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4G1I.pdb
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4G1I.pdb
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HEADER CELL INVASION 10-JUL-12 4G1I
TITLE STRUCTURE OF THE PRGH PERIPLASMIC DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN PRGH;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 170-392;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_COMMON: SALMONELLA TYPHIMURIUM;
SOURCE 5 ORGANISM_TAXID: 90371;
SOURCE 6 GENE: PRGH, STM2874;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS RING-BUILDING MOTIF, TYPE III SECRETION, INVG, CELL INVASION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.C.BERGERON,L.J.WORRALL,N.C.J.STRYNADKA
REVDAT 2 22-MAY-13 4G1I 1 JRNL
REVDAT 1 08-MAY-13 4G1I 0
JRNL AUTH J.R.BERGERON,L.J.WORRALL,N.G.SGOURAKIS,F.DIMAIO,
JRNL AUTH 2 R.A.PFUETZNER,H.B.FELISE,M.VUCKOVIC,A.C.YU,S.I.MILLER,
JRNL AUTH 3 D.BAKER,N.C.STRYNADKA
JRNL TITL A REFINED MODEL OF THE PROTOTYPICAL SALMONELLA SPI-1 T3SS
JRNL TITL 2 BASAL BODY REVEALS THE MOLECULAR BASIS FOR ITS ASSEMBLY.
JRNL REF PLOS PATHOG. V. 9 03307 2013
JRNL REFN ISSN 1553-7366
JRNL PMID 23633951
JRNL DOI 10.1371/JOURNAL.PPAT.1003307
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 36630
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1835
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 45.9714 - 4.3488 0.96 2735 150 0.1898 0.2124
REMARK 3 2 4.3488 - 3.4522 0.99 2682 161 0.1514 0.1952
REMARK 3 3 3.4522 - 3.0159 0.99 2688 132 0.1669 0.2066
REMARK 3 4 3.0159 - 2.7402 0.99 2688 144 0.1659 0.2055
REMARK 3 5 2.7402 - 2.5438 1.00 2667 147 0.1724 0.2186
REMARK 3 6 2.5438 - 2.3938 1.00 2691 133 0.1614 0.1967
REMARK 3 7 2.3938 - 2.2739 1.00 2683 135 0.1750 0.2357
REMARK 3 8 2.2739 - 2.1750 1.00 2658 140 0.1694 0.2386
REMARK 3 9 2.1750 - 2.0912 1.00 2649 139 0.1799 0.1970
REMARK 3 10 2.0912 - 2.0191 1.00 2670 140 0.1836 0.2462
REMARK 3 11 2.0191 - 1.9559 1.00 2640 140 0.1971 0.2549
REMARK 3 12 1.9559 - 1.9000 1.00 2688 144 0.2081 0.2653
REMARK 3 13 1.9000 - 1.8500 1.00 2656 130 0.2385 0.3163
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.570
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) : 1.76820
REMARK 3 B22 (A**2) : -7.96000
REMARK 3 B33 (A**2) : 6.19180
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -5.67610
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 : 0.015 3320
REMARK 3 ANGLE : 1.545 4464
REMARK 3 CHIRALITY : 0.118 463
REMARK 3 PLANARITY : 0.007 572
REMARK 3 DIHEDRAL : 18.006 1281
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 173:184)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6965 -0.6902 31.7675
REMARK 3 T TENSOR
REMARK 3 T11: 0.5711 T22: 0.4950
REMARK 3 T33: 0.3177 T12: 0.1430
REMARK 3 T13: -0.0272 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 0.0146 L22: -0.0008
REMARK 3 L33: 0.0083 L12: 0.0188
REMARK 3 L13: 0.0511 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.3658 S12: -0.2153 S13: 0.4376
REMARK 3 S21: 0.5110 S22: 0.4448 S23: 0.3517
REMARK 3 S31: -0.0042 S32: 0.3471 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 185:201)
REMARK 3 ORIGIN FOR THE GROUP (A): -49.9071 -1.3272 23.1334
REMARK 3 T TENSOR
REMARK 3 T11: 0.5185 T22: 0.3189
REMARK 3 T33: 0.2660 T12: -0.0430
REMARK 3 T13: -0.0575 T23: 0.0727
REMARK 3 L TENSOR
REMARK 3 L11: 0.0446 L22: 0.1058
REMARK 3 L33: 0.0665 L12: -0.0890
REMARK 3 L13: 0.0477 L23: 0.0038
REMARK 3 S TENSOR
REMARK 3 S11: 0.1137 S12: -0.2301 S13: -0.1069
REMARK 3 S21: 0.1997 S22: 0.1010 S23: -0.3091
REMARK 3 S31: 0.5127 S32: -0.0046 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 202:214)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.8297 -3.6560 23.2645
REMARK 3 T TENSOR
REMARK 3 T11: 0.5804 T22: 0.3485
REMARK 3 T33: 0.3654 T12: 0.1192
REMARK 3 T13: -0.1864 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: -0.0106 L22: 0.0024
REMARK 3 L33: 0.0495 L12: 0.0582
REMARK 3 L13: 0.0014 L23: -0.0076
REMARK 3 S TENSOR
REMARK 3 S11: -0.1061 S12: -0.1380 S13: 0.1918
REMARK 3 S21: 0.1369 S22: 0.0958 S23: -0.2818
REMARK 3 S31: 0.1743 S32: 0.3169 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 215:221)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5288 -11.3432 25.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.6038 T22: 0.2562
REMARK 3 T33: 0.3545 T12: 0.0114
REMARK 3 T13: -0.0132 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: -0.0185 L22: -0.0138
REMARK 3 L33: -0.0149 L12: 0.0353
REMARK 3 L13: 0.0039 L23: -0.0338
REMARK 3 S TENSOR
REMARK 3 S11: -0.2398 S12: 0.0656 S13: -0.1549
REMARK 3 S21: -0.2839 S22: -0.2283 S23: 0.4880
REMARK 3 S31: -0.0362 S32: 0.3313 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 222:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -54.4520 7.2484 8.7686
REMARK 3 T TENSOR
REMARK 3 T11: 0.1545 T22: 0.1012
REMARK 3 T33: 0.1148 T12: -0.0036
REMARK 3 T13: -0.0076 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.5352 L22: 0.9221
REMARK 3 L33: -0.2538 L12: 0.7077
REMARK 3 L13: -0.1485 L23: 0.0646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.0032 S13: -0.0367
REMARK 3 S21: 0.0616 S22: -0.0753 S23: 0.0463
REMARK 3 S31: 0.0483 S32: 0.0447 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 267:278)
REMARK 3 ORIGIN FOR THE GROUP (A): -67.8887 6.5540 7.9584
REMARK 3 T TENSOR
REMARK 3 T11: 0.2008 T22: 0.2286
REMARK 3 T33: 0.2630 T12: -0.0122
REMARK 3 T13: 0.0298 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: -0.0110 L22: 0.0224
REMARK 3 L33: -0.0004 L12: 0.0023
REMARK 3 L13: 0.0121 L23: -0.0606
REMARK 3 S TENSOR
REMARK 3 S11: 0.0384 S12: -0.0791 S13: -0.1291
REMARK 3 S21: 0.2594 S22: -0.0358 S23: 0.3742
REMARK 3 S31: -0.1050 S32: -0.0890 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 279:308)
REMARK 3 ORIGIN FOR THE GROUP (A): -54.6837 14.2897 10.2586
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.1535
REMARK 3 T33: 0.1375 T12: -0.0119
REMARK 3 T13: -0.0113 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.3584 L22: 0.4182
REMARK 3 L33: 0.0225 L12: -0.3818
REMARK 3 L13: -0.0344 L23: 0.2846
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.0649 S13: 0.1583
REMARK 3 S21: 0.0779 S22: 0.0408 S23: 0.1535
REMARK 3 S31: 0.0093 S32: -0.0457 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain A and resid 309:331)
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2271 23.5738 -4.6858
REMARK 3 T TENSOR
REMARK 3 T11: 0.2578 T22: 0.2848
REMARK 3 T33: 0.2701 T12: 0.0204
REMARK 3 T13: 0.0892 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 0.1370 L22: 0.1192
REMARK 3 L33: 0.3718 L12: -0.0485
REMARK 3 L13: -0.1787 L23: -0.0988
REMARK 3 S TENSOR
REMARK 3 S11: 0.2037 S12: 0.0785 S13: 0.3154
REMARK 3 S21: -0.2543 S22: -0.2516 S23: -0.2038
REMARK 3 S31: 0.0931 S32: -0.0441 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain A and resid 332:363)
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5902 18.7425 1.8680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.1788
REMARK 3 T33: 0.1281 T12: -0.0013
REMARK 3 T13: 0.0098 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.1352 L22: 0.4043
REMARK 3 L33: 0.2211 L12: 0.1147
REMARK 3 L13: -0.2334 L23: -0.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.0741 S13: -0.0618
REMARK 3 S21: -0.0474 S22: 0.0618 S23: 0.0051
REMARK 3 S31: 0.0905 S32: 0.0957 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 183:217)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5359 38.8532 37.5422
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.4055
REMARK 3 T33: 0.3874 T12: 0.0447
REMARK 3 T13: -0.0864 T23: -0.0841
REMARK 3 L TENSOR
REMARK 3 L11: 0.4464 L22: 0.0580
REMARK 3 L33: 0.1712 L12: -0.0853
REMARK 3 L13: 0.2338 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0639 S12: -0.1802 S13: 0.2625
REMARK 3 S21: 0.0460 S22: 0.0797 S23: -0.2508
REMARK 3 S31: 0.0737 S32: -0.1680 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 218:294)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0552 29.8555 22.0881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.1793
REMARK 3 T33: 0.2137 T12: -0.0091
REMARK 3 T13: -0.0050 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.0178 L22: 0.3225
REMARK 3 L33: 0.2433 L12: 0.6832
REMARK 3 L13: -0.3624 L23: -0.4546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0987 S12: 0.0748 S13: 0.0595
REMARK 3 S21: 0.0731 S22: 0.0117 S23: -0.0742
REMARK 3 S31: 0.0015 S32: -0.0133 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 295:356)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8449 13.1358 35.7373
REMARK 3 T TENSOR
REMARK 3 T11: 0.2244 T22: 0.1825
REMARK 3 T33: 0.1671 T12: 0.0168
REMARK 3 T13: -0.0022 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.7532 L22: 0.2776
REMARK 3 L33: 0.6594 L12: 0.3092
REMARK 3 L13: -0.2490 L23: -0.0753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: -0.0296 S13: -0.0242
REMARK 3 S21: 0.0626 S22: 0.0574 S23: -0.1010
REMARK 3 S31: 0.0649 S32: 0.0240 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain B and resid 357:367)
REMARK 3 ORIGIN FOR THE GROUP (A): -38.5416 10.0416 47.7402
REMARK 3 T TENSOR
REMARK 3 T11: 0.2393 T22: 0.2217
REMARK 3 T33: 0.2800 T12: 0.0020
REMARK 3 T13: 0.0723 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.0330 L22: -0.0259
REMARK 3 L33: 0.0169 L12: 0.1250
REMARK 3 L13: 0.0512 L23: 0.0806
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: 0.3640 S13: -0.7076
REMARK 3 S21: 0.2255 S22: -0.1418 S23: -0.1806
REMARK 3 S31: -0.3558 S32: -0.4870 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 4G1I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43189
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTOMR
REMARK 200 STARTING MODEL: PDB ENTRY 3GR0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BICINE, PH 8.5, 20% PEG6000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 132.21600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.69000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 132.21600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.69000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THOUGH THE CLONED PROTEIN CONSTRUCT THAT WAS CRYSTALLIZED
REMARK 300 IS A MONOMER, THE FULL-LENGTH VERSION OF THIS PROTEIN FORMS A 24-
REMARK 300 MER.
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
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
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 166
REMARK 465 SER A 167
REMARK 465 HIS A 168
REMARK 465 MET A 169
REMARK 465 ALA A 170
REMARK 465 ALA A 171
REMARK 465 GLU A 180
REMARK 465 LYS A 181
REMARK 465 GLU A 182
REMARK 465 ASP A 364
REMARK 465 TRP A 365
REMARK 465 LEU A 366
REMARK 465 LYS A 367
REMARK 465 GLY A 368
REMARK 465 ARG A 369
REMARK 465 SER A 370
REMARK 465 PHE A 371
REMARK 465 GLN A 372
REMARK 465 TYR A 373
REMARK 465 GLY A 374
REMARK 465 ALA A 375
REMARK 465 GLU A 376
REMARK 465 GLY A 377
REMARK 465 TYR A 378
REMARK 465 ILE A 379
REMARK 465 LYS A 380
REMARK 465 MET A 381
REMARK 465 SER A 382
REMARK 465 PRO A 383
REMARK 465 GLY A 384
REMARK 465 HIS A 385
REMARK 465 TRP A 386
REMARK 465 TYR A 387
REMARK 465 PHE A 388
REMARK 465 PRO A 389
REMARK 465 SER A 390
REMARK 465 PRO A 391
REMARK 465 LEU A 392
REMARK 465 GLY B 166
REMARK 465 SER B 167
REMARK 465 HIS B 168
REMARK 465 MET B 169
REMARK 465 ALA B 170
REMARK 465 ALA B 171
REMARK 465 GLU B 180
REMARK 465 LYS B 181
REMARK 465 SER B 370
REMARK 465 PHE B 371
REMARK 465 GLN B 372
REMARK 465 TYR B 373
REMARK 465 GLY B 374
REMARK 465 ALA B 375
REMARK 465 GLU B 376
REMARK 465 GLY B 377
REMARK 465 TYR B 378
REMARK 465 ILE B 379
REMARK 465 LYS B 380
REMARK 465 MET B 381
REMARK 465 SER B 382
REMARK 465 PRO B 383
REMARK 465 GLY B 384
REMARK 465 HIS B 385
REMARK 465 TRP B 386
REMARK 465 TYR B 387
REMARK 465 PHE B 388
REMARK 465 PRO B 389
REMARK 465 SER B 390
REMARK 465 PRO B 391
REMARK 465 LEU B 392
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 GLN A 179 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 344 O HOH A 586 2.03
REMARK 500 O ASP A 363 O HOH A 618 2.03
REMARK 500 O HOH A 609 O HOH A 613 2.08
REMARK 500 O HOH A 593 O HOH A 597 2.16
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 217 -13.44 -49.23
REMARK 500 LYS A 218 16.94 -141.03
REMARK 500 TYR A 246 -72.22 -107.15
REMARK 500 TYR A 354 -80.63 -124.52
REMARK 500 ASP B 215 72.53 23.58
REMARK 500 TYR B 246 -70.57 -111.68
REMARK 500 TYR B 354 -72.81 -127.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 587 DISTANCE = 6.46 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 401
REMARK 610 1PE A 402
REMARK 610 1PE B 401
REMARK 610 1PE B 402
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GR0 RELATED DB: PDB
REMARK 900 ALTERNATIVE CRYSTAL FORM
REMARK 900 RELATED ID: 3GR1 RELATED DB: PDB
REMARK 900 ALTERNATIVE CRYSTAL FORM
REMARK 900 RELATED ID: 4G08 RELATED DB: PDB
REMARK 900 RELATED ID: 4G2S RELATED DB: PDB
DBREF 4G1I A 170 392 UNP P41783 PRGH_SALTY 170 392
DBREF 4G1I B 170 392 UNP P41783 PRGH_SALTY 170 392
SEQADV 4G1I GLY A 166 UNP P41783 EXPRESSION TAG
SEQADV 4G1I SER A 167 UNP P41783 EXPRESSION TAG
SEQADV 4G1I HIS A 168 UNP P41783 EXPRESSION TAG
SEQADV 4G1I MET A 169 UNP P41783 EXPRESSION TAG
SEQADV 4G1I GLY B 166 UNP P41783 EXPRESSION TAG
SEQADV 4G1I SER B 167 UNP P41783 EXPRESSION TAG
SEQADV 4G1I HIS B 168 UNP P41783 EXPRESSION TAG
SEQADV 4G1I MET B 169 UNP P41783 EXPRESSION TAG
SEQRES 1 A 227 GLY SER HIS MET ALA ALA GLU LEU ASP SER LEU LEU GLY
SEQRES 2 A 227 GLN GLU LYS GLU ARG PHE GLN VAL LEU PRO GLY ARG ASP
SEQRES 3 A 227 LYS MET LEU TYR VAL ALA ALA GLN ASN GLU ARG ASP THR
SEQRES 4 A 227 LEU TRP ALA ARG GLN VAL LEU ALA ARG GLY ASP TYR ASP
SEQRES 5 A 227 LYS ASN ALA ARG VAL ILE ASN GLU ASN GLU GLU ASN LYS
SEQRES 6 A 227 ARG ILE SER ILE TRP LEU ASP THR TYR TYR PRO GLN LEU
SEQRES 7 A 227 ALA TYR TYR ARG ILE HIS PHE ASP GLU PRO ARG LYS PRO
SEQRES 8 A 227 VAL PHE TRP LEU SER ARG GLN ARG ASN THR MET SER LYS
SEQRES 9 A 227 LYS GLU LEU GLU VAL LEU SER GLN LYS LEU ARG ALA LEU
SEQRES 10 A 227 MET PRO TYR ALA ASP SER VAL ASN ILE THR LEU MET ASP
SEQRES 11 A 227 ASP VAL THR ALA ALA GLY GLN ALA GLU ALA GLY LEU LYS
SEQRES 12 A 227 GLN GLN ALA LEU PRO TYR SER ARG ARG ASN HIS LYS GLY
SEQRES 13 A 227 GLY VAL THR PHE VAL ILE GLN GLY ALA LEU ASP ASP VAL
SEQRES 14 A 227 GLU ILE LEU ARG ALA ARG GLN PHE VAL ASP SER TYR TYR
SEQRES 15 A 227 ARG THR TRP GLY GLY ARG TYR VAL GLN PHE ALA ILE GLU
SEQRES 16 A 227 LEU LYS ASP ASP TRP LEU LYS GLY ARG SER PHE GLN TYR
SEQRES 17 A 227 GLY ALA GLU GLY TYR ILE LYS MET SER PRO GLY HIS TRP
SEQRES 18 A 227 TYR PHE PRO SER PRO LEU
SEQRES 1 B 227 GLY SER HIS MET ALA ALA GLU LEU ASP SER LEU LEU GLY
SEQRES 2 B 227 GLN GLU LYS GLU ARG PHE GLN VAL LEU PRO GLY ARG ASP
SEQRES 3 B 227 LYS MET LEU TYR VAL ALA ALA GLN ASN GLU ARG ASP THR
SEQRES 4 B 227 LEU TRP ALA ARG GLN VAL LEU ALA ARG GLY ASP TYR ASP
SEQRES 5 B 227 LYS ASN ALA ARG VAL ILE ASN GLU ASN GLU GLU ASN LYS
SEQRES 6 B 227 ARG ILE SER ILE TRP LEU ASP THR TYR TYR PRO GLN LEU
SEQRES 7 B 227 ALA TYR TYR ARG ILE HIS PHE ASP GLU PRO ARG LYS PRO
SEQRES 8 B 227 VAL PHE TRP LEU SER ARG GLN ARG ASN THR MET SER LYS
SEQRES 9 B 227 LYS GLU LEU GLU VAL LEU SER GLN LYS LEU ARG ALA LEU
SEQRES 10 B 227 MET PRO TYR ALA ASP SER VAL ASN ILE THR LEU MET ASP
SEQRES 11 B 227 ASP VAL THR ALA ALA GLY GLN ALA GLU ALA GLY LEU LYS
SEQRES 12 B 227 GLN GLN ALA LEU PRO TYR SER ARG ARG ASN HIS LYS GLY
SEQRES 13 B 227 GLY VAL THR PHE VAL ILE GLN GLY ALA LEU ASP ASP VAL
SEQRES 14 B 227 GLU ILE LEU ARG ALA ARG GLN PHE VAL ASP SER TYR TYR
SEQRES 15 B 227 ARG THR TRP GLY GLY ARG TYR VAL GLN PHE ALA ILE GLU
SEQRES 16 B 227 LEU LYS ASP ASP TRP LEU LYS GLY ARG SER PHE GLN TYR
SEQRES 17 B 227 GLY ALA GLU GLY TYR ILE LYS MET SER PRO GLY HIS TRP
SEQRES 18 B 227 TYR PHE PRO SER PRO LEU
HET 1PE A 401 14
HET 1PE A 402 14
HET PO4 A 403 5
HET PO4 A 404 5
HET 1PE B 401 14
HET 1PE B 402 14
HET PO4 B 403 5
HET PO4 B 404 5
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PO4 PHOSPHATE ION
HETSYN 1PE PEG400
FORMUL 3 1PE 4(C10 H22 O6)
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 11 HOH *233(H2 O)
HELIX 1 1 GLU A 172 GLN A 179 1 8
HELIX 2 2 ASN A 200 ARG A 213 1 14
HELIX 3 3 ASN A 224 TYR A 240 1 17
HELIX 4 4 SER A 268 MET A 283 1 16
HELIX 5 5 ASP A 295 GLN A 310 1 16
HELIX 6 6 ASP A 332 GLY A 351 1 20
HELIX 7 7 LEU B 173 GLN B 179 1 7
HELIX 8 8 ASN B 200 GLY B 214 1 15
HELIX 9 9 ASN B 224 TYR B 240 1 17
HELIX 10 10 SER B 268 MET B 283 1 16
HELIX 11 11 ASP B 295 GLN B 310 1 16
HELIX 12 12 ASP B 332 GLY B 351 1 20
SHEET 1 A 3 PHE A 184 PRO A 188 0
SHEET 2 A 3 LEU A 194 ALA A 198 -1 O TYR A 195 N LEU A 187
SHEET 3 A 3 ALA A 220 ILE A 223 1 O ILE A 223 N VAL A 196
SHEET 1 B 3 TYR A 245 HIS A 249 0
SHEET 2 B 3 VAL A 257 SER A 261 -1 O VAL A 257 N HIS A 249
SHEET 3 B 3 ASN A 290 MET A 294 1 O MET A 294 N LEU A 260
SHEET 1 C 3 TYR A 314 HIS A 319 0
SHEET 2 C 3 GLY A 322 GLY A 329 -1 O VAL A 326 N SER A 315
SHEET 3 C 3 VAL A 355 LEU A 361 1 O GLU A 360 N ILE A 327
SHEET 1 D 3 GLN B 185 PRO B 188 0
SHEET 2 D 3 LEU B 194 ALA B 197 -1 O TYR B 195 N LEU B 187
SHEET 3 D 3 ALA B 220 ILE B 223 1 O ARG B 221 N VAL B 196
SHEET 1 E 3 TYR B 245 HIS B 249 0
SHEET 2 E 3 VAL B 257 SER B 261 -1 O VAL B 257 N HIS B 249
SHEET 3 E 3 ASN B 290 MET B 294 1 O MET B 294 N LEU B 260
SHEET 1 F 3 TYR B 314 ASN B 318 0
SHEET 2 F 3 VAL B 323 ILE B 327 -1 O VAL B 326 N SER B 315
SHEET 3 F 3 VAL B 355 ILE B 359 1 O ALA B 358 N ILE B 327
SITE 1 AC1 8 TYR A 239 TYR A 240 GLN A 263 ASN A 265
SITE 2 AC1 8 THR A 266 VAL A 274 LYS A 278 HOH A 614
SITE 1 AC2 8 GLU A 227 ARG A 231 LEU A 282 THR A 298
SITE 2 AC2 8 GLY A 301 ALA A 305 HOH A 505 TRP B 365
SITE 1 AC3 4 THR A 298 GLN A 302 TRP A 350 HOH A 630
SITE 1 AC4 5 MET A 294 ASP A 295 THR A 298 HOH A 571
SITE 2 AC4 5 HOH A 630
SITE 1 AC5 3 TYR B 239 LYS B 278 ALA B 281
SITE 1 AC6 7 ARG B 221 ARG B 231 LEU B 282 THR B 298
SITE 2 AC6 7 GLY B 301 GLN B 302 HOH B 584
SITE 1 AC7 7 GLY A 329 ALA A 330 LEU A 331 LYS A 362
SITE 2 AC7 7 ARG B 340 VAL B 343 ASP B 344
SITE 1 AC8 4 ALA A 358 HOH A 581 ARG B 317 HOH B 569
CRYST1 264.432 33.380 48.530 90.00 91.60 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003788 0.000000 0.000112 0.00000
SCALE2 0.000000 0.029985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020628 0.00000
ATOM 1 N GLU A 172 -49.847 -6.027 32.848 1.00 42.47 N
ATOM 2 CA GLU A 172 -50.553 -4.786 32.493 1.00 56.33 C
ATOM 3 C GLU A 172 -49.853 -3.635 33.213 1.00 51.50 C
ATOM 4 O GLU A 172 -49.035 -2.930 32.621 1.00 49.32 O
ATOM 5 CB GLU A 172 -52.069 -4.869 32.780 1.00 60.53 C
ATOM 6 CG GLU A 172 -52.523 -5.253 34.204 1.00 69.49 C
ATOM 7 CD GLU A 172 -52.173 -6.685 34.619 1.00 65.19 C
ATOM 8 OE1 GLU A 172 -51.698 -7.474 33.772 1.00 61.98 O
ATOM 9 OE2 GLU A 172 -52.382 -7.014 35.804 1.00 66.14 O
ATOM 10 N LEU A 173 -50.118 -3.488 34.506 1.00 81.91 N
ANISOU 10 N LEU A 173 11865 10053 9205 1989 608 954 N
ATOM 11 CA LEU A 173 -49.147 -2.827 35.364 1.00 72.60 C
ANISOU 11 CA LEU A 173 10734 8950 7902 2070 541 774 C
ATOM 12 C LEU A 173 -47.895 -3.726 35.431 1.00 64.44 C
ANISOU 12 C LEU A 173 9752 8113 6619 2132 478 689 C
ATOM 13 O LEU A 173 -46.797 -3.216 35.599 1.00 58.42 O
ANISOU 13 O LEU A 173 8981 7456 5761 2125 365 557 O
ATOM 14 CB LEU A 173 -49.726 -2.533 36.756 1.00 73.90 C
ANISOU 14 CB LEU A 173 11012 9018 8048 2248 664 709 C
ATOM 15 CG LEU A 173 -50.408 -1.168 37.002 1.00 79.24 C
ANISOU 15 CG LEU A 173 11642 9541 8925 2202 672 699 C
ATOM 16 CD1 LEU A 173 -49.432 -0.084 37.482 1.00 80.70 C
ANISOU 16 CD1 LEU A 173 11819 9784 9061 2204 560 532 C
ATOM 17 CD2 LEU A 173 -51.175 -0.679 35.777 1.00 77.58 C
ANISOU 17 CD2 LEU A 173 11293 9223 8963 2001 641 844 C
ATOM 18 N ASP A 174 -48.060 -5.051 35.266 1.00 59.88 N
ANISOU 18 N ASP A 174 9226 7586 5941 2189 547 768 N
ATOM 19 CA ASP A 174 -46.910 -5.979 35.190 1.00 55.93 C
ANISOU 19 CA ASP A 174 8767 7272 5214 2233 485 704 C
ATOM 20 C ASP A 174 -45.930 -5.539 34.077 1.00 63.48 C
ANISOU 20 C ASP A 174 9597 8334 6190 2050 308 682 C
ATOM 21 O ASP A 174 -44.726 -5.389 34.308 1.00 62.84 O
ANISOU 21 O ASP A 174 9530 8388 5958 2073 207 548 O
ATOM 22 CB ASP A 174 -47.345 -7.445 34.912 1.00 65.32 C
ANISOU 22 CB ASP A 174 10003 8486 6330 2282 577 821 C
ATOM 23 CG ASP A 174 -48.374 -7.995 35.919 1.00 71.39 C
ANISOU 23 CG ASP A 174 10892 9150 7082 2456 757 860 C
ATOM 24 OD1 ASP A 174 -49.029 -7.192 36.620 1.00 77.99 O
ANISOU 24 OD1 ASP A 174 11753 9861 8019 2507 820 836 O
ATOM 25 OD2 ASP A 174 -48.547 -9.250 35.981 1.00 63.38 O
ANISOU 25 OD2 ASP A 174 9946 8178 5955 2540 836 920 O
ATOM 26 N SER A 175 -46.461 -5.338 32.868 1.00 56.94 N
ANISOU 26 N SER A 175 8644 7441 5548 1868 272 815 N
ATOM 27 CA SER A 175 -45.652 -4.964 31.700 1.00 55.00 C
ANISOU 27 CA SER A 175 8271 7286 5342 1681 110 816 C
ATOM 28 C SER A 175 -44.986 -3.613 31.930 1.00 56.22 C
ANISOU 28 C SER A 175 8379 7449 5532 1631 -2 686 C
ATOM 29 O SER A 175 -43.787 -3.445 31.662 1.00 53.47 O
ANISOU 29 O SER A 175 7998 7240 5077 1583 -133 590 O
ATOM 30 CB SER A 175 -46.533 -4.934 30.452 1.00 52.33 C
ANISOU 30 CB SER A 175 7814 6850 5220 1504 111 991 C
ATOM 31 OG SER A 175 -45.809 -5.309 29.299 1.00 62.85 O
ANISOU 31 OG SER A 175 9057 8300 6524 1364 -6 1027 O
ATOM 32 N LEU A 176 -45.769 -2.663 32.445 1.00 53.03 N
ANISOU 32 N LEU A 176 7977 6897 5277 1647 53 683 N
ATOM 33 CA LEU A 176 -45.247 -1.378 32.914 1.00 58.91 C
ANISOU 33 CA LEU A 176 8701 7635 6049 1635 -29 550 C
ATOM 34 C LEU A 176 -43.944 -1.507 33.720 1.00 62.97 C
ANISOU 34 C LEU A 176 9298 8306 6322 1756 -89 375 C
ATOM 35 O LEU A 176 -42.949 -0.839 33.417 1.00 62.07 O
ANISOU 35 O LEU A 176 9123 8281 6180 1672 -230 282 O
ATOM 36 CB LEU A 176 -46.309 -0.665 33.758 1.00 64.87 C
ANISOU 36 CB LEU A 176 9498 8216 6933 1712 82 556 C
ATOM 37 CG LEU A 176 -46.907 0.636 33.212 1.00 74.39 C
ANISOU 37 CG LEU A 176 10586 9287 8390 1557 37 602 C
ATOM 38 CD1 LEU A 176 -48.313 0.849 33.767 1.00 71.94 C
ANISOU 38 CD1 LEU A 176 10316 8790 8226 1624 185 679 C
ATOM 39 CD2 LEU A 176 -45.994 1.832 33.537 1.00 80.02 C
ANISOU 39 CD2 LEU A 176 11271 10046 9086 1530 -85 449 C
ATOM 40 N LEU A 177 -43.947 -2.380 34.732 1.00 66.37 N
ANISOU 40 N LEU A 177 9867 8772 6579 1951 16 330 N
ATOM 41 CA LEU A 177 -42.775 -2.554 35.594 1.00 66.56 C
ANISOU 41 CA LEU A 177 9981 8938 6369 2082 -27 164 C
ATOM 42 C LEU A 177 -41.587 -3.075 34.799 1.00 58.23 C
ANISOU 42 C LEU A 177 8879 8062 5185 2001 -156 135 C
ATOM 43 O LEU A 177 -40.450 -2.726 35.091 1.00 58.98 O
ANISOU 43 O LEU A 177 8984 8273 5151 2020 -257 -4 O
ATOM 44 CB LEU A 177 -43.090 -3.494 36.765 1.00 76.51 C
ANISOU 44 CB LEU A 177 11399 10198 7474 2303 119 139 C
ATOM 45 CG LEU A 177 -44.487 -3.332 37.380 1.00 85.38 C
ANISOU 45 CG LEU A 177 12570 11139 8731 2381 274 214 C
ATOM 46 CD1 LEU A 177 -44.853 -4.457 38.350 1.00 90.74 C
ANISOU 46 CD1 LEU A 177 13396 11822 9258 2584 421 216 C
ATOM 47 CD2 LEU A 177 -44.704 -1.967 38.033 1.00 88.09 C
ANISOU 47 CD2 LEU A 177 12906 11381 9185 2391 266 132 C
ATOM 48 N GLY A 178 -41.868 -3.908 33.795 1.00 56.51 N
ANISOU 48 N GLY A 178 8609 7862 5002 1910 -152 269 N
ATOM 49 CA GLY A 178 -40.845 -4.430 32.894 1.00 56.96 C
ANISOU 49 CA GLY A 178 8607 8078 4957 1814 -272 263 C
ATOM 50 C GLY A 178 -39.897 -3.377 32.344 1.00 53.25 C
ANISOU 50 C GLY A 178 8033 7675 4524 1672 -442 178 C
ATOM 51 O GLY A 178 -38.686 -3.595 32.262 1.00 50.83 O
ANISOU 51 O GLY A 178 7730 7528 4055 1673 -545 81 O
ATOM 52 N GLN A 179 -40.440 -2.216 31.984 1.00 51.67 N
ANISOU 52 N GLN A 179 7741 7353 4538 1551 -473 212 N
ATOM 53 CA GLN A 179 -39.641 -1.156 31.386 1.00 46.37 C
ANISOU 53 CA GLN A 179 6961 6731 3926 1402 -634 145 C
ATOM 54 C GLN A 179 -38.863 -0.323 32.411 1.00 45.91 C
ANISOU 54 C GLN A 179 6958 6714 3771 1496 -682 -35 C
ATOM 55 CB GLN A 179 -40.546 -0.235 30.575 1.00 58.07 C
ANISOU 55 CB GLN A 179 8319 8063 5680 1232 -649 256 C
ATOM 56 CG GLN A 179 -41.720 -0.938 29.898 1.00 70.92 C
ANISOU 56 CG GLN A 179 9918 9591 7438 1179 -550 441 C
ATOM 57 CD GLN A 179 -41.297 -2.007 28.907 1.00 76.76 C
ANISOU 57 CD GLN A 179 10617 10447 8100 1104 -596 518 C
ATOM 58 OE1 GLN A 179 -40.247 -1.916 28.268 1.00 78.00 O
ANISOU 58 OE1 GLN A 179 10711 10735 8192 1007 -733 466 O
ATOM 59 NE2 GLN A 179 -42.124 -3.031 28.774 1.00 80.51 N
ANISOU 59 NE2 GLN A 179 11131 10875 8585 1148 -479 642 N
ATOM 60 N ARG A 183 -41.706 6.758 29.305 1.00 37.81 N
ANISOU 60 N ARG A 183 5285 5008 4071 626 -982 199 N
ATOM 61 CA ARG A 183 -41.788 7.095 27.882 1.00 39.60 C
ANISOU 61 CA ARG A 183 5362 5221 4462 402 -1081 303 C
ATOM 62 C ARG A 183 -42.675 6.113 27.127 1.00 44.05 C
ANISOU 62 C ARG A 183 5903 5734 5099 355 -997 478 C
ATOM 63 O ARG A 183 -42.695 6.131 25.887 1.00 44.22 O
ANISOU 63 O ARG A 183 5808 5765 5229 176 -1073 574 O
ATOM 64 CB ARG A 183 -40.404 7.107 27.256 1.00 50.70 C
ANISOU 64 CB ARG A 183 6709 6803 5751 310 -1243 225 C
ATOM 65 CG ARG A 183 -39.395 7.961 28.024 1.00 58.31 C
ANISOU 65 CG ARG A 183 7703 7839 6613 366 -1331 44 C
ATOM 66 CD ARG A 183 -38.216 8.290 27.129 1.00 60.38 C
ANISOU 66 CD ARG A 183 7865 8239 6838 217 -1508 -7 C
ATOM 67 NE ARG A 183 -37.592 7.081 26.590 1.00 52.02 N
ANISOU 67 NE ARG A 183 6816 7325 5625 213 -1533 22 N
ATOM 68 CZ ARG A 183 -36.631 6.404 27.204 1.00 48.20 C
ANISOU 68 CZ ARG A 183 6424 6988 4902 342 -1545 -88 C
ATOM 69 NH1 ARG A 183 -36.198 6.806 28.381 1.00 49.96 N
ANISOU 69 NH1 ARG A 183 6738 7231 5015 485 -1532 -231 N
ATOM 70 NH2 ARG A 183 -36.111 5.323 26.646 1.00 56.81 N
ANISOU 70 NH2 ARG A 183 7515 8204 5866 327 -1570 -53 N
ATOM 71 N PHE A 184 -43.374 5.241 27.852 1.00 40.43 N
ANISOU 71 N PHE A 184 5557 5228 4578 512 -844 518 N
ATOM 72 CA PHE A 184 -44.208 4.215 27.179 1.00 44.52 C
ANISOU 72 CA PHE A 184 6062 5703 5151 480 -758 684 C
ATOM 73 C PHE A 184 -45.601 4.340 27.707 1.00 49.01 C
ANISOU 73 C PHE A 184 6673 6089 5858 549 -608 765 C
ATOM 74 O PHE A 184 -45.800 4.891 28.782 1.00 47.04 O
ANISOU 74 O PHE A 184 6497 5777 5599 669 -553 680 O
ATOM 75 CB PHE A 184 -43.697 2.774 27.425 1.00 36.60 C
ANISOU 75 CB PHE A 184 5154 4836 3918 603 -714 672 C
ATOM 76 CG PHE A 184 -42.322 2.494 26.817 1.00 43.56 C
ANISOU 76 CG PHE A 184 5992 5905 4652 532 -860 604 C
ATOM 77 CD1 PHE A 184 -41.165 2.646 27.565 1.00 46.47 C
ANISOU 77 CD1 PHE A 184 6423 6401 4831 628 -925 436 C
ATOM 78 CD2 PHE A 184 -42.202 2.110 25.482 1.00 39.51 C
ANISOU 78 CD2 PHE A 184 5373 5441 4199 365 -933 709 C
ATOM 79 CE1 PHE A 184 -39.913 2.425 26.995 1.00 49.92 C
ANISOU 79 CE1 PHE A 184 6819 7010 5140 559 -1060 373 C
ATOM 80 CE2 PHE A 184 -40.961 1.893 24.903 1.00 38.13 C
ANISOU 80 CE2 PHE A 184 5154 5436 3898 295 -1068 648 C
ATOM 81 CZ PHE A 184 -39.809 2.033 25.661 1.00 43.05 C
ANISOU 81 CZ PHE A 184 5842 6186 4330 393 -1131 480 C
ATOM 82 N GLN A 185 -46.582 3.830 26.967 1.00 37.95 N
ANISOU 82 N GLN A 185 5720 4674 4024 -134 -616 404 N
ATOM 83 CA GLN A 185 -47.914 3.683 27.539 1.00 34.03 C
ANISOU 83 CA GLN A 185 5302 4236 3393 -251 -608 494 C
ATOM 84 C GLN A 185 -48.362 2.291 27.208 1.00 37.64 C
ANISOU 84 C GLN A 185 5916 4602 3784 -293 -650 570 C
ATOM 85 O GLN A 185 -48.422 1.938 26.039 1.00 36.52 O
ANISOU 85 O GLN A 185 5789 4402 3684 -299 -602 567 O
ATOM 86 CB GLN A 185 -48.890 4.664 26.908 1.00 38.62 C
ANISOU 86 CB GLN A 185 5800 4905 3967 -337 -484 498 C
ATOM 87 CG GLN A 185 -48.883 6.074 27.470 1.00 46.29 C
ANISOU 87 CG GLN A 185 6634 5992 4961 -334 -439 450 C
ATOM 88 CD GLN A 185 -50.067 6.880 26.936 1.00 56.13 C
ANISOU 88 CD GLN A 185 7827 7326 6173 -438 -323 473 C
ATOM 89 OE1 GLN A 185 -51.221 6.585 27.243 1.00 64.94 O
ANISOU 89 OE1 GLN A 185 9023 8476 7177 -539 -314 554 O
ATOM 90 NE2 GLN A 185 -49.783 7.888 26.125 1.00 56.24 N
ANISOU 90 NE2 GLN A 185 7708 7374 6285 -412 -233 402 N
ATOM 91 N VAL A 186 -48.684 1.493 28.220 1.00 36.56 N
ANISOU 91 N VAL A 186 5897 4450 3542 -322 -738 638 N
ATOM 92 CA VAL A 186 -49.138 0.128 27.970 1.00 42.41 C
ANISOU 92 CA VAL A 186 6795 5104 4215 -364 -783 715 C
ATOM 93 C VAL A 186 -50.644 0.104 27.901 1.00 43.33 C
ANISOU 93 C VAL A 186 6966 5275 4223 -499 -726 799 C
ATOM 94 O VAL A 186 -51.317 0.612 28.807 1.00 42.97 O
ANISOU 94 O VAL A 186 6908 5318 4099 -557 -722 833 O
ATOM 95 CB VAL A 186 -48.668 -0.805 29.082 1.00 42.57 C
ANISOU 95 CB VAL A 186 6922 5073 4179 -322 -913 746 C
ATOM 96 CG1 VAL A 186 -49.160 -2.233 28.806 1.00 40.73 C
ANISOU 96 CG1 VAL A 186 6853 4747 3874 -369 -959 828 C
ATOM 97 CG2 VAL A 186 -47.144 -0.721 29.193 1.00 44.86 C
ANISOU 97 CG2 VAL A 186 7151 5313 4579 -186 -970 659 C
ATOM 98 N LEU A 187 -51.191 -0.465 26.825 1.00 38.30 N
ANISOU 98 N LEU A 187 6385 4584 3581 -549 -680 833 N
ATOM 99 CA LEU A 187 -52.618 -0.312 26.581 1.00 41.65 C
ANISOU 99 CA LEU A 187 6838 5067 3921 -676 -607 902 C
ATOM 100 C LEU A 187 -53.187 -1.671 26.356 1.00 46.97 C
ANISOU 100 C LEU A 187 7671 5657 4519 -729 -651 985 C
ATOM 101 O LEU A 187 -52.585 -2.463 25.629 1.00 44.48 O
ANISOU 101 O LEU A 187 7405 5239 4258 -676 -679 969 O
ATOM 102 CB LEU A 187 -52.884 0.508 25.322 1.00 38.01 C
ANISOU 102 CB LEU A 187 6273 4636 3532 -697 -484 859 C
ATOM 103 CG LEU A 187 -52.130 1.832 25.197 1.00 41.91 C
ANISOU 103 CG LEU A 187 6598 5193 4132 -628 -430 760 C
ATOM 104 CD1 LEU A 187 -52.570 2.484 23.901 1.00 44.85 C
ANISOU 104 CD1 LEU A 187 6892 5590 4561 -665 -308 734 C
ATOM 105 CD2 LEU A 187 -52.450 2.715 26.379 1.00 39.44 C
ANISOU 105 CD2 LEU A 187 6227 4992 3766 -655 -434 764 C
ATOM 106 N PRO A 188 -54.351 -1.937 26.974 1.00 55.99 N
ANISOU 106 N PRO A 188 8893 6842 5537 -834 -657 1073 N
ATOM 107 CA PRO A 188 -55.068 -3.202 26.827 1.00 57.44 C
ANISOU 107 CA PRO A 188 9177 6962 5685 -879 -676 1126 C
ATOM 108 C PRO A 188 -55.769 -3.193 25.480 1.00 50.35 C
ANISOU 108 C PRO A 188 8234 6055 4841 -921 -573 1110 C
ATOM 109 O PRO A 188 -56.355 -2.167 25.091 1.00 49.25 O
ANISOU 109 O PRO A 188 7986 6000 4728 -960 -474 1082 O
ATOM 110 CB PRO A 188 -56.112 -3.134 27.950 1.00 60.44 C
ANISOU 110 CB PRO A 188 9508 7428 6029 -927 -660 1137 C
ATOM 111 CG PRO A 188 -56.410 -1.668 28.083 1.00 65.59 C
ANISOU 111 CG PRO A 188 10038 8195 6690 -952 -583 1107 C
ATOM 112 CD PRO A 188 -55.079 -0.986 27.839 1.00 62.08 C
ANISOU 112 CD PRO A 188 9604 7738 6246 -896 -621 1091 C
ATOM 113 N GLY A 189 -55.697 -4.311 24.774 1.00 48.08 N
ANISOU 113 N GLY A 189 8026 5669 4574 -909 -597 1123 N
ATOM 114 CA GLY A 189 -56.423 -4.447 23.524 1.00 44.64 C
ANISOU 114 CA GLY A 189 7550 5222 4188 -945 -509 1106 C
ATOM 115 C GLY A 189 -57.609 -5.394 23.637 1.00 51.04 C
ANISOU 115 C GLY A 189 8368 6034 4990 -990 -500 1119 C
ATOM 116 O GLY A 189 -57.569 -6.397 24.377 1.00 46.15 O
ANISOU 116 O GLY A 189 7829 5372 4333 -982 -579 1149 O
ATOM 117 N ARG A 190 -58.657 -5.074 22.885 1.00 47.95 N
ANISOU 117 N ARG A 190 7892 5691 4638 -1031 -407 1095 N
ATOM 118 CA ARG A 190 -59.830 -5.926 22.742 1.00 50.94 C
ANISOU 118 CA ARG A 190 8270 6066 5018 -1067 -393 1101 C
ATOM 119 C ARG A 190 -59.539 -7.324 22.193 1.00 56.56 C
ANISOU 119 C ARG A 190 9088 6672 5731 -1051 -447 1121 C
ATOM 120 O ARG A 190 -60.416 -8.184 22.230 1.00 58.96 O
ANISOU 120 O ARG A 190 9409 6967 6025 -1080 -452 1132 O
ATOM 121 CB ARG A 190 -60.850 -5.235 21.847 1.00 49.15 C
ANISOU 121 CB ARG A 190 7931 5901 4843 -1094 -291 1062 C
ATOM 122 CG ARG A 190 -61.419 -3.975 22.456 1.00 47.30 C
ANISOU 122 CG ARG A 190 7587 5773 4613 -1110 -238 1040 C
ATOM 123 CD ARG A 190 -62.478 -3.387 21.537 1.00 53.37 C
ANISOU 123 CD ARG A 190 8249 6590 5439 -1123 -148 998 C
ATOM 124 NE ARG A 190 -61.942 -3.231 20.188 1.00 54.53 N
ANISOU 124 NE ARG A 190 8386 6699 5636 -1103 -107 974 N
ATOM 125 CZ ARG A 190 -61.429 -2.097 19.713 1.00 53.65 C
ANISOU 125 CZ ARG A 190 8204 6621 5560 -1086 -52 942 C
ATOM 126 NH1 ARG A 190 -61.399 -1.013 20.472 1.00 51.29 N
ANISOU 126 NH1 ARG A 190 7836 6399 5253 -1089 -33 929 N
ATOM 127 NH2 ARG A 190 -60.955 -2.052 18.473 1.00 54.98 N
ANISOU 127 NH2 ARG A 190 8367 6746 5775 -1067 -14 923 N
ATOM 128 N ASP A 191 -58.337 -7.536 21.659 1.00 56.51 N
ANISOU 128 N ASP A 191 9150 6583 5739 -1003 -486 1122 N
ATOM 129 CA ASP A 191 -57.931 -8.849 21.161 1.00 53.94 C
ANISOU 129 CA ASP A 191 8928 6148 5417 -978 -544 1137 C
ATOM 130 C ASP A 191 -57.162 -9.609 22.241 1.00 58.85 C
ANISOU 130 C ASP A 191 9652 6714 5992 -942 -657 1169 C
ATOM 131 O ASP A 191 -56.422 -10.549 21.947 1.00 60.16 O
ANISOU 131 O ASP A 191 9913 6780 6165 -898 -723 1178 O
ATOM 132 CB ASP A 191 -57.041 -8.688 19.927 1.00 52.69 C
ANISOU 132 CB ASP A 191 8789 5920 5312 -933 -525 1117 C
ATOM 133 CG ASP A 191 -55.799 -7.835 20.196 1.00 45.71 C
ANISOU 133 CG ASP A 191 7916 5019 4432 -879 -554 1112 C
ATOM 134 OD1 ASP A 191 -55.632 -7.312 21.331 1.00 43.91 O
ANISOU 134 OD1 ASP A 191 7676 4846 4163 -878 -587 1123 O
ATOM 135 OD2 ASP A 191 -54.975 -7.686 19.261 1.00 47.35 O
ANISOU 135 OD2 ASP A 191 8146 5158 4688 -832 -544 1096 O
ATOM 136 N LYS A 192 -57.305 -9.156 23.485 1.00 60.32 N
ANISOU 136 N LYS A 192 9815 6967 6136 -954 -679 1182 N
ATOM 137 CA LYS A 192 -56.511 -9.665 24.600 1.00 66.78 C
ANISOU 137 CA LYS A 192 10717 7746 6912 -912 -786 1206 C
ATOM 138 C LYS A 192 -54.980 -9.483 24.489 1.00 69.40 C
ANISOU 138 C LYS A 192 11108 8004 7258 -827 -856 1199 C
ATOM 139 O LYS A 192 -54.239 -10.061 25.290 1.00 77.54 O
ANISOU 139 O LYS A 192 12215 8985 8262 -777 -956 1213 O
ATOM 140 CB LYS A 192 -56.851 -11.135 24.876 1.00 67.89 C
ANISOU 140 CB LYS A 192 10940 7826 7029 -923 -842 1232 C