 19 A 459 GLU THR SER PHE GLU ALA GLY ILE LYS VAL GLN ILE HIS
SEQRES 20 A 459 SER GLN ASP GLU PRO PRO LEU ILE ASP GLN LEU GLY PHE
SEQRES 21 A 459 GLY VAL ALA PRO GLY PHE GLN THR PHE VAL SER CYS GLN
SEQRES 22 A 459 GLU GLN ARG LEU ILE TYR LEU PRO PRO PRO TRP GLY ASP
SEQRES 23 A 459 CYS LYS ALA THR THR GLY ASP SER GLU PHE TYR ASP THR
SEQRES 24 A 459 TYR SER ILE THR ALA CYS ARG ILE ASP CYS GLU THR ARG
SEQRES 25 A 459 TYR LEU VAL GLU ASN CYS ASN CYS ARG MET VAL HIS MET
SEQRES 26 A 459 PRO GLY ASP ALA PRO TYR CYS THR PRO GLU GLN TYR LYS
SEQRES 27 A 459 GLU CYS ALA ASP PRO ALA LEU ASP PHE LEU VAL GLU LYS
SEQRES 28 A 459 ASP ASN GLU TYR CYS VAL CYS GLU MET PRO CYS ASN VAL
SEQRES 29 A 459 THR ARG TYR GLY LYS GLU LEU SER MET VAL LYS ILE PRO
SEQRES 30 A 459 SER LYS ALA SER ALA LYS TYR LEU ALA LYS LYS TYR ASN
SEQRES 31 A 459 LYS SER GLU GLN TYR ILE GLY GLU ASN ILE LEU VAL LEU
SEQRES 32 A 459 ASP ILE PHE PHE GLU ALA LEU ASN TYR GLU THR ILE GLU
SEQRES 33 A 459 GLN LYS LYS ALA TYR GLU VAL ALA GLY LEU LEU GLY ASP
SEQRES 34 A 459 ILE GLY GLY GLN MET GLY LEU PHE ILE GLY ALA SER ILE
SEQRES 35 A 459 LEU THR VAL LEU GLU LEU PHE ASP TYR ALA TYR GLU VAL
SEQRES 36 A 459 ILE LYS HIS ARG
SEQRES 1 B 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS GLY ALA SER
SEQRES 2 B 459 LEU VAL PRO ARG GLY SER HIS MET SER THR LEU HIS GLY
SEQRES 3 B 459 ILE SER HIS ILE PHE SER TYR GLU ARG LEU SER LEU LYS
SEQRES 4 B 459 ARG VAL VAL TRP ALA LEU CYS PHE MET GLY SER LEU ALA
SEQRES 5 B 459 LEU LEU ALA LEU VAL CYS THR ASN ARG ILE GLN TYR TYR
SEQRES 6 B 459 PHE LEU TYR PRO HIS VAL THR LYS LEU ASP GLU VAL ALA
SEQRES 7 B 459 ALA THR ARG LEU THR PHE PRO ALA VAL THR PHE CYS ASN
SEQRES 8 B 459 LEU ASN GLU PHE ARG PHE SER ARG VAL THR LYS ASN ASP
SEQRES 9 B 459 LEU TYR HIS ALA GLY GLU LEU LEU ALA LEU LEU ASN ASN
SEQRES 10 B 459 ARG TYR GLU ILE PRO ASP THR GLN THR ALA ASP GLU LYS
SEQRES 11 B 459 GLN LEU GLU ILE LEU GLN ASP LYS ALA ASN PHE ARG ASN
SEQRES 12 B 459 PHE LYS PRO LYS PRO PHE ASN MET LEU GLU PHE TYR ASP
SEQRES 13 B 459 ARG ALA GLY HIS ASP ILE ARG GLU MET LEU LEU SER CYS
SEQRES 14 B 459 PHE PHE ARG GLY GLU GLN CYS SER PRO GLU ASP PHE LYS
SEQRES 15 B 459 VAL VAL PHE THR ARG TYR GLY LYS CYS TYR THR PHE ASN
SEQRES 16 B 459 ALA GLY GLN ASP GLY LYS PRO ARG LEU ILE THR MET LYS
SEQRES 17 B 459 GLY GLY THR GLY ASN GLY LEU GLU ILE MET LEU ASP ILE
SEQRES 18 B 459 GLN GLN ASP GLU TYR LEU PRO VAL TRP GLY GLU THR ASP
SEQRES 19 B 459 GLU THR SER PHE GLU ALA GLY ILE LYS VAL GLN ILE HIS
SEQRES 20 B 459 SER GLN ASP GLU PRO PRO LEU ILE ASP GLN LEU GLY PHE
SEQRES 21 B 459 GLY VAL ALA PRO GLY PHE GLN THR PHE VAL SER CYS GLN
SEQRES 22 B 459 GLU GLN ARG LEU ILE TYR LEU PRO PRO PRO TRP GLY ASP
SEQRES 23 B 459 CYS LYS ALA THR THR GLY ASP SER GLU PHE TYR ASP THR
SEQRES 24 B 459 TYR SER ILE THR ALA CYS ARG ILE ASP CYS GLU THR ARG
SEQRES 25 B 459 TYR LEU VAL GLU ASN CYS ASN CYS ARG MET VAL HIS MET
SEQRES 26 B 459 PRO GLY ASP ALA PRO TYR CYS THR PRO GLU GLN TYR LYS
SEQRES 27 B 459 GLU CYS ALA ASP PRO ALA LEU ASP PHE LEU VAL GLU LYS
SEQRES 28 B 459 ASP ASN GLU TYR CYS VAL CYS GLU MET PRO CYS ASN VAL
SEQRES 29 B 459 THR ARG TYR GLY LYS GLU LEU SER MET VAL LYS ILE PRO
SEQRES 30 B 459 SER LYS ALA SER ALA LYS TYR LEU ALA LYS LYS TYR ASN
SEQRES 31 B 459 LYS SER GLU GLN TYR ILE GLY GLU ASN ILE LEU VAL LEU
SEQRES 32 B 459 ASP ILE PHE PHE GLU ALA LEU ASN TYR GLU THR ILE GLU
SEQRES 33 B 459 GLN LYS LYS ALA TYR GLU VAL ALA GLY LEU LEU GLY ASP
SEQRES 34 B 459 ILE GLY GLY GLN MET GLY LEU PHE ILE GLY ALA SER ILE
SEQRES 35 B 459 LEU THR VAL LEU GLU LEU PHE ASP TYR ALA TYR GLU VAL
SEQRES 36 B 459 ILE LYS HIS ARG
SEQRES 1 C 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS GLY ALA SER
SEQRES 2 C 459 LEU VAL PRO ARG GLY SER HIS MET SER THR LEU HIS GLY
SEQRES 3 C 459 ILE SER HIS ILE PHE SER TYR GLU ARG LEU SER LEU LYS
SEQRES 4 C 459 ARG VAL VAL TRP ALA LEU CYS PHE MET GLY SER LEU ALA
SEQRES 5 C 459 LEU LEU ALA LEU VAL CYS THR ASN ARG ILE GLN TYR TYR
SEQRES 6 C 459 PHE LEU TYR PRO HIS VAL THR LYS LEU ASP GLU VAL ALA
SEQRES 7 C 459 ALA THR ARG LEU THR PHE PRO ALA VAL THR PHE CYS ASN
SEQRES 8 C 459 LEU ASN GLU PHE ARG PHE SER ARG VAL THR LYS ASN ASP
SEQRES 9 C 459 LEU TYR HIS ALA GLY GLU LEU LEU ALA LEU LEU ASN ASN
SEQRES 10 C 459 ARG TYR GLU ILE PRO ASP THR GLN THR ALA ASP GLU LYS
SEQRES 11 C 459 GLN LEU GLU ILE LEU GLN ASP LYS ALA ASN PHE ARG ASN
SEQRES 12 C 459 PHE LYS PRO LYS PRO PHE ASN MET LEU GLU PHE TYR ASP
SEQRES 13 C 459 ARG ALA GLY HIS ASP ILE ARG GLU MET LEU LEU SER CYS
SEQRES 14 C 459 PHE PHE ARG GLY GLU GLN CYS SER PRO GLU ASP PHE LYS
SEQRES 15 C 459 VAL VAL PHE THR ARG TYR GLY LYS CYS TYR THR PHE ASN
SEQRES 16 C 459 ALA GLY GLN ASP GLY LYS PRO ARG LEU ILE THR MET LYS
SEQRES 17 C 459 GLY GLY THR GLY ASN GLY LEU GLU ILE MET LEU ASP ILE
SEQRES 18 C 459 GLN GLN ASP GLU TYR LEU PRO VAL TRP GLY GLU THR ASP
SEQRES 19 C 459 GLU THR SER PHE GLU ALA GLY ILE LYS VAL GLN ILE HIS
SEQRES 20 C 459 SER GLN ASP GLU PRO PRO LEU ILE ASP GLN LEU GLY PHE
SEQRES 21 C 459 GLY VAL ALA PRO GLY PHE GLN THR PHE VAL SER CYS GLN
SEQRES 22 C 459 GLU GLN ARG LEU ILE TYR LEU PRO PRO PRO TRP GLY ASP
SEQRES 23 C 459 CYS LYS ALA THR THR GLY ASP SER GLU PHE TYR ASP THR
SEQRES 24 C 459 TYR SER ILE THR ALA CYS ARG ILE ASP CYS GLU THR ARG
SEQRES 25 C 459 TYR LEU VAL GLU ASN CYS ASN CYS ARG MET VAL HIS MET
SEQRES 26 C 459 PRO GLY ASP ALA PRO TYR CYS THR PRO GLU GLN TYR LYS
SEQRES 27 C 459 GLU CYS ALA ASP PRO ALA LEU ASP PHE LEU VAL GLU LYS
SEQRES 28 C 459 ASP ASN GLU TYR CYS VAL CYS GLU MET PRO CYS ASN VAL
SEQRES 29 C 459 THR ARG TYR GLY LYS GLU LEU SER MET VAL LYS ILE PRO
SEQRES 30 C 459 SER LYS ALA SER ALA LYS TYR LEU ALA LYS LYS TYR ASN
SEQRES 31 C 459 LYS SER GLU GLN TYR ILE GLY GLU ASN ILE LEU VAL LEU
SEQRES 32 C 459 ASP ILE PHE PHE GLU ALA LEU ASN TYR GLU THR ILE GLU
SEQRES 33 C 459 GLN LYS LYS ALA TYR GLU VAL ALA GLY LEU LEU GLY ASP
SEQRES 34 C 459 ILE GLY GLY GLN MET GLY LEU PHE ILE GLY ALA SER ILE
SEQRES 35 C 459 LEU THR VAL LEU GLU LEU PHE ASP TYR ALA TYR GLU VAL
SEQRES 36 C 459 ILE LYS HIS ARG
SEQRES 1 D 37 ASP CYS ILE PRO LYS TRP LYS GLY CYS VAL ASN ARG HIS
SEQRES 2 D 37 GLY ASP CYS CYS GLU GLY LEU GLU CYS TRP LYS ARG ARG
SEQRES 3 D 37 ARG SER PHE GLU VAL CYS VAL PRO LYS THR PRO
SEQRES 1 E 37 ASP CYS ILE PRO LYS TRP LYS GLY CYS VAL ASN ARG HIS
SEQRES 2 E 37 GLY ASP CYS CYS GLU GLY LEU GLU CYS TRP LYS ARG ARG
SEQRES 3 E 37 ARG SER PHE GLU VAL CYS VAL PRO LYS THR PRO
SEQRES 1 F 37 ASP CYS ILE PRO LYS TRP LYS GLY CYS VAL ASN ARG HIS
SEQRES 2 F 37 GLY ASP CYS CYS GLU GLY LEU GLU CYS TRP LYS ARG ARG
SEQRES 3 F 37 ARG SER PHE GLU VAL CYS VAL PRO LYS THR PRO
MODRES 3S3X ASN C 367 ASN GLYCOSYLATION SITE
MODRES 3S3X ASN B 367 ASN GLYCOSYLATION SITE
MODRES 3S3X ASN A 394 ASN GLYCOSYLATION SITE
MODRES 3S3X ASN B 394 ASN GLYCOSYLATION SITE
MODRES 3S3X ASN A 367 ASN GLYCOSYLATION SITE
MODRES 3S3X ASN C 394 ASN GLYCOSYLATION SITE
HET NAG A 600 14
HET NAG A 700 14
HET K A 1 1
HET K A 2 1
HET CL A 464 1
HET SO4 A 465 5
HET NAG B 600 14
HET NAG B 700 14
HET NAG C 600 14
HET NAG C 700 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM K POTASSIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
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 7 NAG 6(C8 H15 N O6)
FORMUL 9 K 2(K 1+)
FORMUL 11 CL CL 1-
FORMUL 12 SO4 O4 S 2-
FORMUL 17 HOH *14(H2 O)
HELIX 1 1 VAL A 46 VAL A 61 1 16
HELIX 2 2 CYS A 62 GLN A 67 1 6
HELIX 3 3 THR A 105 GLY A 113 1 9
HELIX 4 4 ASP A 132 ASP A 141 1 10
HELIX 5 5 ASN A 154 GLY A 163 1 10
HELIX 6 6 ASP A 165 MET A 169 1 5
HELIX 7 7 SER A 181 GLU A 183 5 3
HELIX 8 8 GLY A 214 ASN A 217 5 4
HELIX 9 9 GLN A 226 TYR A 230 5 5
HELIX 10 10 LEU A 258 GLY A 263 1 6
HELIX 11 11 SER A 305 ASN A 323 1 19
HELIX 12 12 THR A 337 CYS A 344 1 8
HELIX 13 13 CYS A 344 LYS A 355 1 12
HELIX 14 14 SER A 385 TYR A 393 1 9
HELIX 15 15 SER A 396 ASN A 403 1 8
HELIX 16 16 GLU A 426 GLY A 436 1 11
HELIX 17 17 GLN A 437 THR A 448 1 12
HELIX 18 18 CYS B 50 ALA B 56 1 7
HELIX 19 19 ASN B 64 PHE B 70 1 7
HELIX 20 20 THR B 105 GLY B 113 1 9
HELIX 21 21 ASP B 132 ASP B 141 1 10
HELIX 22 22 ASN B 154 GLY B 163 1 10
HELIX 23 23 ASP B 165 MET B 169 1 5
HELIX 24 24 SER B 181 GLU B 183 5 3
HELIX 25 25 GLY B 214 ASN B 217 5 4
HELIX 26 26 GLN B 226 TYR B 230 5 5
HELIX 27 27 LEU B 258 GLY B 263 1 6
HELIX 28 28 SER B 305 ASN B 323 1 19
HELIX 29 29 THR B 337 CYS B 344 1 8
HELIX 30 30 CYS B 344 LYS B 355 1 12
HELIX 31 31 SER B 385 TYR B 393 1 9
HELIX 32 32 SER B 396 ASN B 403 1 8
HELIX 33 33 GLU B 426 ILE B 442 1 17
HELIX 34 34 CYS C 50 LEU C 71 1 22
HELIX 35 35 THR C 105 GLY C 113 1 9
HELIX 36 36 ASP C 132 ASP C 141 1 10
HELIX 37 37 ASN C 154 GLY C 163 1 10
HELIX 38 38 ASP C 165 MET C 169 1 5
HELIX 39 39 SER C 181 GLU C 183 5 3
HELIX 40 40 GLY C 214 ASN C 217 5 4
HELIX 41 41 GLN C 226 TYR C 230 5 5
HELIX 42 42 LEU C 258 GLY C 263 1 6
HELIX 43 43 SER C 305 ASN C 323 1 19
HELIX 44 44 THR C 337 CYS C 344 1 8
HELIX 45 45 CYS C 344 LYS C 355 1 12
HELIX 46 46 SER C 385 TYR C 393 1 9
HELIX 47 47 SER C 396 ASN C 403 1 8
HELIX 48 48 GLU C 426 VAL C 449 1 24
SHEET 1 A 5 HIS A 74 VAL A 81 0
SHEET 2 A 5 ILE A 404 LYS A 423 -1 O LYS A 422 N VAL A 75
SHEET 3 A 5 LEU A 219 ASP A 224 -1 N ILE A 221 O LEU A 407
SHEET 4 A 5 LEU A 170 PHE A 175 -1 N LEU A 171 O MET A 222
SHEET 5 A 5 GLU A 178 GLN A 179 -1 O GLU A 178 N PHE A 175
SHEET 1 B 4 HIS A 74 VAL A 81 0
SHEET 2 B 4 ILE A 404 LYS A 423 -1 O LYS A 422 N VAL A 75
SHEET 3 B 4 PHE A 270 ILE A 282 1 N THR A 272 O ASP A 408
SHEET 4 B 4 ASN A 367 LYS A 379 -1 O ARG A 370 N GLN A 279
SHEET 1 C 2 LEU A 86 THR A 87 0
SHEET 2 C 2 ILE A 209 THR A 210 -1 O THR A 210 N LEU A 86
SHEET 1 D 5 PHE A 185 THR A 190 0
SHEET 2 D 5 GLY A 193 PHE A 198 -1 O GLY A 193 N THR A 190
SHEET 3 D 5 ALA A 90 ASN A 95 -1 N VAL A 91 O PHE A 198
SHEET 4 D 5 ILE A 246 HIS A 251 -1 O LYS A 247 N CYS A 94
SHEET 5 D 5 PHE A 264 VAL A 266 -1 O PHE A 264 N VAL A 248
SHEET 1 E 5 HIS B 74 VAL B 81 0
SHEET 2 E 5 ILE B 404 LYS B 423 -1 O LYS B 422 N VAL B 75
SHEET 3 E 5 LEU B 219 ASP B 224 -1 N ILE B 221 O LEU B 407
SHEET 4 E 5 LEU B 170 PHE B 175 -1 N LEU B 171 O MET B 222
SHEET 5 E 5 GLU B 178 GLN B 179 -1 O GLU B 178 N PHE B 175
SHEET 1 F 4 HIS B 74 VAL B 81 0
SHEET 2 F 4 ILE B 404 LYS B 423 -1 O LYS B 422 N VAL B 75
SHEET 3 F 4 PHE B 270 ILE B 282 1 N THR B 272 O VAL B 406
SHEET 4 F 4 ASN B 367 LYS B 379 -1 O ARG B 370 N GLN B 279
SHEET 1 G 2 LEU B 86 THR B 87 0
SHEET 2 G 2 ILE B 209 THR B 210 -1 O THR B 210 N LEU B 86
SHEET 1 H 5 PHE B 185 THR B 190 0
SHEET 2 H 5 GLY B 193 PHE B 198 -1 O GLY B 193 N THR B 190
SHEET 3 H 5 ALA B 90 ASN B 95 -1 N VAL B 91 O PHE B 198
SHEET 4 H 5 ILE B 246 HIS B 251 -1 O LYS B 247 N CYS B 94
SHEET 5 H 5 PHE B 264 VAL B 266 -1 O PHE B 264 N VAL B 248
SHEET 1 I 5 HIS C 74 VAL C 81 0
SHEET 2 I 5 ILE C 404 LYS C 423 -1 O LYS C 422 N VAL C 75
SHEET 3 I 5 LEU C 219 ASP C 224 -1 N ILE C 221 O LEU C 407
SHEET 4 I 5 LEU C 170 PHE C 175 -1 N LEU C 171 O MET C 222
SHEET 5 I 5 GLU C 178 GLN C 179 -1 O GLU C 178 N PHE C 175
SHEET 1 J 4 HIS C 74 VAL C 81 0
SHEET 2 J 4 ILE C 404 LYS C 423 -1 O LYS C 422 N VAL C 75
SHEET 3 J 4 PHE C 270 ILE C 282 1 N THR C 272 O VAL C 406
SHEET 4 J 4 ASN C 367 LYS C 379 -1 O ARG C 370 N GLN C 279
SHEET 1 K 2 LEU C 86 THR C 87 0
SHEET 2 K 2 ILE C 209 THR C 210 -1 O THR C 210 N LEU C 86
SHEET 1 L 5 PHE C 185 THR C 190 0
SHEET 2 L 5 GLY C 193 PHE C 198 -1 O GLY C 193 N THR C 190
SHEET 3 L 5 ALA C 90 ASN C 95 -1 N VAL C 91 O PHE C 198
SHEET 4 L 5 ILE C 246 HIS C 251 -1 O LYS C 247 N CYS C 94
SHEET 5 L 5 PHE C 264 VAL C 266 -1 O PHE C 264 N VAL C 248
SHEET 1 M 2 LEU D 21 TRP D 24 0
SHEET 2 M 2 VAL D 32 PRO D 35 -1 O VAL D 34 N GLU D 22
SHEET 1 N 2 LEU E 21 TRP E 24 0
SHEET 2 N 2 VAL E 32 PRO E 35 -1 O VAL E 34 N GLU E 22
SHEET 1 O 2 LEU F 21 TRP F 24 0
SHEET 2 O 2 VAL F 32 PRO F 35 -1 O VAL F 34 N GLU F 22
SSBOND 1 CYS A 94 CYS A 195 1555 1555 2.03
SSBOND 2 CYS A 173 CYS A 180 1555 1555 2.03
SSBOND 3 CYS A 291 CYS A 366 1555 1555 2.03
SSBOND 4 CYS A 309 CYS A 362 1555 1555 2.03
SSBOND 5 CYS A 313 CYS A 360 1555 1555 2.03
SSBOND 6 CYS A 322 CYS A 344 1555 1555 2.03
SSBOND 7 CYS A 324 CYS A 336 1555 1555 2.03
SSBOND 8 CYS B 94 CYS B 195 1555 1555 2.03
SSBOND 9 CYS B 173 CYS B 180 1555 1555 2.03
SSBOND 10 CYS B 291 CYS B 366 1555 1555 2.03
SSBOND 11 CYS B 309 CYS B 362 1555 1555 2.03
SSBOND 12 CYS B 313 CYS B 360 1555 1555 2.03
SSBOND 13 CYS B 322 CYS B 344 1555 1555 2.03
SSBOND 14 CYS B 324 CYS B 336 1555 1555 2.03
SSBOND 15 CYS C 94 CYS C 195 1555 1555 2.03
SSBOND 16 CYS C 173 CYS C 180 1555 1555 2.03
SSBOND 17 CYS C 291 CYS C 366 1555 1555 2.03
SSBOND 18 CYS C 309 CYS C 362 1555 1555 2.03
SSBOND 19 CYS C 313 CYS C 360 1555 1555 2.04
SSBOND 20 CYS C 322 CYS C 344 1555 1555 2.03
SSBOND 21 CYS C 324 CYS C 336 1555 1555 2.03
SSBOND 22 CYS D 3 CYS D 18 1555 1555 2.03
SSBOND 23 CYS D 10 CYS D 23 1555 1555 2.03
SSBOND 24 CYS D 17 CYS D 33 1555 1555 2.03
SSBOND 25 CYS E 3 CYS E 18 1555 1555 2.03
SSBOND 26 CYS E 10 CYS E 23 1555 1555 2.03
SSBOND 27 CYS E 17 CYS E 33 1555 1555 2.03
SSBOND 28 CYS F 3 CYS F 18 1555 1555 2.03
SSBOND 29 CYS F 10 CYS F 23 1555 1555 2.03
SSBOND 30 CYS F 17 CYS F 33 1555 1555 2.03
LINK ND2 ASN A 367 C1 NAG A 600 1555 1555 1.44
LINK ND2 ASN A 394 C1 NAG A 700 1555 1555 1.44
LINK ND2 ASN B 367 C1 NAG B 600 1555 1555 1.44
LINK ND2 ASN B 394 C1 NAG B 700 1555 1555 1.44
LINK ND2 ASN C 367 C1 NAG C 600 1555 1555 1.44
LINK ND2 ASN C 394 C1 NAG C 700 1555 1555 1.44
LINK K K A 2 OD2 ASP A 260 1555 1555 3.17
LINK K K A 2 OE1 GLU A 314 1555 1555 3.47
CISPEP 1 ILE A 380 PRO A 381 0 2.88
CISPEP 2 ILE B 380 PRO B 381 0 2.63
CISPEP 3 ILE C 380 PRO C 381 0 2.94
CRYST1 232.396 109.442 127.269 90.00 119.81 90.00 C 1 2 1 12
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 0.004303 0.000000 0.002465 0.00000
SCALE2 0.000000 0.009137 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009056 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
