HEADER HYDROLASE 22-DEC-16 5UCG
TITLE STRUCTURE OF THE PP2C PHOSPHATASE DOMAIN AND A FRAGMENT OF THE
TITLE 2 REGULATORY DOMAIN OF THE CELL FATE DETERMINANT SPOIIE FROM BACILLUS
TITLE 3 SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAGE II SPORULATION PROTEIN E;
COMPND 3 CHAIN: A, E, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 465-809;
COMPND 5 SYNONYM: STAGE II SPORULATION PROTEIN H;
COMPND 6 EC: 3.1.3.16;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: SPOIIE, SPOIIH, BSU00640;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: DE3;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET47B
KEYWDS PPM PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BRADSHAW,V.LEVDIKOV,C.ZIMANYI,R.GAUDET,A.WILKINSON,R.LOSICK
REVDAT 4 04-OCT-23 5UCG 1 REMARK
REVDAT 3 01-JAN-20 5UCG 1 REMARK
REVDAT 2 20-SEP-17 5UCG 1 REMARK
REVDAT 1 31-MAY-17 5UCG 0
JRNL AUTH N.BRADSHAW,V.M.LEVDIKOV,C.M.ZIMANYI,R.GAUDET,A.J.WILKINSON,
JRNL AUTH 2 R.LOSICK
JRNL TITL A WIDESPREAD FAMILY OF SERINE/THREONINE PROTEIN PHOSPHATASES
JRNL TITL 2 SHARES A COMMON REGULATORY SWITCH WITH PROTEASOMAL
JRNL TITL 3 PROTEASES.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28527238
JRNL DOI 10.7554/ELIFE.26111
REMARK 2
REMARK 2 RESOLUTION. 3.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 3.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 21558
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.279
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1091
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 50.0582 - 7.8036 1.00 3176 150 0.2372 0.2711
REMARK 3 2 7.8036 - 6.1976 1.00 3014 156 0.3178 0.3612
REMARK 3 3 6.1976 - 5.4153 1.00 2946 161 0.3285 0.3552
REMARK 3 4 5.4153 - 4.9206 1.00 2930 151 0.2657 0.3062
REMARK 3 5 4.9206 - 4.5682 1.00 2905 161 0.2555 0.3255
REMARK 3 6 4.5682 - 4.2990 0.95 2751 165 0.2807 0.3272
REMARK 3 7 4.2990 - 4.0838 0.60 1732 95 0.2868 0.3817
REMARK 3 8 4.0838 - 3.9061 0.35 1013 52 0.2959 0.3014
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) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.26
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 : 0.002 13340
REMARK 3 ANGLE : 0.525 17928
REMARK 3 CHIRALITY : 0.043 2055
REMARK 3 PLANARITY : 0.002 2319
REMARK 3 DIHEDRAL : 15.875 8224
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 465 THROUGH 591 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0887 -57.5885 -26.2392
REMARK 3 T TENSOR
REMARK 3 T11: 0.8805 T22: 0.8612
REMARK 3 T33: 0.4164 T12: 0.2827
REMARK 3 T13: 0.1380 T23: 0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 2.0801 L22: 1.3272
REMARK 3 L33: 1.0279 L12: 0.2901
REMARK 3 L13: -0.2512 L23: 0.5118
REMARK 3 S TENSOR
REMARK 3 S11: 0.3570 S12: 0.3336 S13: 0.2761
REMARK 3 S21: -0.6231 S22: -0.1405 S23: -0.1782
REMARK 3 S31: -0.0035 S32: 0.6145 S33: -0.1900
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 592 THROUGH 809 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5136 -47.8654 -1.7844
REMARK 3 T TENSOR
REMARK 3 T11: 0.5178 T22: 0.5561
REMARK 3 T33: 0.1386 T12: 0.1601
REMARK 3 T13: 0.0290 T23: -0.1909
REMARK 3 L TENSOR
REMARK 3 L11: 1.4380 L22: 2.5797
REMARK 3 L33: 2.9035 L12: 0.7442
REMARK 3 L13: -0.8201 L23: 0.3347
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: 0.2106 S13: 0.2530
REMARK 3 S21: -0.3512 S22: -0.0629 S23: 0.5421
REMARK 3 S31: -0.1668 S32: -0.8338 S33: 0.1970
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 467 THROUGH 591 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9878 -3.7848 16.6143
REMARK 3 T TENSOR
REMARK 3 T11: 0.7393 T22: 1.2029
REMARK 3 T33: 0.8390 T12: -0.5268
REMARK 3 T13: -0.3784 T23: 0.3336
REMARK 3 L TENSOR
REMARK 3 L11: 0.2763 L22: 1.0136
REMARK 3 L33: 0.6144 L12: 0.0148
REMARK 3 L13: 0.1394 L23: -0.0619
REMARK 3 S TENSOR
REMARK 3 S11: -0.1794 S12: 0.1662 S13: 0.0058
REMARK 3 S21: -0.0595 S22: 0.0634 S23: -0.4453
REMARK 3 S31: -0.3642 S32: 0.5994 S33: 0.2003
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 592 THROUGH 809 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2808 -8.0358 20.8578
REMARK 3 T TENSOR
REMARK 3 T11: 0.4862 T22: 0.6395
REMARK 3 T33: 0.2054 T12: -0.2607
REMARK 3 T13: -0.0904 T23: 0.3010
REMARK 3 L TENSOR
REMARK 3 L11: 2.0837 L22: 1.3741
REMARK 3 L33: 2.7093 L12: 1.1781
REMARK 3 L13: 0.6237 L23: 0.0487
REMARK 3 S TENSOR
REMARK 3 S11: -0.5431 S12: 0.5093 S13: 0.7121
REMARK 3 S21: -0.2962 S22: 0.4520 S23: 0.5228
REMARK 3 S31: -0.8496 S32: -0.1294 S33: -0.2277
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 465 THROUGH 610 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0750 -58.7846 -32.9643
REMARK 3 T TENSOR
REMARK 3 T11: 1.2182 T22: 1.1893
REMARK 3 T33: 0.8128 T12: 0.1338
REMARK 3 T13: -0.5111 T23: -0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 1.5676 L22: 0.6471
REMARK 3 L33: 0.3712 L12: 0.3090
REMARK 3 L13: -0.2149 L23: 0.0273
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: 1.0415 S13: 0.0435
REMARK 3 S21: -0.5798 S22: -0.0010 S23: 0.3350
REMARK 3 S31: -0.3066 S32: -0.2560 S33: -0.0961
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 611 THROUGH 804 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1878 -78.0828 -15.3939
REMARK 3 T TENSOR
REMARK 3 T11: 1.0046 T22: 0.4620
REMARK 3 T33: 1.3229 T12: 0.0334
REMARK 3 T13: -0.4669 T23: -0.1536
REMARK 3 L TENSOR
REMARK 3 L11: 0.2104 L22: 1.1803
REMARK 3 L33: 2.7446 L12: 0.3766
REMARK 3 L13: -0.2689 L23: -1.0261
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: 0.0805 S13: -0.8097
REMARK 3 S21: -0.0060 S22: 0.0161 S23: -0.4303
REMARK 3 S31: -0.0176 S32: 0.5752 S33: 0.0287
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 469 THROUGH 610 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6701 -75.3962 4.1754
REMARK 3 T TENSOR
REMARK 3 T11: 0.8701 T22: 0.7230
REMARK 3 T33: 1.7606 T12: -0.2223
REMARK 3 T13: -0.4214 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.3441 L22: 1.1563
REMARK 3 L33: 1.0185 L12: 0.4972
REMARK 3 L13: -0.2410 L23: 0.0665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0268 S12: 0.0387 S13: -0.3851
REMARK 3 S21: -0.0215 S22: 0.0769 S23: 0.2152
REMARK 3 S31: 0.6881 S32: -0.4170 S33: -0.0632
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 611 THROUGH 807 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6656 -53.4471 -11.5960
REMARK 3 T TENSOR
REMARK 3 T11: 1.0070 T22: 0.7149
REMARK 3 T33: 1.3127 T12: -0.0261
REMARK 3 T13: -0.5411 T23: -0.0950
REMARK 3 L TENSOR
REMARK 3 L11: 1.2163 L22: 2.2330
REMARK 3 L33: 2.7262 L12: 0.9006
REMARK 3 L13: -1.4874 L23: -0.8273
REMARK 3 S TENSOR
REMARK 3 S11: 0.3112 S12: 0.2130 S13: 0.2352
REMARK 3 S21: 0.1607 S22: -0.2082 S23: 1.0456
REMARK 3 S31: -0.5492 S32: -0.7020 S33: -0.0220
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 469 THROUGH 591 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6551 -40.2634 32.8598
REMARK 3 T TENSOR
REMARK 3 T11: 0.7772 T22: 1.0386
REMARK 3 T33: 1.0046 T12: -0.1183
REMARK 3 T13: 0.2157 T23: 0.4810
REMARK 3 L TENSOR
REMARK 3 L11: 0.8656 L22: 0.1052
REMARK 3 L33: 0.8126 L12: 0.0684
REMARK 3 L13: 0.1541 L23: -0.0251
REMARK 3 S TENSOR
REMARK 3 S11: 0.1521 S12: -0.5460 S13: -0.2700
REMARK 3 S21: 0.2724 S22: 0.0601 S23: 0.6114
REMARK 3 S31: 0.3513 S32: -0.6600 S33: -0.1660
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 592 THROUGH 808 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7854 -37.7119 22.1703
REMARK 3 T TENSOR
REMARK 3 T11: 0.4318 T22: 0.5153
REMARK 3 T33: 0.5837 T12: 0.0846
REMARK 3 T13: -0.2945 T23: 0.2673
REMARK 3 L TENSOR
REMARK 3 L11: 3.1977 L22: 1.2896
REMARK 3 L33: 3.5879 L12: 0.6579
REMARK 3 L13: -0.1333 L23: -1.8818
REMARK 3 S TENSOR
REMARK 3 S11: 0.2285 S12: 0.3355 S13: -0.8709
REMARK 3 S21: -0.5232 S22: -0.1655 S23: -0.2498
REMARK 3 S31: 1.0944 S32: 0.5150 S33: -0.4653
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 5UCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225653.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24917
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.900
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 1.44800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3T91
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 MM LISO4, 8% PEG8000, 0.05 MM NAF,
REMARK 280 6% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 165.34800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.81100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.81100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 248.02200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.81100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.81100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 82.67400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.81100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.81100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 248.02200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.81100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.81100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.67400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 165.34800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ALA E 465
REMARK 465 HIS E 466
REMARK 465 PRO E 575
REMARK 465 HIS E 576
REMARK 465 PRO E 577
REMARK 465 ASN E 578
REMARK 465 GLY E 579
REMARK 465 GLY B 548
REMARK 465 GLU B 549
REMARK 465 SER B 550
REMARK 465 ASP B 805
REMARK 465 HIS B 806
REMARK 465 ASN B 807
REMARK 465 THR B 808
REMARK 465 PRO B 809
REMARK 465 ALA C 465
REMARK 465 HIS C 466
REMARK 465 LEU C 467
REMARK 465 THR C 468
REMARK 465 GLY C 546
REMARK 465 HIS C 547
REMARK 465 GLY C 629
REMARK 465 MET C 630
REMARK 465 GLY C 631
REMARK 465 ASN C 632
REMARK 465 GLY C 633
REMARK 465 ALA C 634
REMARK 465 THR C 808
REMARK 465 PRO C 809
REMARK 465 ALA D 465
REMARK 465 HIS D 466
REMARK 465 LEU D 467
REMARK 465 THR D 468
REMARK 465 HIS D 573
REMARK 465 SER D 574
REMARK 465 PRO D 575
REMARK 465 HIS D 576
REMARK 465 PRO D 577
REMARK 465 SER D 716
REMARK 465 PRO D 809
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 O ASP E 628 OG SER E 640 2.14
REMARK 500 O LYS C 696 ND2 ASN C 717 2.17
REMARK 500 O LYS A 696 ND2 ASN A 717 2.19
REMARK 500 OG SER D 545 OE1 GLU D 549 2.19
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 HIS A 466 -145.36 -121.58
REMARK 500 SER A 545 -128.74 59.35
REMARK 500 HIS A 547 -169.40 59.94
REMARK 500 LEU A 562 -14.45 70.62
REMARK 500 GLU A 563 -32.01 -132.51
REMARK 500 SER A 574 80.32 -164.22
REMARK 500 TYR A 591 92.58 59.17
REMARK 500 LEU A 606 -102.40 56.61
REMARK 500 LEU A 617 77.94 -106.64
REMARK 500 ASP A 628 -104.59 -113.40
REMARK 500 ARG A 671 -12.58 78.20
REMARK 500 TYR A 677 -164.51 -105.14
REMARK 500 ASP A 689 24.79 -143.59
REMARK 500 ASN A 717 157.72 179.35
REMARK 500 ILE A 722 42.02 -141.26
REMARK 500 ASP A 727 -145.30 47.79
REMARK 500 LYS A 736 -169.90 -123.31
REMARK 500 HIS A 754 55.95 -102.84
REMARK 500 GLU A 756 -60.80 -91.08
REMARK 500 LYS A 770 64.05 -115.74
REMARK 500 LYS E 470 -43.03 63.76
REMARK 500 HIS E 518 71.61 -69.57
REMARK 500 GLU E 522 -149.53 56.60
REMARK 500 GLN E 524 -106.93 54.04
REMARK 500 LEU E 562 158.31 69.81
REMARK 500 TYR E 591 88.97 62.07
REMARK 500 LEU E 617 78.98 -105.75
REMARK 500 ASP E 628 -111.24 -114.42
REMARK 500 ARG E 671 -12.24 78.90
REMARK 500 TYR E 677 -161.92 -109.06
REMARK 500 ASP E 727 -143.86 43.67
REMARK 500 LYS E 736 -168.89 -126.53
REMARK 500 HIS E 754 51.14 -94.88
REMARK 500 LYS E 770 64.45 -117.69
REMARK 500 HIS B 466 -124.43 -123.52
REMARK 500 LEU B 469 68.33 32.94
REMARK 500 LYS B 470 -71.26 -59.38
REMARK 500 GLU B 522 153.27 67.16
REMARK 500 GLN B 524 -111.28 54.33
REMARK 500 SER B 545 -112.71 55.24
REMARK 500 GLU B 564 -166.18 61.14
REMARK 500 LYS B 569 87.70 -155.79
REMARK 500 SER B 574 81.80 58.64
REMARK 500 PRO B 577 23.22 -69.94
REMARK 500 SER B 581 114.23 -164.58
REMARK 500 TYR B 591 91.35 61.60
REMARK 500 LEU B 617 77.15 -104.75
REMARK 500 ASP B 628 -89.16 -112.70
REMARK 500 ARG B 671 -13.12 77.59
REMARK 500 TYR B 677 -163.88 -105.40
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5UCG A 465 809 UNP P37475 SP2E_BACSU 465 809
DBREF 5UCG E 465 809 UNP P37475 SP2E_BACSU 465 809
DBREF 5UCG B 465 809 UNP P37475 SP2E_BACSU 465 809
DBREF 5UCG C 465 809 UNP P37475 SP2E_BACSU 465 809
DBREF 5UCG D 465 809 UNP P37475 SP2E_BACSU 465 809
SEQRES 1 A 345 ALA HIS LEU THR LEU LYS LYS LYS VAL GLN ASP SER ARG
SEQRES 2 A 345 ARG LEU VAL ALA GLU GLN LEU LEU GLY VAL SER GLU VAL
SEQRES 3 A 345 MET ALA ASP PHE SER ARG GLU ILE LYS ARG GLU ARG GLU
SEQRES 4 A 345 GLN HIS PHE LEU GLN GLU GLU GLN ILE ILE GLU ALA LEU
SEQRES 5 A 345 GLN HIS PHE GLY ILE GLU ILE GLN HIS VAL GLU ILE TYR
SEQRES 6 A 345 SER LEU GLU GLN GLY ASN ILE ASP ILE GLU MET THR ILE
SEQRES 7 A 345 PRO PHE SER GLY HIS GLY GLU SER GLU LYS ILE ILE ALA
SEQRES 8 A 345 PRO MET LEU SER ASP ILE LEU GLU GLU GLN ILE LEU VAL
SEQRES 9 A 345 LYS ALA GLU GLN HIS SER PRO HIS PRO ASN GLY TYR SER
SEQRES 10 A 345 HIS VAL ALA PHE GLY SER THR LYS SER TYR ARG VAL SER
SEQRES 11 A 345 THR GLY ALA ALA HIS ALA ALA LYS GLY GLY GLY LEU VAL
SEQRES 12 A 345 SER GLY ASP SER TYR SER MET MET GLU LEU GLY ALA ARG
SEQRES 13 A 345 LYS TYR ALA ALA ALA ILE SER ASP GLY MET GLY ASN GLY
SEQRES 14 A 345 ALA ARG ALA HIS PHE GLU SER ASN GLU THR ILE LYS LEU
SEQRES 15 A 345 LEU GLU LYS ILE LEU GLU SER GLY ILE ASP GLU LYS ILE
SEQRES 16 A 345 ALA ILE LYS THR ILE ASN SER ILE LEU SER LEU ARG THR
SEQRES 17 A 345 THR ASP GLU ILE TYR SER THR LEU ASP LEU SER ILE ILE
SEQRES 18 A 345 ASP LEU GLN ASP ALA SER CYS LYS PHE LEU LYS VAL GLY
SEQRES 19 A 345 SER THR PRO SER PHE ILE LYS ARG GLY ASP GLN VAL MET
SEQRES 20 A 345 LYS VAL GLN ALA SER ASN LEU PRO ILE GLY ILE ILE ASN
SEQRES 21 A 345 GLU PHE ASP VAL GLU VAL VAL SER GLU GLN LEU LYS ALA
SEQRES 22 A 345 GLY ASP LEU LEU ILE MET MET SER ASP GLY ILE PHE GLU
SEQRES 23 A 345 GLY PRO LYS HIS VAL GLU ASN HIS ASP LEU TRP MET LYS
SEQRES 24 A 345 ARG LYS MET LYS GLY LEU LYS THR ASN ASP PRO GLN GLU
SEQRES 25 A 345 ILE ALA ASP LEU LEU MET GLU GLU VAL ILE ARG THR ARG
SEQRES 26 A 345 SER GLY GLN ILE GLU ASP ASP MET THR VAL VAL VAL VAL
SEQRES 27 A 345 ARG ILE ASP HIS ASN THR PRO
SEQRES 1 E 345 ALA HIS LEU THR LEU LYS LYS LYS VAL GLN ASP SER ARG
SEQRES 2 E 345 ARG LEU VAL ALA GLU GLN LEU LEU GLY VAL SER GLU VAL
SEQRES 3 E 345 MET ALA ASP PHE SER ARG GLU ILE LYS ARG GLU ARG GLU
SEQRES 4 E 345 GLN HIS PHE LEU GLN GLU GLU GLN ILE ILE GLU ALA LEU
SEQRES 5 E 345 GLN HIS PHE GLY ILE GLU ILE GLN HIS VAL GLU ILE TYR
SEQRES 6 E 345 SER LEU GLU GLN GLY ASN ILE ASP ILE GLU MET THR ILE
SEQRES 7 E 345 PRO PHE SER GLY HIS GLY GLU SER GLU LYS ILE ILE ALA
SEQRES 8 E 345 PRO MET LEU SER ASP ILE LEU GLU GLU GLN ILE LEU VAL
SEQRES 9 E 345 LYS ALA GLU GLN HIS SER PRO HIS PRO ASN GLY TYR SER
SEQRES 10 E 345 HIS VAL ALA PHE GLY SER THR LYS SER TYR ARG VAL SER
SEQRES 11 E 345 THR GLY ALA ALA HIS ALA ALA LYS GLY GLY GLY LEU VAL
SEQRES 12 E 345 SER GLY ASP SER TYR SER MET MET GLU LEU GLY ALA ARG
SEQRES 13 E 345 LYS TYR ALA ALA ALA ILE SER ASP GLY MET GLY ASN GLY
SEQRES 14 E 345 ALA ARG ALA HIS PHE GLU SER ASN GLU THR ILE LYS LEU
SEQRES 15 E 345 LEU GLU LYS ILE LEU GLU SER GLY ILE ASP GLU LYS ILE
SEQRES 16 E 345 ALA ILE LYS THR ILE ASN SER ILE LEU SER LEU ARG THR
SEQRES 17 E 345 THR ASP GLU ILE TYR SER THR LEU ASP LEU SER ILE ILE
SEQRES 18 E 345 ASP LEU GLN ASP ALA SER CYS LYS PHE LEU LYS VAL GLY
SEQRES 19 E 345 SER THR PRO SER PHE ILE LYS ARG GLY ASP GLN VAL MET
SEQRES 20 E 345 LYS VAL GLN ALA SER ASN LEU PRO ILE GLY ILE ILE ASN
SEQRES 21 E 345 GLU PHE ASP VAL GLU VAL VAL SER GLU GLN LEU LYS ALA
SEQRES 22 E 345 GLY ASP LEU LEU ILE MET MET SER ASP GLY ILE PHE GLU
SEQRES 23 E 345 GLY PRO LYS HIS VAL GLU ASN HIS ASP LEU TRP MET LYS
SEQRES 24 E 345 ARG LYS MET LYS GLY LEU LYS THR ASN ASP PRO GLN GLU
SEQRES 25 E 345 ILE ALA ASP LEU LEU MET GLU GLU VAL ILE ARG THR ARG
SEQRES 26 E 345 SER GLY GLN ILE GLU ASP ASP MET THR VAL VAL VAL VAL
SEQRES 27 E 345 ARG ILE ASP HIS ASN THR PRO
SEQRES 1 B 345 ALA HIS LEU THR LEU LYS LYS LYS VAL GLN ASP SER ARG
SEQRES 2 B 345 ARG LEU VAL ALA GLU GLN LEU LEU GLY VAL SER GLU VAL
SEQRES 3 B 345 MET ALA ASP PHE SER ARG GLU ILE LYS ARG GLU ARG GLU
SEQRES 4 B 345 GLN HIS PHE LEU GLN GLU GLU GLN ILE ILE GLU ALA LEU
SEQRES 5 B 345 GLN HIS PHE GLY ILE GLU ILE GLN HIS VAL GLU ILE TYR
SEQRES 6 B 345 SER LEU GLU GLN GLY ASN ILE ASP ILE GLU MET THR ILE
SEQRES 7 B 345 PRO PHE SER GLY HIS GLY GLU SER GLU LYS ILE ILE ALA
SEQRES 8 B 345 PRO MET LEU SER ASP ILE LEU GLU GLU GLN ILE LEU VAL
SEQRES 9 B 345 LYS ALA GLU GLN HIS SER PRO HIS PRO ASN GLY TYR SER
SEQRES 10 B 345 HIS VAL ALA PHE GLY SER THR LYS SER TYR ARG VAL SER
SEQRES 11 B 345 THR GLY ALA ALA HIS ALA ALA LYS GLY GLY GLY LEU VAL
SEQRES 12 B 345 SER GLY ASP SER TYR SER MET MET GLU LEU GLY ALA ARG
SEQRES 13 B 345 LYS TYR ALA ALA ALA ILE SER ASP GLY MET GLY ASN GLY
SEQRES 14 B 345 ALA ARG ALA HIS PHE GLU SER ASN GLU THR ILE LYS LEU
SEQRES 15 B 345 LEU GLU LYS ILE LEU GLU SER GLY ILE ASP GLU LYS ILE
SEQRES 16 B 345 ALA ILE LYS THR ILE ASN SER ILE LEU SER LEU ARG THR
SEQRES 17 B 345 THR ASP GLU ILE TYR SER THR LEU ASP LEU SER ILE ILE
SEQRES 18 B 345 ASP LEU GLN ASP ALA SER CYS LYS PHE LEU LYS VAL GLY
SEQRES 19 B 345 SER THR PRO SER PHE ILE LYS ARG GLY ASP GLN VAL MET
SEQRES 20 B 345 LYS VAL GLN ALA SER ASN LEU PRO ILE GLY ILE ILE ASN
SEQRES 21 B 345 GLU PHE ASP VAL GLU VAL VAL SER GLU GLN LEU LYS ALA
SEQRES 22 B 345 GLY ASP LEU LEU ILE MET MET SER ASP GLY ILE PHE GLU
SEQRES 23 B 345 GLY PRO LYS HIS VAL GLU ASN HIS ASP LEU TRP MET LYS
SEQRES 24 B 345 ARG LYS MET LYS GLY LEU LYS THR ASN ASP PRO GLN GLU
SEQRES 25 B 345 ILE ALA ASP LEU LEU MET GLU GLU VAL ILE ARG THR ARG
SEQRES 26 B 345 SER GLY GLN ILE GLU ASP ASP MET THR VAL VAL VAL VAL
SEQRES 27 B 345 ARG ILE ASP HIS ASN THR PRO
SEQRES 1 C 345 ALA HIS LEU THR LEU LYS LYS LYS VAL GLN ASP SER ARG
SEQRES 2 C 345 ARG LEU VAL ALA GLU GLN LEU LEU GLY VAL SER GLU VAL
SEQRES 3 C 345 MET ALA ASP PHE SER ARG GLU ILE LYS ARG GLU ARG GLU
SEQRES 4 C 345 GLN HIS PHE LEU GLN GLU GLU GLN ILE ILE GLU ALA LEU
SEQRES 5 C 345 GLN HIS PHE GLY ILE GLU ILE GLN HIS VAL GLU ILE TYR
SEQRES 6 C 345 SER LEU GLU GLN GLY ASN ILE ASP ILE GLU MET THR ILE
SEQRES 7 C 345 PRO PHE SER GLY HIS GLY GLU SER GLU LYS ILE ILE ALA
SEQRES 8 C 345 PRO MET LEU SER ASP ILE LEU GLU GLU GLN ILE LEU VAL
SEQRES 9 C 345 LYS ALA GLU GLN HIS SER PRO HIS PRO ASN GLY TYR SER
SEQRES 10 C 345 HIS VAL ALA PHE GLY SER THR LYS SER TYR ARG VAL SER
SEQRES 11 C 345 THR GLY ALA ALA HIS ALA ALA LYS GLY GLY GLY LEU VAL
SEQRES 12 C 345 SER GLY ASP SER TYR SER MET MET GLU LEU GLY ALA ARG
SEQRES 13 C 345 LYS TYR ALA ALA ALA ILE SER ASP GLY MET GLY ASN GLY
SEQRES 14 C 345 ALA ARG ALA HIS PHE GLU SER ASN GLU THR ILE LYS LEU
SEQRES 15 C 345 LEU GLU LYS ILE LEU GLU SER GLY ILE ASP GLU LYS ILE
SEQRES 16 C 345 ALA ILE LYS THR ILE ASN SER ILE LEU SER LEU ARG THR
SEQRES 17 C 345 THR ASP GLU ILE TYR SER THR LEU ASP LEU SER ILE ILE
SEQRES 18 C 345 ASP LEU GLN ASP ALA SER CYS LYS PHE LEU LYS VAL GLY
SEQRES 19 C 345 SER THR PRO SER PHE ILE LYS ARG GLY ASP GLN VAL MET
SEQRES 20 C 345 LYS VAL GLN ALA SER ASN LEU PRO ILE GLY ILE ILE ASN
SEQRES 21 C 345 GLU PHE ASP VAL GLU VAL VAL SER GLU GLN LEU LYS ALA
SEQRES 22 C 345 GLY ASP LEU LEU ILE MET MET SER ASP GLY ILE PHE GLU
SEQRES 23 C 345 GLY PRO LYS HIS VAL GLU ASN HIS ASP LEU TRP MET LYS
SEQRES 24 C 345 ARG LYS MET LYS GLY LEU LYS THR ASN ASP PRO GLN GLU
SEQRES 25 C 345 ILE ALA ASP LEU LEU MET GLU GLU VAL ILE ARG THR ARG
SEQRES 26 C 345 SER GLY GLN ILE GLU ASP ASP MET THR VAL VAL VAL VAL
SEQRES 27 C 345 ARG ILE ASP HIS ASN THR PRO
SEQRES 1 D 345 ALA HIS LEU THR LEU LYS LYS LYS VAL GLN ASP SER ARG
SEQRES 2 D 345 ARG LEU VAL ALA GLU GLN LEU LEU GLY VAL SER GLU VAL
SEQRES 3 D 345 MET ALA ASP PHE SER ARG GLU ILE LYS ARG GLU ARG GLU
SEQRES 4 D 345 GLN HIS PHE LEU GLN GLU GLU GLN ILE ILE GLU ALA LEU
SEQRES 5 D 345 GLN HIS PHE GLY ILE GLU ILE GLN HIS VAL GLU ILE TYR
SEQRES 6 D 345 SER LEU GLU GLN GLY ASN ILE ASP ILE GLU MET THR ILE
SEQRES 7 D 345 PRO PHE SER GLY HIS GLY GLU SER GLU LYS ILE ILE ALA
SEQRES 8 D 345 PRO MET LEU SER ASP ILE LEU GLU GLU GLN ILE LEU VAL
SEQRES 9 D 345 LYS ALA GLU GLN HIS SER PRO HIS PRO ASN GLY TYR SER
SEQRES 10 D 345 HIS VAL ALA PHE GLY SER THR LYS SER TYR ARG VAL SER
SEQRES 11 D 345 THR GLY ALA ALA HIS ALA ALA LYS GLY GLY GLY LEU VAL
SEQRES 12 D 345 SER GLY ASP SER TYR SER MET MET GLU LEU GLY ALA ARG
SEQRES 13 D 345 LYS TYR ALA ALA ALA ILE SER ASP GLY MET GLY ASN GLY
SEQRES 14 D 345 ALA ARG ALA HIS PHE GLU SER ASN GLU THR ILE LYS LEU
SEQRES 15 D 345 LEU GLU LYS ILE LEU GLU SER GLY ILE ASP GLU LYS ILE
SEQRES 16 D 345 ALA ILE LYS THR ILE ASN SER ILE LEU SER LEU ARG THR
SEQRES 17 D 345 THR ASP GLU ILE TYR SER THR LEU ASP LEU SER ILE ILE
SEQRES 18 D 345 ASP LEU GLN ASP ALA SER CYS LYS PHE LEU LYS VAL GLY
SEQRES 19 D 345 SER THR PRO SER PHE ILE LYS ARG GLY ASP GLN VAL MET
SEQRES 20 D 345 LYS VAL GLN ALA SER ASN LEU PRO ILE GLY ILE ILE ASN
SEQRES 21 D 345 GLU PHE ASP VAL GLU VAL VAL SER GLU GLN LEU LYS ALA
SEQRES 22 D 345 GLY ASP LEU LEU ILE MET MET SER ASP GLY ILE PHE GLU
SEQRES 23 D 345 GLY PRO LYS HIS VAL GLU ASN HIS ASP LEU TRP MET LYS
SEQRES 24 D 345 ARG LYS MET LYS GLY LEU LYS THR ASN ASP PRO GLN GLU
SEQRES 25 D 345 ILE ALA ASP LEU LEU MET GLU GLU VAL ILE ARG THR ARG
SEQRES 26 D 345 SER GLY GLN ILE GLU ASP ASP MET THR VAL VAL VAL VAL
SEQRES 27 D 345 ARG ILE ASP HIS ASN THR PRO
HELIX 1 AA1 LYS A 472 PHE A 519 1 48
HELIX 2 AA2 GLY A 548 ILE A 553 1 6
HELIX 3 AA3 ILE A 554 LEU A 562 1 9
HELIX 4 AA4 GLY A 633 LEU A 651 1 19
HELIX 5 AA5 GLU A 652 GLY A 654 5 3
HELIX 6 AA6 ASP A 656 LEU A 668 1 13
HELIX 7 AA7 SER A 745 GLU A 750 1 6
HELIX 8 AA8 ASN A 757 GLY A 768 1 12
HELIX 9 AA9 ASP A 773 THR A 788 1 16
HELIX 10 AB1 LYS E 471 HIS E 518 1 48
HELIX 11 AB2 GLY E 548 ILE E 553 1 6
HELIX 12 AB3 ILE E 553 LEU E 562 1 10
HELIX 13 AB4 ALA E 634 LEU E 651 1 18
HELIX 14 AB5 ASP E 656 LEU E 668 1 13
HELIX 15 AB6 SER E 745 GLU E 750 1 6
HELIX 16 AB7 ASN E 757 GLY E 768 1 12
HELIX 17 AB8 ASP E 773 ARG E 789 1 17
HELIX 18 AB9 LYS B 471 HIS B 518 1 48
HELIX 19 AC1 ILE B 553 LEU B 562 1 10
HELIX 20 AC2 ASN B 632 LEU B 651 1 20
HELIX 21 AC3 ASP B 656 LEU B 668 1 13
HELIX 22 AC4 SER B 745 GLU B 750 1 6
HELIX 23 AC5 ASN B 757 GLY B 768 1 12
HELIX 24 AC6 ASP B 773 THR B 788 1 16
HELIX 25 AC7 LYS C 472 ALA C 515 1 44
HELIX 26 AC8 ALA C 515 GLY C 520 1 6
HELIX 27 AC9 GLU C 549 ILE C 553 1 5
HELIX 28 AD1 ILE C 553 LEU C 562 1 10
HELIX 29 AD2 ALA C 636 LEU C 651 1 16
HELIX 30 AD3 ASP C 656 LEU C 668 1 13
HELIX 31 AD4 SER C 745 GLU C 750 1 6
HELIX 32 AD5 ASN C 757 GLY C 768 1 12
HELIX 33 AD6 ASP C 773 THR C 788 1 16
HELIX 34 AD7 LYS D 470 HIS D 518 1 49
HELIX 35 AD8 PRO D 556 LEU D 562 1 7
HELIX 36 AD9 ASN D 632 LEU D 651 1 20
HELIX 37 AE1 ASP D 656 LEU D 668 1 13
HELIX 38 AE2 SER D 745 GLU D 750 1 6
HELIX 39 AE3 ASN D 757 GLY D 768 1 12
HELIX 40 AE4 ASP D 773 THR D 788 1 16
SHEET 1 AA1 4 HIS A 525 LEU A 531 0
SHEET 2 AA1 4 ILE A 536 ILE A 542 -1 O THR A 541 N HIS A 525
SHEET 3 AA1 4 SER A 581 SER A 587 -1 O VAL A 583 N MET A 540
SHEET 4 AA1 4 ILE A 566 GLN A 572 -1 N LYS A 569 O ALA A 584
SHEET 1 AA2 5 ARG A 592 ALA A 600 0
SHEET 2 AA2 5 MET A 797 ASP A 805 -1 O VAL A 801 N GLY A 596
SHEET 3 AA2 5 LEU A 740 MET A 744 -1 N LEU A 741 O VAL A 802
SHEET 4 AA2 5 SER A 702 ARG A 706 -1 N LYS A 705 O LEU A 740
SHEET 5 AA2 5 GLN A 709 VAL A 713 -1 O MET A 711 N ILE A 704
SHEET 1 AA3 3 SER A 611 SER A 613 0
SHEET 2 AA3 3 LYS A 621 SER A 627 -1 O SER A 627 N SER A 611
SHEET 3 AA3 3 GLU A 616 LEU A 617 -1 N LEU A 617 O LYS A 621
SHEET 1 AA4 5 SER A 611 SER A 613 0
SHEET 2 AA4 5 LYS A 621 SER A 627 -1 O SER A 627 N SER A 611
SHEET 3 AA4 5 LEU A 680 ASP A 686 -1 O ILE A 685 N TYR A 622
SHEET 4 AA4 5 SER A 691 LYS A 696 -1 O SER A 691 N ASP A 686
SHEET 5 AA4 5 VAL A 730 GLN A 734 -1 O VAL A 731 N PHE A 694
SHEET 1 AA5 4 GLU E 527 LEU E 531 0
SHEET 2 AA5 4 ILE E 536 ILE E 542 -1 O GLU E 539 N GLU E 527
SHEET 3 AA5 4 SER E 581 SER E 587 -1 O PHE E 585 N ILE E 538
SHEET 4 AA5 4 ILE E 566 LEU E 567 -1 N LEU E 567 O GLY E 586
SHEET 1 AA6 4 GLU E 527 LEU E 531 0
SHEET 2 AA6 4 ILE E 536 ILE E 542 -1 O GLU E 539 N GLU E 527
SHEET 3 AA6 4 SER E 581 SER E 587 -1 O PHE E 585 N ILE E 538
SHEET 4 AA6 4 ALA E 570 GLN E 572 -1 N GLU E 571 O HIS E 582
SHEET 1 AA7 5 ARG E 592 ALA E 600 0
SHEET 2 AA7 5 MET E 797 ASP E 805 -1 O ASP E 805 N ARG E 592
SHEET 3 AA7 5 LEU E 740 MET E 744 -1 N MET E 743 O VAL E 800
SHEET 4 AA7 5 SER E 702 ARG E 706 -1 N LYS E 705 O LEU E 740
SHEET 5 AA7 5 GLN E 709 VAL E 713 -1 O VAL E 713 N SER E 702
SHEET 1 AA8 3 SER E 611 SER E 613 0
SHEET 2 AA8 3 LYS E 621 SER E 627 -1 O ALA E 625 N SER E 613
SHEET 3 AA8 3 GLU E 616 LEU E 617 -1 N LEU E 617 O LYS E 621
SHEET 1 AA9 5 SER E 611 SER E 613 0
SHEET 2 AA9 5 LYS E 621 SER E 627 -1 O ALA E 625 N SER E 613
SHEET 3 AA9 5 LEU E 680 ASP E 686 -1 O ILE E 685 N TYR E 622
SHEET 4 AA9 5 SER E 691 LYS E 696 -1 O LEU E 695 N LEU E 682
SHEET 5 AA9 5 VAL E 731 GLN E 734 -1 O VAL E 731 N PHE E 694
SHEET 1 AB1 4 GLU B 527 LEU B 531 0
SHEET 2 AB1 4 ILE B 536 THR B 541 -1 O GLU B 539 N GLU B 527
SHEET 3 AB1 4 HIS B 582 SER B 587 -1 O PHE B 585 N ILE B 538
SHEET 4 AB1 4 ILE B 566 LEU B 567 -1 N LEU B 567 O GLY B 586
SHEET 1 AB2 4 GLU B 527 LEU B 531 0
SHEET 2 AB2 4 ILE B 536 THR B 541 -1 O GLU B 539 N GLU B 527
SHEET 3 AB2 4 HIS B 582 SER B 587 -1 O PHE B 585 N ILE B 538
SHEET 4 AB2 4 ALA B 570 GLU B 571 -1 N GLU B 571 O HIS B 582
SHEET 1 AB3 5 ALA B 597 ALA B 600 0
SHEET 2 AB3 5 MET B 797 ARG B 803 -1 O VAL B 799 N ALA B 598
SHEET 3 AB3 5 LEU B 740 MET B 744 -1 N LEU B 741 O VAL B 802
SHEET 4 AB3 5 SER B 702 ARG B 706 -1 N LYS B 705 O LEU B 740
SHEET 5 AB3 5 GLN B 709 VAL B 713 -1 O MET B 711 N ILE B 704
SHEET 1 AB4 3 SER B 611 SER B 613 0
SHEET 2 AB4 3 LYS B 621 SER B 627 -1 O ALA B 625 N SER B 613
SHEET 3 AB4 3 GLU B 616 LEU B 617 -1 N LEU B 617 O LYS B 621
SHEET 1 AB5 5 SER B 611 SER B 613 0
SHEET 2 AB5 5 LYS B 621 SER B 627 -1 O ALA B 625 N SER B 613
SHEET 3 AB5 5 LEU B 680 ASP B 686 -1 O SER B 683 N ALA B 624
SHEET 4 AB5 5 SER B 691 VAL B 697 -1 O SER B 691 N ASP B 686
SHEET 5 AB5 5 VAL B 731 GLN B 734 -1 O GLU B 733 N CYS B 692
SHEET 1 AB6 4 GLU C 527 LEU C 531 0
SHEET 2 AB6 4 ILE C 536 MET C 540 -1 O ASP C 537 N SER C 530
SHEET 3 AB6 4 HIS C 582 SER C 587 -1 O PHE C 585 N ILE C 538
SHEET 4 AB6 4 ILE C 566 GLU C 571 -1 N LYS C 569 O ALA C 584
SHEET 1 AB7 5 ARG C 592 ALA C 600 0
SHEET 2 AB7 5 MET C 797 ASP C 805 -1 O VAL C 801 N GLY C 596
SHEET 3 AB7 5 LEU C 740 MET C 744 -1 N LEU C 741 O VAL C 802
SHEET 4 AB7 5 SER C 702 ARG C 706 -1 N LYS C 705 O LEU C 740
SHEET 5 AB7 5 GLN C 709 VAL C 713 -1 O MET C 711 N ILE C 704
SHEET 1 AB8 3 SER C 611 SER C 613 0
SHEET 2 AB8 3 LYS C 621 SER C 627 -1 O SER C 627 N SER C 611
SHEET 3 AB8 3 GLU C 616 LEU C 617 -1 N LEU C 617 O LYS C 621
SHEET 1 AB9 5 SER C 611 SER C 613 0
SHEET 2 AB9 5 LYS C 621 SER C 627 -1 O SER C 627 N SER C 611
SHEET 3 AB9 5 LEU C 680 ASP C 686 -1 O SER C 683 N ALA C 624
SHEET 4 AB9 5 SER C 691 LYS C 696 -1 O SER C 691 N ASP C 686
SHEET 5 AB9 5 VAL C 731 GLN C 734 -1 O VAL C 731 N PHE C 694
SHEET 1 AC1 4 GLU D 527 LEU D 531 0
SHEET 2 AC1 4 ILE D 536 PRO D 543 -1 O ASP D 537 N SER D 530
SHEET 3 AC1 4 TYR D 580 SER D 587 -1 O SER D 581 N ILE D 542
SHEET 4 AC1 4 ILE D 566 LEU D 567 -1 N LEU D 567 O GLY D 586
SHEET 1 AC2 4 GLU D 527 LEU D 531 0
SHEET 2 AC2 4 ILE D 536 PRO D 543 -1 O ASP D 537 N SER D 530
SHEET 3 AC2 4 TYR D 580 SER D 587 -1 O SER D 581 N ILE D 542
SHEET 4 AC2 4 ALA D 570 GLU D 571 -1 N GLU D 571 O HIS D 582
SHEET 1 AC3 5 ARG D 592 ALA D 600 0
SHEET 2 AC3 5 MET D 797 ASP D 805 -1 O VAL D 801 N GLY D 596
SHEET 3 AC3 5 LEU D 740 MET D 744 -1 N LEU D 741 O VAL D 802
SHEET 4 AC3 5 SER D 702 ARG D 706 -1 N LYS D 705 O LEU D 740
SHEET 5 AC3 5 GLN D 709 VAL D 713 -1 O MET D 711 N ILE D 704
SHEET 1 AC4 3 SER D 611 SER D 613 0
SHEET 2 AC4 3 LYS D 621 ASP D 628 -1 O ALA D 625 N SER D 613
SHEET 3 AC4 3 GLU D 616 LEU D 617 -1 N LEU D 617 O LYS D 621
SHEET 1 AC5 5 SER D 611 SER D 613 0
SHEET 2 AC5 5 LYS D 621 ASP D 628 -1 O ALA D 625 N SER D 613
SHEET 3 AC5 5 THR D 679 ASP D 686 -1 O ILE D 685 N TYR D 622
SHEET 4 AC5 5 SER D 691 LYS D 696 -1 O SER D 691 N ASP D 686
SHEET 5 AC5 5 VAL D 730 GLN D 734 -1 O GLU D 733 N CYS D 692
CRYST1 125.622 125.622 330.696 90.00 90.00 90.00 P 43 21 2 40
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 0.007960 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003024 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
