HEADER RNA BINDING PROTEIN 31-MAR-18 6G63
TITLE RNASE E IN COMPLEX WITH SRNA RRPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE E;
COMPND 3 CHAIN: A, G, L, N;
COMPND 4 SYNONYM: RNASE E;
COMPND 5 EC: 3.1.26.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RNA (5'-
COMPND 10 R(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP
COMPND 11 *U)-3');
COMPND 12 CHAIN: B;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: BECAUSE OF THE LOW RESOLUTION, WE MODELLED THE RNA
COMPND 15 STRUCTURE AS TWO CHAINS IN A DUPLEX OF POLYU:POLYA. THE SEQUENCE OF
COMPND 16 THE RNA USED IN THE CRYSTAL IS
COMPND 17 ACGGUUAUAAAUCAACACAUUGAUUUAUAAGCAUGGAAAUCCCCUGAGUGAAACAACGAAUUGCUGUGU
COMPND 18 GUAGUCUUUGCCCGUCUCCUACGAUGGGCUUUUUUUU
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: RNE, AMS, HMP1, B1084, JW1071;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RNASE E, SMALL REGULATORY RNA, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.B.BANDYRA,B.F.LUISI
REVDAT 3 31-OCT-18 6G63 1 COMPND JRNL
REVDAT 2 10-OCT-18 6G63 1 COMPND JRNL
REVDAT 1 03-OCT-18 6G63 0
JRNL AUTH K.J.BANDYRA,J.M.WANDZIK,B.F.LUISI
JRNL TITL SUBSTRATE RECOGNITION AND AUTOINHIBITION IN THE CENTRAL
JRNL TITL 2 RIBONUCLEASE RNASE E.
JRNL REF MOL. CELL V. 72 275 2018
JRNL REFN ISSN 1097-4164
JRNL PMID 30270108
JRNL DOI 10.1016/J.MOLCEL.2018.08.039
REMARK 2
REMARK 2 RESOLUTION. 3.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 3.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27869
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.275
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 1371
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 19.9469 - 8.3207 0.99 2670 111 0.2270 0.2215
REMARK 3 2 8.3207 - 6.6860 1.00 2658 152 0.3051 0.3431
REMARK 3 3 6.6860 - 5.8654 1.00 2622 154 0.3254 0.3345
REMARK 3 4 5.8654 - 5.3404 1.00 2662 126 0.2830 0.3217
REMARK 3 5 5.3404 - 4.9640 1.00 2672 133 0.2985 0.3813
REMARK 3 6 4.9640 - 4.6753 1.00 2661 129 0.2738 0.2453
REMARK 3 7 4.6753 - 4.4438 1.00 2629 132 0.2517 0.3021
REMARK 3 8 4.4438 - 4.2523 1.00 2643 135 0.2716 0.2892
REMARK 3 9 4.2523 - 4.0901 1.00 2634 152 0.3081 0.2998
REMARK 3 10 4.0901 - 3.9501 1.00 2647 147 0.3655 0.3666
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) : 0.660
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 16451
REMARK 3 ANGLE : 1.012 22300
REMARK 3 CHIRALITY : 0.054 2538
REMARK 3 PLANARITY : 0.008 2847
REMARK 3 DIHEDRAL : 18.794 10141
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.1366 -3.5297 -2.2766
REMARK 3 T TENSOR
REMARK 3 T11: 4.9503 T22: 6.0917
REMARK 3 T33: 3.7841 T12: 0.1100
REMARK 3 T13: 0.3520 T23: 0.7253
REMARK 3 L TENSOR
REMARK 3 L11: 1.6634 L22: -0.6976
REMARK 3 L33: 0.8668 L12: 0.0158
REMARK 3 L13: 0.3904 L23: 0.5893
REMARK 3 S TENSOR
REMARK 3 S11: 1.5849 S12: 1.7710 S13: 0.6233
REMARK 3 S21: 0.5390 S22: 0.5395 S23: 0.5887
REMARK 3 S31: -1.2919 S32: -1.5827 S33: -1.2074
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 33 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4995 33.6122 0.0835
REMARK 3 T TENSOR
REMARK 3 T11: 5.4235 T22: 3.6951
REMARK 3 T33: 3.9791 T12: 0.5900
REMARK 3 T13: -0.0882 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.3227 L22: 1.5322
REMARK 3 L33: 0.4596 L12: 1.6360
REMARK 3 L13: -0.9381 L23: 0.0460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1533 S12: -0.4705 S13: 1.0435
REMARK 3 S21: 0.9115 S22: 1.1554 S23: -0.6835
REMARK 3 S31: -2.2618 S32: 0.7148 S33: -0.5307
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 33 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8660 -47.4112 -33.5190
REMARK 3 T TENSOR
REMARK 3 T11: 3.8096 T22: 4.6817
REMARK 3 T33: 4.1466 T12: 0.1192
REMARK 3 T13: 0.0784 T23: 0.2730
REMARK 3 L TENSOR
REMARK 3 L11: 1.6318 L22: 0.9405
REMARK 3 L33: 2.5754 L12: 0.4034
REMARK 3 L13: -1.1364 L23: 0.5738
REMARK 3 S TENSOR
REMARK 3 S11: -0.5726 S12: -1.8932 S13: -1.1136
REMARK 3 S21: -1.3506 S22: 0.2855 S23: -0.7075
REMARK 3 S31: -0.2368 S32: 2.1654 S33: -0.2757
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'N' AND (RESID 33 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4411 -56.8764 31.4593
REMARK 3 T TENSOR
REMARK 3 T11: 3.9373 T22: 3.1614
REMARK 3 T33: 3.8884 T12: -0.2239
REMARK 3 T13: -0.1350 T23: 0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 1.3451 L22: 1.1735
REMARK 3 L33: 5.3279 L12: 1.3608
REMARK 3 L13: 1.1002 L23: 0.3246
REMARK 3 S TENSOR
REMARK 3 S11: -1.0795 S12: -0.2169 S13: 1.0413
REMARK 3 S21: -1.4572 S22: -0.6462 S23: 0.0945
REMARK 3 S31: 2.1816 S32: -0.0503 S33: 1.2683
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2825 -2.1493 -22.6854
REMARK 3 T TENSOR
REMARK 3 T11: 2.5343 T22: 1.9653
REMARK 3 T33: 2.1197 T12: 0.8272
REMARK 3 T13: -0.6389 T23: 0.2066
REMARK 3 L TENSOR
REMARK 3 L11: 2.5248 L22: 3.1365
REMARK 3 L33: 2.5494 L12: -0.3902
REMARK 3 L13: 0.6129 L23: 1.7016
REMARK 3 S TENSOR
REMARK 3 S11: -1.2712 S12: -0.0816 S13: -0.5912
REMARK 3 S21: -0.3246 S22: 1.0872 S23: -0.0082
REMARK 3 S31: 0.6999 S32: -1.9356 S33: -0.6238
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4093 3.6202 -5.1581
REMARK 3 T TENSOR
REMARK 3 T11: 2.0074 T22: 1.4427
REMARK 3 T33: 1.3576 T12: 0.8750
REMARK 3 T13: -0.0779 T23: -0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 3.0552 L22: 2.6356
REMARK 3 L33: 3.8465 L12: -0.9954
REMARK 3 L13: 2.4902 L23: 0.0260
REMARK 3 S TENSOR
REMARK 3 S11: 0.3037 S12: -0.4402 S13: -0.1908
REMARK 3 S21: -0.7594 S22: 0.2695 S23: 0.7102
REMARK 3 S31: -0.5869 S32: -1.4269 S33: -0.3641
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 3 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4964 15.5036 20.5746
REMARK 3 T TENSOR
REMARK 3 T11: 2.5576 T22: 1.5959
REMARK 3 T33: 2.9192 T12: 0.8985
REMARK 3 T13: -0.3465 T23: -0.8801
REMARK 3 L TENSOR
REMARK 3 L11: 3.1270 L22: 2.7930
REMARK 3 L33: 4.7764 L12: -1.1971
REMARK 3 L13: 0.6762 L23: -1.8119
REMARK 3 S TENSOR
REMARK 3 S11: -0.0423 S12: -0.3856 S13: -0.3588
REMARK 3 S21: -1.2107 S22: -0.2780 S23: -0.2062
REMARK 3 S31: 0.0413 S32: 2.6063 S33: -0.8128
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 212 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4472 8.2362 2.9218
REMARK 3 T TENSOR
REMARK 3 T11: 2.5461 T22: 1.0035
REMARK 3 T33: 1.6027 T12: 0.8306
REMARK 3 T13: -0.3111 T23: 0.0703
REMARK 3 L TENSOR
REMARK 3 L11: 1.8942 L22: 4.6275
REMARK 3 L33: 4.9304 L12: -0.1427
REMARK 3 L13: -0.6475 L23: 2.6574
REMARK 3 S TENSOR
REMARK 3 S11: 0.1442 S12: -0.0488 S13: 0.2714
REMARK 3 S21: -0.5157 S22: 0.4897 S23: -0.6134
REMARK 3 S31: -1.1950 S32: -0.2270 S33: -0.4666
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 3 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0246 -47.2181 -25.2733
REMARK 3 T TENSOR
REMARK 3 T11: 3.2880 T22: 1.5657
REMARK 3 T33: 1.5147 T12: 0.8970
REMARK 3 T13: -0.5902 T23: -0.3338
REMARK 3 L TENSOR
REMARK 3 L11: 4.2334 L22: 8.1108
REMARK 3 L33: 4.2097 L12: 0.1052
REMARK 3 L13: -0.4566 L23: 1.2868
REMARK 3 S TENSOR
REMARK 3 S11: 0.4277 S12: 0.1012 S13: 0.3942
REMARK 3 S21: -0.5063 S22: -0.0754 S23: 1.1385
REMARK 3 S31: 0.8147 S32: 0.4390 S33: 0.1796
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 212 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7469 -40.0418 -6.9050
REMARK 3 T TENSOR
REMARK 3 T11: 2.0058 T22: 1.2532
REMARK 3 T33: 1.3301 T12: 0.7614
REMARK 3 T13: -0.3632 T23: -0.1934
REMARK 3 L TENSOR
REMARK 3 L11: 1.2652 L22: 2.4453
REMARK 3 L33: 3.1930 L12: 1.5252
REMARK 3 L13: 0.5694 L23: 1.2732
REMARK 3 S TENSOR
REMARK 3 S11: -0.0846 S12: 0.0309 S13: -0.1893
REMARK 3 S21: -0.1331 S22: 0.4678 S23: -0.1440
REMARK 3 S31: 0.4808 S32: 0.1792 S33: -0.4041
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'N' AND (RESID 3 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1008 -32.2331 22.9302
REMARK 3 T TENSOR
REMARK 3 T11: 2.7862 T22: 2.0039
REMARK 3 T33: 1.5131 T12: 1.1169
REMARK 3 T13: -0.0206 T23: -0.2273
REMARK 3 L TENSOR
REMARK 3 L11: 2.0379 L22: 2.7129
REMARK 3 L33: 5.6749 L12: -0.8929
REMARK 3 L13: 1.8549 L23: 1.2636
REMARK 3 S TENSOR
REMARK 3 S11: 0.3074 S12: 0.9754 S13: 0.9280
REMARK 3 S21: 0.9977 S22: 0.6178 S23: -1.1356
REMARK 3 S31: 1.2627 S32: 0.9573 S33: -0.7114
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'N' AND (RESID 212 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4986 -37.8872 4.6067
REMARK 3 T TENSOR
REMARK 3 T11: 2.1143 T22: 1.1246
REMARK 3 T33: 1.3173 T12: 0.6658
REMARK 3 T13: -0.1894 T23: -0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 3.1684 L22: 1.0161
REMARK 3 L33: 3.2975 L12: 0.4106
REMARK 3 L13: 1.9674 L23: 1.1229
REMARK 3 S TENSOR
REMARK 3 S11: 0.3765 S12: -0.4314 S13: -0.4538
REMARK 3 S21: -0.0788 S22: 0.2805 S23: -0.2746
REMARK 3 S31: 0.4323 S32: 0.2385 S33: -0.5488
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 6G63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER R 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28217
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.950
REMARK 200 RESOLUTION RANGE LOW (A) : 95.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.19
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M KCL, 0.01 M MGCL2, 0.05 M TRIS
REMARK 280 -HCL PH 8.5 AND 30% (V/V) PEG 400, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 155.34000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 310.68000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 233.01000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 388.35000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.67000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 102260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, L, N, 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 MET A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 51
REMARK 465 SER A 52
REMARK 465 LEU A 53
REMARK 465 ALA A 80
REMARK 465 ASN A 81
REMARK 465 TYR A 82
REMARK 465 SER A 83
REMARK 465 ALA A 84
REMARK 465 HIS A 85
REMARK 465 GLY A 86
REMARK 465 ASN A 132
REMARK 465 ASN A 133
REMARK 465 PRO A 134
REMARK 465 ARG A 135
REMARK 465 PRO G 51
REMARK 465 SER G 52
REMARK 465 LEU G 53
REMARK 465 ALA G 80
REMARK 465 ASN G 81
REMARK 465 TYR G 82
REMARK 465 SER G 83
REMARK 465 ALA G 84
REMARK 465 HIS G 85
REMARK 465 GLY G 86
REMARK 465 ARG G 142
REMARK 465 ILE G 143
REMARK 465 GLU G 144
REMARK 465 GLU G 159
REMARK 465 LEU G 160
REMARK 465 PRO G 161
REMARK 465 GLU G 162
REMARK 465 ALA L 80
REMARK 465 ASN L 81
REMARK 465 TYR L 82
REMARK 465 SER L 83
REMARK 465 ALA L 84
REMARK 465 HIS L 85
REMARK 465 GLY L 86
REMARK 465 GLU L 144
REMARK 465 GLY L 145
REMARK 465 ASP L 146
REMARK 465 ASP L 147
REMARK 465 ARG L 148
REMARK 465 THR L 149
REMARK 465 ALA L 309
REMARK 465 THR L 310
REMARK 465 ARG L 311
REMARK 465 GLY L 312
REMARK 465 ALA N 80
REMARK 465 ASN N 81
REMARK 465 TYR N 82
REMARK 465 SER N 83
REMARK 465 ALA N 84
REMARK 465 HIS N 85
REMARK 465 GLY N 86
REMARK 465 GLU N 144
REMARK 465 GLY N 145
REMARK 465 ASP N 146
REMARK 465 ASP N 147
REMARK 465 ARG N 148
REMARK 465 THR N 149
REMARK 465 ARG N 311
REMARK 465 GLY N 312
REMARK 465 GLY N 313
REMARK 465 N B 12
REMARK 465 N B 13
REMARK 465 N B 14
REMARK 465 N B 15
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 ILE A 214 CG1 CG2 CD1
REMARK 470 VAL A 215 CG1 CG2
REMARK 470 ILE G 214 CG1 CG2 CD1
REMARK 470 VAL G 215 CG1 CG2
REMARK 470 ILE L 214 CG1 CG2 CD1
REMARK 470 VAL L 215 CG1 CG2
REMARK 470 ILE N 214 CG1 CG2 CD1
REMARK 470 VAL N 215 CG1 CG2
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 N 28 HH TYR N 221 1.37
REMARK 500 HZ3 LYS A 38 O GLN A 209 1.57
REMARK 500 O PHE N 218 H LEU N 222 1.57
REMARK 500 H GLY A 124 O LEU A 127 1.58
REMARK 500 O ARG N 219 HH21 ARG N 371 1.59
REMARK 500 OD1 ASP N 28 OH TYR N 221 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH22 ARG A 3 OP1 U B 26 5554 1.38
REMARK 500 NH2 ARG A 3 OP1 U B 26 5554 1.91
REMARK 500 NE2 GLN A 22 O2' U B 24 5554 1.97
REMARK 500 N ARG A 3 O3' U B 26 5554 2.10
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 VAL L 353 CB VAL L 353 CG1 -0.156
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 G 357 CG - CD - NE ANGL. DEV. = -13.1 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 ALA A 8 11.12 -145.35
REMARK 500 ASP A 20 -73.62 -95.89
REMARK 500 HIS A 34 23.32 -145.92
REMARK 500 LYS A 37 -79.11 -68.60
REMARK 500 GLU A 108 62.00 63.84
REMARK 500 GLU A 159 45.25 -93.76
REMARK 500 GLN A 209 -136.10 41.44
REMARK 500 SER A 211 26.33 -160.01
REMARK 500 ASN A 212 109.65 -55.12
REMARK 500 LEU A 247 3.21 -68.73
REMARK 500 ARG A 311 55.94 34.07
REMARK 500 ASN A 435 18.84 55.53
REMARK 500 ASN A 453 -60.20 -129.39
REMARK 500 GLU A 494 154.67 -49.77
REMARK 500 HIS G 34 -116.82 44.59
REMARK 500 LYS G 37 46.32 -73.44
REMARK 500 ALA G 39 18.27 57.00
REMARK 500 MET G 130 71.09 -110.97
REMARK 500 TYR G 221 -12.77 -143.75
REMARK 500 LEU G 247 8.28 -68.56
REMARK 500 ALA G 298 -1.98 -141.86
REMARK 500 ASN G 453 -64.67 -130.51
REMARK 500 THR G 481 -60.28 -25.38
REMARK 500 HIS L 34 43.52 -73.04
REMARK 500 GLN L 36 75.38 -104.35
REMARK 500 ALA L 39 14.31 -161.18
REMARK 500 MET L 130 69.75 -114.28
REMARK 500 SER L 140 131.45 -37.93
REMARK 500 GLU L 159 41.46 -85.56
REMARK 500 PRO L 202 -169.02 -59.83
REMARK 500 ALA L 203 -78.18 -73.45
REMARK 500 THR L 296 -168.84 -109.54
REMARK 500 ALA L 298 -7.16 -144.76
REMARK 500 ASN L 435 18.85 57.53
REMARK 500 ASN L 453 -68.30 -124.29
REMARK 500 ALA N 39 19.73 52.47
REMARK 500 MET N 130 71.24 -114.64
REMARK 500 GLU N 159 42.41 -84.63
REMARK 500 ALA N 171 -9.99 -59.02
REMARK 500 ARG N 249 52.93 -115.78
REMARK 500 THR N 296 -167.85 -112.28
REMARK 500 ALA N 298 -7.38 -144.57
REMARK 500 ARG N 406 -60.67 -91.12
REMARK 500 ASN N 435 19.24 59.72
REMARK 500 ASN N 453 -61.83 -130.05
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 ASN L 212 VAL L 213 -149.70
REMARK 500 GLU N 210 SER N 211 -147.73
REMARK 500
REMARK 500 REMARK: NULL
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 U N 601
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 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 404 SG
REMARK 620 2 CYS A 407 SG 94.4
REMARK 620 3 CYS G 404 SG 126.4 106.5
REMARK 620 4 CYS G 407 SG 109.0 120.9 101.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 404 SG
REMARK 620 2 CYS L 407 SG 96.1
REMARK 620 3 CYS N 404 SG 132.1 120.6
REMARK 620 4 CYS N 407 SG 112.8 101.0 90.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue U N 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F6C RELATED DB: PDB
DBREF 6G63 A 1 510 UNP P21513 RNE_ECOLI 1 510
DBREF 6G63 G 1 510 UNP P21513 RNE_ECOLI 1 510
DBREF 6G63 L 1 510 UNP P21513 RNE_ECOLI 1 510
DBREF 6G63 N 1 510 UNP P21513 RNE_ECOLI 1 510
DBREF 6G63 B 0 26 PDB 6G63 6G63 0 26
SEQADV 6G63 ARG A 303 UNP P21513 ASP 303 ENGINEERED MUTATION
SEQADV 6G63 ARG A 346 UNP P21513 ASP 346 ENGINEERED MUTATION
SEQADV 6G63 ARG G 303 UNP P21513 ASP 303 ENGINEERED MUTATION
SEQADV 6G63 ARG G 346 UNP P21513 ASP 346 ENGINEERED MUTATION
SEQADV 6G63 ARG L 303 UNP P21513 ASP 303 ENGINEERED MUTATION
SEQADV 6G63 ARG L 346 UNP P21513 ASP 346 ENGINEERED MUTATION
SEQADV 6G63 ARG N 303 UNP P21513 ASP 303 ENGINEERED MUTATION
SEQADV 6G63 ARG N 346 UNP P21513 ASP 346 ENGINEERED MUTATION
SEQRES 1 A 510 MET LYS ARG MET LEU ILE ASN ALA THR GLN GLN GLU GLU
SEQRES 2 A 510 LEU ARG VAL ALA LEU VAL ASP GLY GLN ARG LEU TYR ASP
SEQRES 3 A 510 LEU ASP ILE GLU SER PRO GLY HIS GLU GLN LYS LYS ALA
SEQRES 4 A 510 ASN ILE TYR LYS GLY LYS ILE THR ARG ILE GLU PRO SER
SEQRES 5 A 510 LEU GLU ALA ALA PHE VAL ASP TYR GLY ALA GLU ARG HIS
SEQRES 6 A 510 GLY PHE LEU PRO LEU LYS GLU ILE ALA ARG GLU TYR PHE
SEQRES 7 A 510 PRO ALA ASN TYR SER ALA HIS GLY ARG PRO ASN ILE LYS
SEQRES 8 A 510 ASP VAL LEU ARG GLU GLY GLN GLU VAL ILE VAL GLN ILE
SEQRES 9 A 510 ASP LYS GLU GLU ARG GLY ASN LYS GLY ALA ALA LEU THR
SEQRES 10 A 510 THR PHE ILE SER LEU ALA GLY SER TYR LEU VAL LEU MET
SEQRES 11 A 510 PRO ASN ASN PRO ARG ALA GLY GLY ILE SER ARG ARG ILE
SEQRES 12 A 510 GLU GLY ASP ASP ARG THR GLU LEU LYS GLU ALA LEU ALA
SEQRES 13 A 510 SER LEU GLU LEU PRO GLU GLY MET GLY LEU ILE VAL ARG
SEQRES 14 A 510 THR ALA GLY VAL GLY LYS SER ALA GLU ALA LEU GLN TRP
SEQRES 15 A 510 ASP LEU SER PHE ARG LEU LYS HIS TRP GLU ALA ILE LYS
SEQRES 16 A 510 LYS ALA ALA GLU SER ARG PRO ALA PRO PHE LEU ILE HIS
SEQRES 17 A 510 GLN GLU SER ASN VAL ILE VAL ARG ALA PHE ARG ASP TYR
SEQRES 18 A 510 LEU ARG GLN ASP ILE GLY GLU ILE LEU ILE ASP ASN PRO
SEQRES 19 A 510 LYS VAL LEU GLU LEU ALA ARG GLN HIS ILE ALA ALA LEU
SEQRES 20 A 510 GLY ARG PRO ASP PHE SER SER LYS ILE LYS LEU TYR THR
SEQRES 21 A 510 GLY GLU ILE PRO LEU PHE SER HIS TYR GLN ILE GLU SER
SEQRES 22 A 510 GLN ILE GLU SER ALA PHE GLN ARG GLU VAL ARG LEU PRO
SEQRES 23 A 510 SER GLY GLY SER ILE VAL ILE ASP SER THR GLU ALA LEU
SEQRES 24 A 510 THR ALA ILE ARG ILE ASN SER ALA ARG ALA THR ARG GLY
SEQRES 25 A 510 GLY ASP ILE GLU GLU THR ALA PHE ASN THR ASN LEU GLU
SEQRES 26 A 510 ALA ALA ASP GLU ILE ALA ARG GLN LEU ARG LEU ARG ASP
SEQRES 27 A 510 LEU GLY GLY LEU ILE VAL ILE ARG PHE ILE ASP MET THR
SEQRES 28 A 510 PRO VAL ARG HIS GLN ARG ALA VAL GLU ASN ARG LEU ARG
SEQRES 29 A 510 GLU ALA VAL ARG GLN ASP ARG ALA ARG ILE GLN ILE SER
SEQRES 30 A 510 HIS ILE SER ARG PHE GLY LEU LEU GLU MET SER ARG GLN
SEQRES 31 A 510 ARG LEU SER PRO SER LEU GLY GLU SER SER HIS HIS VAL
SEQRES 32 A 510 CYS PRO ARG CYS SER GLY THR GLY THR VAL ARG ASP ASN
SEQRES 33 A 510 GLU SER LEU SER LEU SER ILE LEU ARG LEU ILE GLU GLU
SEQRES 34 A 510 GLU ALA LEU LYS GLU ASN THR GLN GLU VAL HIS ALA ILE
SEQRES 35 A 510 VAL PRO VAL PRO ILE ALA SER TYR LEU LEU ASN GLU LYS
SEQRES 36 A 510 ARG SER ALA VAL ASN ALA ILE GLU THR ARG GLN ASP GLY
SEQRES 37 A 510 VAL ARG CYS VAL ILE VAL PRO ASN ASP GLN MET GLU THR
SEQRES 38 A 510 PRO HIS TYR HIS VAL LEU ARG VAL ARG LYS GLY GLU GLU
SEQRES 39 A 510 THR PRO THR LEU SER TYR MET LEU PRO LYS LEU HIS GLU
SEQRES 40 A 510 GLU ALA MET
SEQRES 1 G 510 MET LYS ARG MET LEU ILE ASN ALA THR GLN GLN GLU GLU
SEQRES 2 G 510 LEU ARG VAL ALA LEU VAL ASP GLY GLN ARG LEU TYR ASP
SEQRES 3 G 510 LEU ASP ILE GLU SER PRO GLY HIS GLU GLN LYS LYS ALA
SEQRES 4 G 510 ASN ILE TYR LYS GLY LYS ILE THR ARG ILE GLU PRO SER
SEQRES 5 G 510 LEU GLU ALA ALA PHE VAL ASP TYR GLY ALA GLU ARG HIS
SEQRES 6 G 510 GLY PHE LEU PRO LEU LYS GLU ILE ALA ARG GLU TYR PHE
SEQRES 7 G 510 PRO ALA ASN TYR SER ALA HIS GLY ARG PRO ASN ILE LYS
SEQRES 8 G 510 ASP VAL LEU ARG GLU GLY GLN GLU VAL ILE VAL GLN ILE
SEQRES 9 G 510 ASP LYS GLU GLU ARG GLY ASN LYS GLY ALA ALA LEU THR
SEQRES 10 G 510 THR PHE ILE SER LEU ALA GLY SER TYR LEU VAL LEU MET
SEQRES 11 G 510 PRO ASN ASN PRO ARG ALA GLY GLY ILE SER ARG ARG ILE
SEQRES 12 G 510 GLU GLY ASP ASP ARG THR GLU LEU LYS GLU ALA LEU ALA
SEQRES 13 G 510 SER LEU GLU LEU PRO GLU GLY MET GLY LEU ILE VAL ARG
SEQRES 14 G 510 THR ALA GLY VAL GLY LYS SER ALA GLU ALA LEU GLN TRP
SEQRES 15 G 510 ASP LEU SER PHE ARG LEU LYS HIS TRP GLU ALA ILE LYS
SEQRES 16 G 510 LYS ALA ALA GLU SER ARG PRO ALA PRO PHE LEU ILE HIS
SEQRES 17 G 510 GLN GLU SER ASN VAL ILE VAL ARG ALA PHE ARG ASP TYR
SEQRES 18 G 510 LEU ARG GLN ASP ILE GLY GLU ILE LEU ILE ASP ASN PRO
SEQRES 19 G 510 LYS VAL LEU GLU LEU ALA ARG GLN HIS ILE ALA ALA LEU
SEQRES 20 G 510 GLY ARG PRO ASP PHE SER SER LYS ILE LYS LEU TYR THR
SEQRES 21 G 510 GLY GLU ILE PRO LEU PHE SER HIS TYR GLN ILE GLU SER
SEQRES 22 G 510 GLN ILE GLU SER ALA PHE GLN ARG GLU VAL ARG LEU PRO
SEQRES 23 G 510 SER GLY GLY SER ILE VAL ILE ASP SER THR GLU ALA LEU
SEQRES 24 G 510 THR ALA ILE ARG ILE ASN SER ALA ARG ALA THR ARG GLY
SEQRES 25 G 510 GLY ASP ILE GLU GLU THR ALA PHE ASN THR ASN LEU GLU
SEQRES 26 G 510 ALA ALA ASP GLU ILE ALA ARG GLN LEU ARG LEU ARG ASP
SEQRES 27 G 510 LEU GLY GLY LEU ILE VAL ILE ARG PHE ILE ASP MET THR
SEQRES 28 G 510 PRO VAL ARG HIS GLN ARG ALA VAL GLU ASN ARG LEU ARG
SEQRES 29 G 510 GLU ALA VAL ARG GLN ASP ARG ALA ARG ILE GLN ILE SER
SEQRES 30 G 510 HIS ILE SER ARG PHE GLY LEU LEU GLU MET SER ARG GLN
SEQRES 31 G 510 ARG LEU SER PRO SER LEU GLY GLU SER SER HIS HIS VAL
SEQRES 32 G 510 CYS PRO ARG CYS SER GLY THR GLY THR VAL ARG ASP ASN
SEQRES 33 G 510 GLU SER LEU SER LEU SER ILE LEU ARG LEU ILE GLU GLU
SEQRES 34 G 510 GLU ALA LEU LYS GLU ASN THR GLN GLU VAL HIS ALA ILE
SEQRES 35 G 510 VAL PRO VAL PRO ILE ALA SER TYR LEU LEU ASN GLU LYS
SEQRES 36 G 510 ARG SER ALA VAL ASN ALA ILE GLU THR ARG GLN ASP GLY
SEQRES 37 G 510 VAL ARG CYS VAL ILE VAL PRO ASN ASP GLN MET GLU THR
SEQRES 38 G 510 PRO HIS TYR HIS VAL LEU ARG VAL ARG LYS GLY GLU GLU
SEQRES 39 G 510 THR PRO THR LEU SER TYR MET LEU PRO LYS LEU HIS GLU
SEQRES 40 G 510 GLU ALA MET
SEQRES 1 L 510 MET LYS ARG MET LEU ILE ASN ALA THR GLN GLN GLU GLU
SEQRES 2 L 510 LEU ARG VAL ALA LEU VAL ASP GLY GLN ARG LEU TYR ASP
SEQRES 3 L 510 LEU ASP ILE GLU SER PRO GLY HIS GLU GLN LYS LYS ALA
SEQRES 4 L 510 ASN ILE TYR LYS GLY LYS ILE THR ARG ILE GLU PRO SER
SEQRES 5 L 510 LEU GLU ALA ALA PHE VAL ASP TYR GLY ALA GLU ARG HIS
SEQRES 6 L 510 GLY PHE LEU PRO LEU LYS GLU ILE ALA ARG GLU TYR PHE
SEQRES 7 L 510 PRO ALA ASN TYR SER ALA HIS GLY ARG PRO ASN ILE LYS
SEQRES 8 L 510 ASP VAL LEU ARG GLU GLY GLN GLU VAL ILE VAL GLN ILE
SEQRES 9 L 510 ASP LYS GLU GLU ARG GLY ASN LYS GLY ALA ALA LEU THR
SEQRES 10 L 510 THR PHE ILE SER LEU ALA GLY SER TYR LEU VAL LEU MET
SEQRES 11 L 510 PRO ASN ASN PRO ARG ALA GLY GLY ILE SER ARG ARG ILE
SEQRES 12 L 510 GLU GLY ASP ASP ARG THR GLU LEU LYS GLU ALA LEU ALA
SEQRES 13 L 510 SER LEU GLU LEU PRO GLU GLY MET GLY LEU ILE VAL ARG
SEQRES 14 L 510 THR ALA GLY VAL GLY LYS SER ALA GLU ALA LEU GLN TRP
SEQRES 15 L 510 ASP LEU SER PHE ARG LEU LYS HIS TRP GLU ALA ILE LYS
SEQRES 16 L 510 LYS ALA ALA GLU SER ARG PRO ALA PRO PHE LEU ILE HIS
SEQRES 17 L 510 GLN GLU SER ASN VAL ILE VAL ARG ALA PHE ARG ASP TYR
SEQRES 18 L 510 LEU ARG GLN ASP ILE GLY GLU ILE LEU ILE ASP ASN PRO
SEQRES 19 L 510 LYS VAL LEU GLU LEU ALA ARG GLN HIS ILE ALA ALA LEU
SEQRES 20 L 510 GLY ARG PRO ASP PHE SER SER LYS ILE LYS LEU TYR THR
SEQRES 21 L 510 GLY GLU ILE PRO LEU PHE SER HIS TYR GLN ILE GLU SER
SEQRES 22 L 510 GLN ILE GLU SER ALA PHE GLN ARG GLU VAL ARG LEU PRO
SEQRES 23 L 510 SER GLY GLY SER ILE VAL ILE ASP SER THR GLU ALA LEU
SEQRES 24 L 510 THR ALA ILE ARG ILE ASN SER ALA ARG ALA THR ARG GLY
SEQRES 25 L 510 GLY ASP ILE GLU GLU THR ALA PHE ASN THR ASN LEU GLU
SEQRES 26 L 510 ALA ALA ASP GLU ILE ALA ARG GLN LEU ARG LEU ARG ASP
SEQRES 27 L 510 LEU GLY GLY LEU ILE VAL ILE ARG PHE ILE ASP MET THR
SEQRES 28 L 510 PRO VAL ARG HIS GLN ARG ALA VAL GLU ASN ARG LEU ARG
SEQRES 29 L 510 GLU ALA VAL ARG GLN ASP ARG ALA ARG ILE GLN ILE SER
SEQRES 30 L 510 HIS ILE SER ARG PHE GLY LEU LEU GLU MET SER ARG GLN
SEQRES 31 L 510 ARG LEU SER PRO SER LEU GLY GLU SER SER HIS HIS VAL
SEQRES 32 L 510 CYS PRO ARG CYS SER GLY THR GLY THR VAL ARG ASP ASN
SEQRES 33 L 510 GLU SER LEU SER LEU SER ILE LEU ARG LEU ILE GLU GLU
SEQRES 34 L 510 GLU ALA LEU LYS GLU ASN THR GLN GLU VAL HIS ALA ILE
SEQRES 35 L 510 VAL PRO VAL PRO ILE ALA SER TYR LEU LEU ASN GLU LYS
SEQRES 36 L 510 ARG SER ALA VAL ASN ALA ILE GLU THR ARG GLN ASP GLY
SEQRES 37 L 510 VAL ARG CYS VAL ILE VAL PRO ASN ASP GLN MET GLU THR
SEQRES 38 L 510 PRO HIS TYR HIS VAL LEU ARG VAL ARG LYS GLY GLU GLU
SEQRES 39 L 510 THR PRO THR LEU SER TYR MET LEU PRO LYS LEU HIS GLU
SEQRES 40 L 510 GLU ALA MET
SEQRES 1 N 510 MET LYS ARG MET LEU ILE ASN ALA THR GLN GLN GLU GLU
SEQRES 2 N 510 LEU ARG VAL ALA LEU VAL ASP GLY GLN ARG LEU TYR ASP
SEQRES 3 N 510 LEU ASP ILE GLU SER PRO GLY HIS GLU GLN LYS LYS ALA
SEQRES 4 N 510 ASN ILE TYR LYS GLY LYS ILE THR ARG ILE GLU PRO SER
SEQRES 5 N 510 LEU GLU ALA ALA PHE VAL ASP TYR GLY ALA GLU ARG HIS
SEQRES 6 N 510 GLY PHE LEU PRO LEU LYS GLU ILE ALA ARG GLU TYR PHE
SEQRES 7 N 510 PRO ALA ASN TYR SER ALA HIS GLY ARG PRO ASN ILE LYS
SEQRES 8 N 510 ASP VAL LEU ARG GLU GLY GLN GLU VAL ILE VAL GLN ILE
SEQRES 9 N 510 ASP LYS GLU GLU ARG GLY ASN LYS GLY ALA ALA LEU THR
SEQRES 10 N 510 THR PHE ILE SER LEU ALA GLY SER TYR LEU VAL LEU MET
SEQRES 11 N 510 PRO ASN ASN PRO ARG ALA GLY GLY ILE SER ARG ARG ILE
SEQRES 12 N 510 GLU GLY ASP ASP ARG THR GLU LEU LYS GLU ALA LEU ALA
SEQRES 13 N 510 SER LEU GLU LEU PRO GLU GLY MET GLY LEU ILE VAL ARG
SEQRES 14 N 510 THR ALA GLY VAL GLY LYS SER ALA GLU ALA LEU GLN TRP
SEQRES 15 N 510 ASP LEU SER PHE ARG LEU LYS HIS TRP GLU ALA ILE LYS
SEQRES 16 N 510 LYS ALA ALA GLU SER ARG PRO ALA PRO PHE LEU ILE HIS
SEQRES 17 N 510 GLN GLU SER ASN VAL ILE VAL ARG ALA PHE ARG ASP TYR
SEQRES 18 N 510 LEU ARG GLN ASP ILE GLY GLU ILE LEU ILE ASP ASN PRO
SEQRES 19 N 510 LYS VAL LEU GLU LEU ALA ARG GLN HIS ILE ALA ALA LEU
SEQRES 20 N 510 GLY ARG PRO ASP PHE SER SER LYS ILE LYS LEU TYR THR
SEQRES 21 N 510 GLY GLU ILE PRO LEU PHE SER HIS TYR GLN ILE GLU SER
SEQRES 22 N 510 GLN ILE GLU SER ALA PHE GLN ARG GLU VAL ARG LEU PRO
SEQRES 23 N 510 SER GLY GLY SER ILE VAL ILE ASP SER THR GLU ALA LEU
SEQRES 24 N 510 THR ALA ILE ARG ILE ASN SER ALA ARG ALA THR ARG GLY
SEQRES 25 N 510 GLY ASP ILE GLU GLU THR ALA PHE ASN THR ASN LEU GLU
SEQRES 26 N 510 ALA ALA ASP GLU ILE ALA ARG GLN LEU ARG LEU ARG ASP
SEQRES 27 N 510 LEU GLY GLY LEU ILE VAL ILE ARG PHE ILE ASP MET THR
SEQRES 28 N 510 PRO VAL ARG HIS GLN ARG ALA VAL GLU ASN ARG LEU ARG
SEQRES 29 N 510 GLU ALA VAL ARG GLN ASP ARG ALA ARG ILE GLN ILE SER
SEQRES 30 N 510 HIS ILE SER ARG PHE GLY LEU LEU GLU MET SER ARG GLN
SEQRES 31 N 510 ARG LEU SER PRO SER LEU GLY GLU SER SER HIS HIS VAL
SEQRES 32 N 510 CYS PRO ARG CYS SER GLY THR GLY THR VAL ARG ASP ASN
SEQRES 33 N 510 GLU SER LEU SER LEU SER ILE LEU ARG LEU ILE GLU GLU
SEQRES 34 N 510 GLU ALA LEU LYS GLU ASN THR GLN GLU VAL HIS ALA ILE
SEQRES 35 N 510 VAL PRO VAL PRO ILE ALA SER TYR LEU LEU ASN GLU LYS
SEQRES 36 N 510 ARG SER ALA VAL ASN ALA ILE GLU THR ARG GLN ASP GLY
SEQRES 37 N 510 VAL ARG CYS VAL ILE VAL PRO ASN ASP GLN MET GLU THR
SEQRES 38 N 510 PRO HIS TYR HIS VAL LEU ARG VAL ARG LYS GLY GLU GLU
SEQRES 39 N 510 THR PRO THR LEU SER TYR MET LEU PRO LYS LEU HIS GLU
SEQRES 40 N 510 GLU ALA MET
SEQRES 1 B 27 A A A A A A A A A A A A N
SEQRES 2 B 27 N N N U U U U U U U U U U
SEQRES 3 B 27 U
HET ZN A 601 1
HET ZN L 601 1
HET U N 601 31
HETNAM ZN ZINC ION
HETNAM U URIDINE-5'-MONOPHOSPHATE
FORMUL 6 ZN 2(ZN 2+)
FORMUL 8 U C9 H13 N2 O9 P
HELIX 1 AA1 LYS A 71 ILE A 73 5 3
HELIX 2 AA2 ALA A 74 PHE A 78 5 5
HELIX 3 AA3 ASN A 89 VAL A 93 5 5
HELIX 4 AA4 GLU A 144 ALA A 156 1 13
HELIX 5 AA5 THR A 170 VAL A 173 5 4
HELIX 6 AA6 SER A 176 ARG A 201 1 26
HELIX 7 AA7 ASN A 212 LEU A 222 1 11
HELIX 8 AA8 ASN A 233 LEU A 247 1 15
HELIX 9 AA9 ASP A 251 SER A 254 5 4
HELIX 10 AB1 PRO A 264 TYR A 269 1 6
HELIX 11 AB2 ILE A 271 SER A 277 1 7
HELIX 12 AB3 ASP A 314 ASP A 338 1 25
HELIX 13 AB4 PRO A 352 GLN A 369 1 18
HELIX 14 AB5 SER A 395 SER A 400 1 6
HELIX 15 AB6 ASP A 415 LEU A 432 1 18
HELIX 16 AB7 VAL A 445 LEU A 452 1 8
HELIX 17 AB8 LYS A 455 GLN A 466 1 12
HELIX 18 AB9 LEU A 498 TYR A 500 5 3
HELIX 19 AC1 MET A 501 MET A 510 1 10
HELIX 20 AC2 LYS G 71 ILE G 73 5 3
HELIX 21 AC3 ALA G 74 PHE G 78 5 5
HELIX 22 AC4 ASN G 89 VAL G 93 5 5
HELIX 23 AC5 ASP G 146 LEU G 158 1 13
HELIX 24 AC6 THR G 170 VAL G 173 5 4
HELIX 25 AC7 ALA G 179 SER G 200 1 22
HELIX 26 AC8 ILE G 214 ASP G 220 1 7
HELIX 27 AC9 ASN G 233 LEU G 247 1 15
HELIX 28 AD1 ASP G 251 SER G 254 5 4
HELIX 29 AD2 PRO G 264 TYR G 269 1 6
HELIX 30 AD3 ILE G 271 ALA G 278 1 8
HELIX 31 AD4 ASP G 314 ASP G 338 1 25
HELIX 32 AD5 PRO G 352 ARG G 368 1 17
HELIX 33 AD6 ASP G 415 LEU G 432 1 18
HELIX 34 AD7 VAL G 445 LEU G 452 1 8
HELIX 35 AD8 LYS G 455 GLN G 466 1 12
HELIX 36 AD9 LEU G 498 TYR G 500 5 3
HELIX 37 AE1 MET G 501 MET G 510 1 10
HELIX 38 AE2 LYS L 71 ILE L 73 5 3
HELIX 39 AE3 ALA L 74 PHE L 78 5 5
HELIX 40 AE4 ASN L 89 VAL L 93 5 5
HELIX 41 AE5 LEU L 151 LEU L 158 1 8
HELIX 42 AE6 THR L 170 VAL L 173 5 4
HELIX 43 AE7 GLU L 178 ARG L 201 1 24
HELIX 44 AE8 ILE L 214 ASP L 220 1 7
HELIX 45 AE9 ASN L 233 LEU L 247 1 15
HELIX 46 AF1 ARG L 249 SER L 254 5 6
HELIX 47 AF2 PRO L 264 TYR L 269 1 6
HELIX 48 AF3 ILE L 271 GLU L 276 1 6
HELIX 49 AF4 SER L 277 PHE L 279 5 3
HELIX 50 AF5 ASP L 314 ASP L 338 1 25
HELIX 51 AF6 PRO L 352 ARG L 368 1 17
HELIX 52 AF7 SER L 395 SER L 400 1 6
HELIX 53 AF8 ASP L 415 LEU L 432 1 18
HELIX 54 AF9 VAL L 445 ASN L 453 1 9
HELIX 55 AG1 LYS L 455 GLN L 466 1 12
HELIX 56 AG2 LEU L 498 TYR L 500 5 3
HELIX 57 AG3 MET L 501 MET L 510 1 10
HELIX 58 AG4 LYS N 71 ILE N 73 5 3
HELIX 59 AG5 ALA N 74 PHE N 78 5 5
HELIX 60 AG6 ASN N 89 VAL N 93 5 5
HELIX 61 AG7 LEU N 151 LEU N 158 1 8
HELIX 62 AG8 THR N 170 VAL N 173 5 4
HELIX 63 AG9 ALA N 179 ARG N 201 1 23
HELIX 64 AH1 ASN N 212 LEU N 222 1 11
HELIX 65 AH2 ASN N 233 LEU N 247 1 15
HELIX 66 AH3 ASP N 251 SER N 254 5 4
HELIX 67 AH4 PRO N 264 TYR N 269 1 6
HELIX 68 AH5 ILE N 271 SER N 277 1 7
HELIX 69 AH6 ILE N 315 ASP N 338 1 24
HELIX 70 AH7 PRO N 352 GLN N 369 1 18
HELIX 71 AH8 SER N 395 SER N 400 1 6
HELIX 72 AH9 ASP N 415 LEU N 432 1 18
HELIX 73 AI1 VAL N 445 ASN N 453 1 9
HELIX 74 AI2 LYS N 455 GLN N 466 1 12
HELIX 75 AI3 TYR N 500 MET N 510 1 11
SHEET 1 AA1 5 LEU A 24 GLU A 30 0
SHEET 2 AA1 5 LEU A 14 VAL A 19 -1 N LEU A 18 O ASP A 26
SHEET 3 AA1 5 MET A 4 ASN A 7 -1 N ASN A 7 O ARG A 15
SHEET 4 AA1 5 ILE A 229 ILE A 231 1 O LEU A 230 N ILE A 6
SHEET 5 AA1 5 ILE A 256 LEU A 258 1 O LYS A 257 N ILE A 229
SHEET 1 AA2 6 ILE A 41 ILE A 49 0
SHEET 2 AA2 6 ALA A 55 ASP A 59 -1 O PHE A 57 N ARG A 48
SHEET 3 AA2 6 GLY A 66 PRO A 69 -1 O LEU A 68 N ALA A 56
SHEET 4 AA2 6 ALA A 115 THR A 117 1 O LEU A 116 N PHE A 67
SHEET 5 AA2 6 GLU A 99 LYS A 106 -1 N GLN A 103 O THR A 117
SHEET 6 AA2 6 ILE A 41 ILE A 49 -1 N TYR A 42 O VAL A 102
SHEET 1 AA3 3 LEU A 122 ALA A 123 0
SHEET 2 AA3 3 LEU A 127 MET A 130 -1 O LEU A 129 N LEU A 122
SHEET 3 AA3 3 GLY A 165 VAL A 168 -1 O GLY A 165 N MET A 130
SHEET 1 AA4 6 GLU A 282 ARG A 284 0
SHEET 2 AA4 6 SER A 290 SER A 295 -1 O ILE A 291 N VAL A 283
SHEET 3 AA4 6 LEU A 299 ASN A 305 -1 O ALA A 301 N ASP A 294
SHEET 4 AA4 6 GLY A 341 ARG A 346 1 O VAL A 344 N THR A 300
SHEET 5 AA4 6 LEU A 384 ARG A 389 -1 O MET A 387 N ILE A 343
SHEET 6 AA4 6 ILE A 374 ILE A 376 -1 N GLN A 375 O SER A 388
SHEET 1 AA5 2 HIS A 401 VAL A 403 0
SHEET 2 AA5 2 THR G 412 ARG G 414 -1 O VAL G 413 N HIS A 402
SHEET 1 AA6 2 THR A 412 ARG A 414 0
SHEET 2 AA6 2 HIS G 401 VAL G 403 -1 O HIS G 402 N VAL A 413
SHEET 1 AA7 3 ARG A 470 ASN A 476 0
SHEET 2 AA7 3 THR A 436 PRO A 444 1 N ALA A 441 O VAL A 474
SHEET 3 AA7 3 HIS A 485 ARG A 490 -1 O LEU A 487 N HIS A 440
SHEET 1 AA8 5 ARG G 23 GLU G 30 0
SHEET 2 AA8 5 LEU G 14 ASP G 20 -1 N ASP G 20 O ARG G 23
SHEET 3 AA8 5 LYS G 2 ASN G 7 -1 N ARG G 3 O VAL G 19
SHEET 4 AA8 5 ILE G 226 ILE G 231 1 O LEU G 230 N ILE G 6
SHEET 5 AA8 5 ILE G 256 LEU G 258 1 O LYS G 257 N ILE G 229
SHEET 1 AA9 6 ILE G 41 ILE G 49 0
SHEET 2 AA9 6 ALA G 55 ASP G 59 -1 O PHE G 57 N THR G 47
SHEET 3 AA9 6 GLY G 66 PRO G 69 -1 O GLY G 66 N VAL G 58
SHEET 4 AA9 6 ALA G 114 THR G 117 1 O ALA G 114 N PHE G 67
SHEET 5 AA9 6 GLU G 99 LYS G 106 -1 N GLN G 103 O THR G 117
SHEET 6 AA9 6 ILE G 41 ILE G 49 -1 N TYR G 42 O VAL G 102
SHEET 1 AB1 4 LEU G 122 ALA G 123 0
SHEET 2 AB1 4 LEU G 127 MET G 130 -1 O LEU G 129 N LEU G 122
SHEET 3 AB1 4 GLY G 165 VAL G 168 -1 O GLY G 165 N MET G 130
SHEET 4 AB1 4 GLY G 138 ILE G 139 1 N GLY G 138 O VAL G 168
SHEET 1 AB2 6 GLU G 282 ARG G 284 0
SHEET 2 AB2 6 SER G 290 SER G 295 -1 O ILE G 291 N VAL G 283
SHEET 3 AB2 6 THR G 300 ASN G 305 -1 O ALA G 301 N ASP G 294
SHEET 4 AB2 6 GLY G 341 ARG G 346 1 O ARG G 346 N ILE G 302
SHEET 5 AB2 6 LEU G 384 ARG G 389 -1 O MET G 387 N ILE G 343
SHEET 6 AB2 6 ILE G 374 ILE G 376 -1 N GLN G 375 O SER G 388
SHEET 1 AB3 3 ARG G 470 ASN G 476 0
SHEET 2 AB3 3 THR G 436 PRO G 444 1 N ALA G 441 O VAL G 472
SHEET 3 AB3 3 HIS G 485 ARG G 490 -1 O HIS G 485 N ILE G 442
SHEET 1 AB4 5 ARG L 23 GLU L 30 0
SHEET 2 AB4 5 LEU L 14 ASP L 20 -1 N ASP L 20 O ARG L 23
SHEET 3 AB4 5 LYS L 2 ASN L 7 -1 N LEU L 5 O ALA L 17
SHEET 4 AB4 5 ILE L 226 ILE L 231 1 O LEU L 230 N ILE L 6
SHEET 5 AB4 5 ILE L 256 LEU L 258 1 O LYS L 257 N ILE L 229
SHEET 1 AB5 7 PHE L 205 HIS L 208 0
SHEET 2 AB5 7 ILE L 41 GLU L 50 -1 N LYS L 43 O PHE L 205
SHEET 3 AB5 7 GLU L 99 ILE L 104 -1 O VAL L 100 N GLY L 44
SHEET 4 AB5 7 ALA L 114 THR L 117 -1 O THR L 117 N GLN L 103
SHEET 5 AB5 7 GLY L 66 PRO L 69 1 N PHE L 67 O LEU L 116
SHEET 6 AB5 7 ALA L 55 ASP L 59 -1 N ALA L 56 O LEU L 68
SHEET 7 AB5 7 ILE L 41 GLU L 50 -1 N THR L 47 O PHE L 57
SHEET 1 AB6 4 LEU L 122 ALA L 123 0
SHEET 2 AB6 4 LEU L 127 MET L 130 -1 O LEU L 129 N LEU L 122
SHEET 3 AB6 4 GLY L 165 VAL L 168 -1 O GLY L 165 N MET L 130
SHEET 4 AB6 4 GLY L 138 ILE L 139 1 N GLY L 138 O VAL L 168
SHEET 1 AB7 6 GLU L 282 ARG L 284 0
SHEET 2 AB7 6 SER L 290 SER L 295 -1 O ILE L 291 N VAL L 283
SHEET 3 AB7 6 LEU L 299 ASN L 305 -1 O ASN L 305 N SER L 290
SHEET 4 AB7 6 GLY L 341 ARG L 346 1 O VAL L 344 N ILE L 302
SHEET 5 AB7 6 LEU L 384 ARG L 389 -1 O MET L 387 N ILE L 343
SHEET 6 AB7 6 ILE L 374 ILE L 379 -1 N SER L 377 O GLU L 386
SHEET 1 AB8 2 HIS L 401 VAL L 403 0
SHEET 2 AB8 2 THR N 412 ARG N 414 -1 O VAL N 413 N HIS L 402
SHEET 1 AB9 2 THR L 412 ARG L 414 0
SHEET 2 AB9 2 HIS N 401 VAL N 403 -1 O HIS N 402 N VAL L 413
SHEET 1 AC1 3 ARG L 470 ASN L 476 0
SHEET 2 AC1 3 THR L 436 PRO L 444 1 N ALA L 441 O VAL L 474
SHEET 3 AC1 3 HIS L 485 ARG L 490 -1 O LEU L 487 N HIS L 440
SHEET 1 AC2 5 ARG N 23 GLU N 30 0
SHEET 2 AC2 5 LEU N 14 ASP N 20 -1 N ASP N 20 O ARG N 23
SHEET 3 AC2 5 LYS N 2 ASN N 7 -1 N ARG N 3 O VAL N 19
SHEET 4 AC2 5 ILE N 226 ILE N 231 1 O GLY N 227 N LYS N 2
SHEET 5 AC2 5 ILE N 256 LEU N 258 1 O LYS N 257 N ILE N 229
SHEET 1 AC3 7 PHE N 205 HIS N 208 0
SHEET 2 AC3 7 ILE N 41 GLU N 50 -1 N ILE N 41 O ILE N 207
SHEET 3 AC3 7 GLU N 99 LYS N 106 -1 O VAL N 100 N GLY N 44
SHEET 4 AC3 7 ALA N 115 THR N 117 -1 O THR N 117 N GLN N 103
SHEET 5 AC3 7 GLY N 66 PRO N 69 1 N PHE N 67 O LEU N 116
SHEET 6 AC3 7 ALA N 55 ASP N 59 -1 N ALA N 56 O LEU N 68
SHEET 7 AC3 7 ILE N 41 GLU N 50 -1 N LYS N 45 O ASP N 59
SHEET 1 AC4 4 LEU N 122 ALA N 123 0
SHEET 2 AC4 4 LEU N 127 MET N 130 -1 O LEU N 129 N LEU N 122
SHEET 3 AC4 4 GLY N 165 VAL N 168 -1 O GLY N 165 N MET N 130
SHEET 4 AC4 4 GLY N 138 ILE N 139 1 N GLY N 138 O VAL N 168
SHEET 1 AC5 6 GLU N 282 ARG N 284 0
SHEET 2 AC5 6 SER N 290 SER N 295 -1 O ILE N 291 N VAL N 283
SHEET 3 AC5 6 LEU N 299 ASN N 305 -1 O ASN N 305 N SER N 290
SHEET 4 AC5 6 GLY N 341 ARG N 346 1 O ARG N 346 N ILE N 302
SHEET 5 AC5 6 LEU N 384 ARG N 389 -1 O MET N 387 N ILE N 343
SHEET 6 AC5 6 ILE N 374 ILE N 379 -1 N SER N 377 O GLU N 386
SHEET 1 AC6 3 ARG N 470 ASN N 476 0
SHEET 2 AC6 3 THR N 436 PRO N 444 1 N VAL N 443 O VAL N 474
SHEET 3 AC6 3 HIS N 485 ARG N 490 -1 O LEU N 487 N HIS N 440
LINK SG CYS A 404 ZN ZN A 601 1555 1555 2.14
LINK SG CYS A 407 ZN ZN A 601 1555 1555 2.44
LINK SG CYS G 404 ZN ZN A 601 1555 1555 2.20
LINK SG CYS G 407 ZN ZN A 601 1555 1555 2.53
LINK SG CYS L 404 ZN ZN L 601 1555 1555 2.30
LINK SG CYS L 407 ZN ZN L 601 1555 1555 2.53
LINK SG CYS N 404 ZN ZN L 601 1555 1555 2.21
LINK SG CYS N 407 ZN ZN L 601 1555 1555 2.58
SITE 1 AC1 4 CYS A 404 CYS A 407 CYS G 404 CYS G 407
SITE 1 AC2 4 CYS L 404 CYS L 407 CYS N 404 CYS N 407
SITE 1 AC3 7 SER N 140 ARG N 142 ILE N 167 ARG N 169
SITE 2 AC3 7 THR N 170 ARG N 223 ARG N 371
CRYST1 110.630 110.630 466.020 90.00 90.00 120.00 P 61 24
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 0.009039 0.005219 0.000000 0.00000
SCALE2 0.000000 0.010437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002146 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
