LinkDB: 4HPE
Original site: 4HPE
Chemical substance (4) PDB-CCD (4) Gene (2) KEGG GENES (2) Protein sequence (7) UniProt (1) PDBSTR (6) Protein domain (5) InterPro (5) All databases (18)
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HEADER HYDROLASE 23-OCT-12 4HPE
TITLE CRYSTAL STRUCTURE OF A PUTATIVE CELL WALL HYDROLASE (CD630_03720) FROM
TITLE 2 CLOSTRIDIUM DIFFICILE 630 AT 2.38 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CELL WALL HYDROLASE TN916-LIKE,CTN1-ORF17;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 29-335;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM DIFFICILE;
SOURCE 3 ORGANISM_TAXID: 272563;
SOURCE 4 STRAIN: 630;
SOURCE 5 GENE: CD630_03720, YP_001086839.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS TWO DOMAINS PROTEIN, SLT/LYSOZYME-LIKE MURAMIDASE, NLPC/P60 LD
KEYWDS 2 ENDOPEPTIDASE, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 06-DEC-23 4HPE 1 REMARK
REVDAT 4 20-SEP-23 4HPE 1 REMARK
REVDAT 3 01-FEB-23 4HPE 1 REMARK SEQADV LINK
REVDAT 2 15-NOV-17 4HPE 1 REMARK
REVDAT 1 28-NOV-12 4HPE 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE CELL WALL HYDROLASE
JRNL TITL 2 (CD630_03720) FROM CLOSTRIDIUM DIFFICILE 630 AT 2.38 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 76620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 3897
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.62
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5072
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2048
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4805
REMARK 3 BIN R VALUE (WORKING SET) : 0.2028
REMARK 3 BIN FREE R VALUE : 0.2399
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.26
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.49640
REMARK 3 B22 (A**2) : 1.26620
REMARK 3 B33 (A**2) : 6.23020
REMARK 3 B12 (A**2) : 1.78990
REMARK 3 B13 (A**2) : 3.64590
REMARK 3 B23 (A**2) : 0.72640
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.325
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13685 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 18559 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 6078 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 361 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2011 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13685 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1673 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 15948 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.23
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.73
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5140 2.6826 -48.1151
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: -0.1005
REMARK 3 T33: -0.1081 T12: 0.1007
REMARK 3 T13: -0.0082 T23: 0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 0.5531 L22: 1.3434
REMARK 3 L33: 1.1190 L12: -0.1506
REMARK 3 L13: 0.1328 L23: -0.5546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0508 S12: -0.0692 S13: -0.0227
REMARK 3 S21: 0.0986 S22: -0.0651 S23: -0.0931
REMARK 3 S31: -0.1084 S32: 0.1061 S33: 0.1160
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7688 27.8097 -70.4707
REMARK 3 T TENSOR
REMARK 3 T11: 0.0566 T22: -0.0630
REMARK 3 T33: -0.1003 T12: 0.0869
REMARK 3 T13: -0.0354 T23: 0.1181
REMARK 3 L TENSOR
REMARK 3 L11: 1.7177 L22: 1.9407
REMARK 3 L33: 2.8439 L12: 0.0945
REMARK 3 L13: 0.6517 L23: -0.1333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.2420 S13: 0.0590
REMARK 3 S21: 0.1031 S22: -0.2160 S23: -0.4924
REMARK 3 S31: -0.1687 S32: 0.4846 S33: 0.1681
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {B|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9915 38.0744 -68.7990
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: -0.1936
REMARK 3 T33: -0.1934 T12: 0.1494
REMARK 3 T13: 0.0775 T23: 0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 1.4567 L22: 2.7885
REMARK 3 L33: 2.0915 L12: -0.7858
REMARK 3 L13: 1.1517 L23: -1.2394
REMARK 3 S TENSOR
REMARK 3 S11: 0.0358 S12: -0.0159 S13: 0.0160
REMARK 3 S21: 0.3328 S22: 0.0272 S23: 0.0766
REMARK 3 S31: -0.0465 S32: 0.0089 S33: -0.0630
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {B|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7307 8.5948 -52.6701
REMARK 3 T TENSOR
REMARK 3 T11: 0.1400 T22: -0.1451
REMARK 3 T33: -0.0835 T12: 0.1920
REMARK 3 T13: 0.1264 T23: 0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 1.4896 L22: 2.4737
REMARK 3 L33: 1.6373 L12: -0.1979
REMARK 3 L13: 0.0787 L23: -0.0178
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.0657 S13: -0.0725
REMARK 3 S21: 0.2365 S22: 0.0285 S23: 0.4853
REMARK 3 S31: -0.1712 S32: -0.2972 S33: -0.0096
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {C|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4518 -28.1400 -62.5314
REMARK 3 T TENSOR
REMARK 3 T11: 0.0937 T22: -0.0461
REMARK 3 T33: -0.0955 T12: 0.0860
REMARK 3 T13: 0.1133 T23: 0.0743
REMARK 3 L TENSOR
REMARK 3 L11: 0.6314 L22: 0.6925
REMARK 3 L33: 1.4763 L12: 0.3609
REMARK 3 L13: 0.0194 L23: -0.3602
REMARK 3 S TENSOR
REMARK 3 S11: -0.0432 S12: 0.0091 S13: 0.0191
REMARK 3 S21: -0.0018 S22: 0.0563 S23: 0.0424
REMARK 3 S31: 0.0842 S32: -0.1635 S33: -0.0131
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {C|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1192 -26.3928 -95.9628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1024 T22: -0.0039
REMARK 3 T33: -0.2449 T12: -0.0547
REMARK 3 T13: 0.0182 T23: 0.1152
REMARK 3 L TENSOR
REMARK 3 L11: 2.6132 L22: 3.0066
REMARK 3 L33: 2.3265 L12: 0.6231
REMARK 3 L13: 0.2111 L23: -0.4225
REMARK 3 S TENSOR
REMARK 3 S11: 0.0881 S12: 0.0926 S13: 0.0838
REMARK 3 S21: -0.2163 S22: 0.0054 S23: 0.2383
REMARK 3 S31: 0.3077 S32: -0.4559 S33: -0.0936
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {D|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8142 -10.3058 -21.9531
REMARK 3 T TENSOR
REMARK 3 T11: -0.0579 T22: -0.0351
REMARK 3 T33: -0.1104 T12: 0.0901
REMARK 3 T13: 0.0892 T23: 0.0857
REMARK 3 L TENSOR
REMARK 3 L11: 0.8693 L22: 2.2466
REMARK 3 L33: 4.5936 L12: 0.3280
REMARK 3 L13: 1.0118 L23: 1.2970
REMARK 3 S TENSOR
REMARK 3 S11: -0.0750 S12: 0.0421 S13: 0.2009
REMARK 3 S21: -0.0149 S22: 0.0980 S23: -0.2705
REMARK 3 S31: -0.3555 S32: 0.5191 S33: -0.0231
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {D|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9954 -41.5729 -32.9324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0351 T22: -0.0290
REMARK 3 T33: -0.1056 T12: 0.1593
REMARK 3 T13: 0.1269 T23: 0.1060
REMARK 3 L TENSOR
REMARK 3 L11: 1.7599 L22: 1.8592
REMARK 3 L33: 2.7591 L12: 0.0349
REMARK 3 L13: -0.9780 L23: -0.7304
REMARK 3 S TENSOR
REMARK 3 S11: -0.1251 S12: -0.2280 S13: -0.2647
REMARK 3 S21: -0.0620 S22: 0.0228 S23: -0.1695
REMARK 3 S31: 0.3356 S32: 0.2398 S33: 0.1023
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {E|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9603 -40.1766 -35.9554
REMARK 3 T TENSOR
REMARK 3 T11: -0.0923 T22: 0.0259
REMARK 3 T33: -0.1638 T12: 0.0565
REMARK 3 T13: 0.0588 T23: 0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 1.0567 L22: 5.3561
REMARK 3 L33: 2.2323 L12: 0.8730
REMARK 3 L13: 0.4968 L23: -0.3111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: -0.0882 S13: -0.0594
REMARK 3 S21: -0.1520 S22: 0.0903 S23: 0.5422
REMARK 3 S31: 0.3060 S32: -0.4308 S33: -0.0717
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {E|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 63.6967 -11.7331 -18.9842
REMARK 3 T TENSOR
REMARK 3 T11: 0.0136 T22: -0.0074
REMARK 3 T33: -0.1279 T12: 0.1966
REMARK 3 T13: 0.0748 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 2.2197 L22: 1.8030
REMARK 3 L33: 3.2095 L12: -0.6363
REMARK 3 L13: 0.6748 L23: -0.7814
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: -0.2124 S13: 0.1153
REMARK 3 S21: 0.1058 S22: 0.0467 S23: 0.1566
REMARK 3 S31: -0.2772 S32: -0.3965 S33: -0.0304
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {F|43 - 205}
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6023 23.7975 -16.6521
REMARK 3 T TENSOR
REMARK 3 T11: 0.2321 T22: -0.2319
REMARK 3 T33: -0.3042 T12: 0.1556
REMARK 3 T13: 0.1731 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 1.0205 L22: 3.3970
REMARK 3 L33: 5.1954 L12: 0.6018
REMARK 3 L13: -0.4204 L23: -1.7730
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: 0.2563 S13: -0.0999
REMARK 3 S21: -0.4850 S22: -0.0044 S23: -0.1831
REMARK 3 S31: 0.3975 S32: 0.2216 S33: 0.0050
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {F|210 - 335}
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9928 29.7123 16.3272
REMARK 3 T TENSOR
REMARK 3 T11: 0.0686 T22: -0.1108
REMARK 3 T33: -0.0370 T12: 0.1345
REMARK 3 T13: 0.1020 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 0.7824 L22: 2.7530
REMARK 3 L33: 1.6823 L12: -0.2261
REMARK 3 L13: 0.1563 L23: 0.0037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: -0.0888 S13: 0.1544
REMARK 3 S21: -0.0721 S22: -0.0116 S23: -0.4596
REMARK 3 S31: -0.0056 S32: 0.2575 S33: -0.0160
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. A MET-INHIBITION PROTOCOL WAS USED
REMARK 3 FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.
REMARK 3 THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 3. CL AND GOL MODELED ARE PRESENT IN PROTEIN/CRYO
REMARK 3 CONDITIONS. 4. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR
REMARK 3 RESTRAINT REPRESENTATION (-AUTONCS). 5. CYS242 IS OXIDIZED (OCS)
REMARK 3 BASED ON ELECTRON DENSITY.
REMARK 4
REMARK 4 4HPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : RHODIUM-COATED VERTICAL AND
REMARK 200 HORIZONTAL FOCUSING MIRRORS;
REMARK 200 LIQUID-NITROGEN COOLED DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE MARCH 15, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76631
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 49.396
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: 4FDY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.00% 2-PROPANOL, 24.00% POLYETHYLENE
REMARK 280 GLYCOL 4000, 0.1M SODIUM CITRATE - CITRIC ACID PH 5.1, NANODROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 ALA A 29
REMARK 465 ASP A 30
REMARK 465 SER A 31
REMARK 465 ASP A 32
REMARK 465 ASP A 33
REMARK 465 GLU A 34
REMARK 465 ASN A 35
REMARK 465 SER A 36
REMARK 465 ASN A 37
REMARK 465 PHE A 38
REMARK 465 SER A 39
REMARK 465 SER A 40
REMARK 465 GLY A 41
REMARK 465 ILE A 42
REMARK 465 VAL A 206
REMARK 465 PRO A 207
REMARK 465 GLN A 208
REMARK 465 VAL A 209
REMARK 465 GLY B 0
REMARK 465 ALA B 29
REMARK 465 ASP B 30
REMARK 465 SER B 31
REMARK 465 ASP B 32
REMARK 465 ASP B 33
REMARK 465 GLU B 34
REMARK 465 ASN B 35
REMARK 465 SER B 36
REMARK 465 ASN B 37
REMARK 465 PHE B 38
REMARK 465 SER B 39
REMARK 465 SER B 40
REMARK 465 GLY B 41
REMARK 465 ILE B 42
REMARK 465 VAL B 206
REMARK 465 PRO B 207
REMARK 465 GLN B 208
REMARK 465 VAL B 209
REMARK 465 GLY C 0
REMARK 465 ALA C 29
REMARK 465 ASP C 30
REMARK 465 SER C 31
REMARK 465 ASP C 32
REMARK 465 ASP C 33
REMARK 465 GLU C 34
REMARK 465 ASN C 35
REMARK 465 SER C 36
REMARK 465 ASN C 37
REMARK 465 PHE C 38
REMARK 465 SER C 39
REMARK 465 SER C 40
REMARK 465 GLY C 41
REMARK 465 ILE C 42
REMARK 465 VAL C 206
REMARK 465 PRO C 207
REMARK 465 GLN C 208
REMARK 465 VAL C 209
REMARK 465 GLY D 0
REMARK 465 ALA D 29
REMARK 465 ASP D 30
REMARK 465 SER D 31
REMARK 465 ASP D 32
REMARK 465 ASP D 33
REMARK 465 GLU D 34
REMARK 465 ASN D 35
REMARK 465 SER D 36
REMARK 465 ASN D 37
REMARK 465 PHE D 38
REMARK 465 SER D 39
REMARK 465 SER D 40
REMARK 465 GLY D 41
REMARK 465 ILE D 42
REMARK 465 PRO D 207
REMARK 465 GLN D 208
REMARK 465 VAL D 209
REMARK 465 GLY E 0
REMARK 465 ALA E 29
REMARK 465 ASP E 30
REMARK 465 SER E 31
REMARK 465 ASP E 32
REMARK 465 ASP E 33
REMARK 465 GLU E 34
REMARK 465 ASN E 35
REMARK 465 SER E 36
REMARK 465 ASN E 37
REMARK 465 PHE E 38
REMARK 465 SER E 39
REMARK 465 SER E 40
REMARK 465 GLY E 41
REMARK 465 ILE E 42
REMARK 465 VAL E 206
REMARK 465 PRO E 207
REMARK 465 GLN E 208
REMARK 465 VAL E 209
REMARK 465 GLY F 0
REMARK 465 ALA F 29
REMARK 465 ASP F 30
REMARK 465 SER F 31
REMARK 465 ASP F 32
REMARK 465 ASP F 33
REMARK 465 GLU F 34
REMARK 465 ASN F 35
REMARK 465 SER F 36
REMARK 465 ASN F 37
REMARK 465 PHE F 38
REMARK 465 SER F 39
REMARK 465 SER F 40
REMARK 465 GLY F 41
REMARK 465 ILE F 42
REMARK 465 VAL F 206
REMARK 465 PRO F 207
REMARK 465 GLN F 208
REMARK 465 VAL F 209
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 THR A 43 OG1 CG2
REMARK 470 SER A 210 OG
REMARK 470 LYS A 334 CG CD CE NZ
REMARK 470 THR B 43 OG1 CG2
REMARK 470 LYS B 124 CG CD CE NZ
REMARK 470 SER B 210 OG
REMARK 470 GLU B 212 CG CD OE1 OE2
REMARK 470 LYS B 334 CG CD CE NZ
REMARK 470 THR C 43 OG1 CG2
REMARK 470 LYS C 124 CG CD CE NZ
REMARK 470 SER C 210 OG
REMARK 470 GLU C 212 CG CD OE1 OE2
REMARK 470 LYS C 334 CG CD CE NZ
REMARK 470 THR D 43 OG1 CG2
REMARK 470 LYS D 124 CG CD CE NZ
REMARK 470 SER D 210 OG
REMARK 470 GLU D 212 CG CD OE1 OE2
REMARK 470 ASN D 303 CB CG OD1 ND2
REMARK 470 LYS D 334 CG CD CE NZ
REMARK 470 THR E 43 OG1 CG2
REMARK 470 LYS E 124 CG CD CE NZ
REMARK 470 SER E 210 OG
REMARK 470 ASN E 303 CB CG OD1 ND2
REMARK 470 LYS E 334 CG CD CE NZ
REMARK 470 THR F 43 OG1 CG2
REMARK 470 LYS F 124 CG CD CE NZ
REMARK 470 SER F 210 OG
REMARK 470 LYS F 334 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 82 -10.65 -145.98
REMARK 500 ASN A 190 65.96 -67.60
REMARK 500 SER A 239 -168.95 75.92
REMARK 500 SER B 82 -6.66 -141.09
REMARK 500 ASN B 190 64.85 -65.58
REMARK 500 SER B 239 -168.94 75.45
REMARK 500 SER C 82 -7.77 -141.47
REMARK 500 ASN C 190 62.34 -68.57
REMARK 500 SER C 239 -170.28 75.44
REMARK 500 SER D 82 -9.65 -143.94
REMARK 500 ASN D 190 63.25 -65.30
REMARK 500 TYR D 191 119.77 -160.94
REMARK 500 SER D 239 -169.73 73.78
REMARK 500 SER E 82 -8.91 -142.22
REMARK 500 ASN E 190 65.03 -67.87
REMARK 500 TYR E 191 119.50 -162.40
REMARK 500 SER E 239 -170.04 74.26
REMARK 500 SER F 82 -10.38 -142.28
REMARK 500 ASN F 190 63.35 -65.64
REMARK 500 SER F 239 -168.55 73.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-391770 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (29-335) WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 4HPE A 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
DBREF 4HPE B 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
DBREF 4HPE C 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
DBREF 4HPE D 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
DBREF 4HPE E 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
DBREF 4HPE F 29 335 UNP Q18DB2 Q18DB2_CLOD6 29 335
SEQADV 4HPE GLY A 0 UNP Q18DB2 EXPRESSION TAG
SEQADV 4HPE GLY B 0 UNP Q18DB2 EXPRESSION TAG
SEQADV 4HPE GLY C 0 UNP Q18DB2 EXPRESSION TAG
SEQADV 4HPE GLY D 0 UNP Q18DB2 EXPRESSION TAG
SEQADV 4HPE GLY E 0 UNP Q18DB2 EXPRESSION TAG
SEQADV 4HPE GLY F 0 UNP Q18DB2 EXPRESSION TAG
SEQRES 1 A 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 A 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 A 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 A 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 A 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 A 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 A 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 A 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 A 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 A 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 A 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 A 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 A 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 A 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 A 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 A 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 A 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 A 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 A 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 A 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 A 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 A 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 A 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 A 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
SEQRES 1 B 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 B 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 B 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 B 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 B 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 B 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 B 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 B 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 B 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 B 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 B 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 B 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 B 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 B 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 B 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 B 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 B 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 B 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 B 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 B 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 B 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 B 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 B 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 B 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
SEQRES 1 C 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 C 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 C 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 C 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 C 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 C 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 C 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 C 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 C 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 C 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 C 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 C 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 C 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 C 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 C 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 C 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 C 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 C 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 C 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 C 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 C 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 C 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 C 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 C 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
SEQRES 1 D 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 D 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 D 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 D 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 D 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 D 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 D 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 D 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 D 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 D 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 D 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 D 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 D 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 D 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 D 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 D 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 D 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 D 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 D 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 D 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 D 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 D 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 D 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 D 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
SEQRES 1 E 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 E 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 E 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 E 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 E 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 E 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 E 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 E 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 E 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 E 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 E 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 E 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 E 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 E 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 E 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 E 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 E 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 E 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 E 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 E 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 E 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 E 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 E 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 E 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
SEQRES 1 F 308 GLY ALA ASP SER ASP ASP GLU ASN SER ASN PHE SER SER
SEQRES 2 F 308 GLY ILE THR GLY MSE ASN LEU SER ALA GLU VAL LEU LYS
SEQRES 3 F 308 HIS GLN PRO MSE VAL GLU LYS TYR ALA ARG GLU ASN GLY
SEQRES 4 F 308 ILE SER GLU TYR VAL ASN VAL LEU LEU ALA ILE ILE GLN
SEQRES 5 F 308 VAL GLU SER GLY GLY THR ALA GLU ASP VAL MSE GLN SER
SEQRES 6 F 308 SER GLU SER LEU GLY LEU PRO PRO ASN SER LEU ASP THR
SEQRES 7 F 308 GLU SER SER ILE LYS GLN GLY CYS LYS TYR PHE ALA SER
SEQRES 8 F 308 LEU LEU SER SER SER LYS ASN GLN GLY ILE ASP ASP LEU
SEQRES 9 F 308 ASN VAL ALA ILE GLN SER TYR ASN TYR GLY GLY GLY TYR
SEQRES 10 F 308 VAL GLY TYR VAL ALA GLY LYS GLY LYS LYS HIS THR PHE
SEQRES 11 F 308 ASN LEU ALA GLU SER PHE ALA ARG GLU LYS SER GLY GLY
SEQRES 12 F 308 LYS LYS VAL THR TYR THR ASN PRO ILE ALA VAL ALA LYS
SEQRES 13 F 308 ASN GLY GLY TRP ARG TRP ASN TYR GLY ASN MSE PHE TYR
SEQRES 14 F 308 VAL GLU LEU VAL ASN GLN TYR LEU THR VAL PRO GLN VAL
SEQRES 15 F 308 SER GLY GLU LEU ALA GLN LYS VAL MSE ASN GLU ALA LEU
SEQRES 16 F 308 LYS TYR GLN GLY TRP LYS TYR VAL TYR GLY GLY SER ASN
SEQRES 17 F 308 PRO ASN THR SER PHE ASP OCS SER GLY LEU THR GLN TRP
SEQRES 18 F 308 CYS TYR GLY LYS ALA GLY ILE SER LEU PRO ARG THR ALA
SEQRES 19 F 308 GLN ALA GLN TYR ASP ALA THR GLN HIS LEU PRO LEU SER
SEQRES 20 F 308 GLN ALA LYS ALA GLY ASP LEU VAL PHE PHE HIS SER THR
SEQRES 21 F 308 TYR ASN ALA GLY SER TYR VAL THR HIS VAL GLY ILE TYR
SEQRES 22 F 308 VAL GLY ASN ASN GLN MSE TYR HIS ALA GLY ASP PRO ILE
SEQRES 23 F 308 GLY TYR ALA ASP LEU SER SER SER TYR TRP GLN GLN HIS
SEQRES 24 F 308 LEU ILE GLY ALA GLY ARG VAL LYS GLN
MODRES 4HPE MSE A 45 MET SELENOMETHIONINE
MODRES 4HPE MSE A 57 MET SELENOMETHIONINE
MODRES 4HPE MSE A 90 MET SELENOMETHIONINE
MODRES 4HPE MSE A 194 MET SELENOMETHIONINE
MODRES 4HPE MSE A 218 MET SELENOMETHIONINE
MODRES 4HPE OCS A 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE A 306 MET SELENOMETHIONINE
MODRES 4HPE MSE B 45 MET SELENOMETHIONINE
MODRES 4HPE MSE B 57 MET SELENOMETHIONINE
MODRES 4HPE MSE B 90 MET SELENOMETHIONINE
MODRES 4HPE MSE B 194 MET SELENOMETHIONINE
MODRES 4HPE MSE B 218 MET SELENOMETHIONINE
MODRES 4HPE OCS B 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE B 306 MET SELENOMETHIONINE
MODRES 4HPE MSE C 45 MET SELENOMETHIONINE
MODRES 4HPE MSE C 57 MET SELENOMETHIONINE
MODRES 4HPE MSE C 90 MET SELENOMETHIONINE
MODRES 4HPE MSE C 194 MET SELENOMETHIONINE
MODRES 4HPE MSE C 218 MET SELENOMETHIONINE
MODRES 4HPE OCS C 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE C 306 MET SELENOMETHIONINE
MODRES 4HPE MSE D 45 MET SELENOMETHIONINE
MODRES 4HPE MSE D 57 MET SELENOMETHIONINE
MODRES 4HPE MSE D 90 MET SELENOMETHIONINE
MODRES 4HPE MSE D 194 MET SELENOMETHIONINE
MODRES 4HPE MSE D 218 MET SELENOMETHIONINE
MODRES 4HPE OCS D 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE D 306 MET SELENOMETHIONINE
MODRES 4HPE MSE E 45 MET SELENOMETHIONINE
MODRES 4HPE MSE E 57 MET SELENOMETHIONINE
MODRES 4HPE MSE E 90 MET SELENOMETHIONINE
MODRES 4HPE MSE E 194 MET SELENOMETHIONINE
MODRES 4HPE MSE E 218 MET SELENOMETHIONINE
MODRES 4HPE OCS E 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE E 306 MET SELENOMETHIONINE
MODRES 4HPE MSE F 45 MET SELENOMETHIONINE
MODRES 4HPE MSE F 57 MET SELENOMETHIONINE
MODRES 4HPE MSE F 90 MET SELENOMETHIONINE
MODRES 4HPE MSE F 194 MET SELENOMETHIONINE
MODRES 4HPE MSE F 218 MET SELENOMETHIONINE
MODRES 4HPE OCS F 242 CYS CYSTEINESULFONIC ACID
MODRES 4HPE MSE F 306 MET SELENOMETHIONINE
HET MSE A 45 8
HET MSE A 57 8
HET MSE A 90 8
HET MSE A 194 8
HET MSE A 218 8
HET OCS A 242 9
HET MSE A 306 8
HET MSE B 45 8
HET MSE B 57 8
HET MSE B 90 8
HET MSE B 194 8
HET MSE B 218 8
HET OCS B 242 9
HET MSE B 306 8
HET MSE C 45 8
HET MSE C 57 8
HET MSE C 90 8
HET MSE C 194 8
HET MSE C 218 8
HET OCS C 242 9
HET MSE C 306 8
HET MSE D 45 8
HET MSE D 57 8
HET MSE D 90 8
HET MSE D 194 8
HET MSE D 218 8
HET OCS D 242 9
HET MSE D 306 8
HET MSE E 45 8
HET MSE E 57 8
HET MSE E 90 8
HET MSE E 194 8
HET MSE E 218 8
HET OCS E 242 9
HET MSE E 306 8
HET MSE F 45 8
HET MSE F 57 8
HET MSE F 90 8
HET MSE F 194 8
HET MSE F 218 8
HET OCS F 242 9
HET MSE F 306 8
HET CL A 401 1
HET CL A 402 1
HET CL A 403 1
HET CL A 404 1
HET GOL A 405 6
HET GOL A 406 6
HET CL B 401 1
HET GOL B 402 6
HET CL C 401 1
HET CL D 401 1
HET GOL D 402 6
HET CL E 401 1
HET CL F 401 1
HETNAM MSE SELENOMETHIONINE
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 1 OCS 6(C3 H7 N O5 S)
FORMUL 7 CL 9(CL 1-)
FORMUL 11 GOL 4(C3 H8 O3)
FORMUL 20 HOH *590(H2 O)
HELIX 1 1 SER A 48 LYS A 53 1 6
HELIX 2 2 HIS A 54 ASN A 65 1 12
HELIX 3 3 ILE A 67 GLU A 69 5 3
HELIX 4 4 TYR A 70 SER A 82 1 13
HELIX 5 5 SER A 93 GLY A 97 5 5
HELIX 6 6 ASP A 104 GLN A 126 1 23
HELIX 7 7 ASP A 130 GLY A 141 1 12
HELIX 8 8 GLY A 142 GLY A 150 1 9
HELIX 9 9 THR A 156 GLY A 169 1 14
HELIX 10 10 ASN A 177 GLY A 185 1 9
HELIX 11 11 PHE A 195 GLN A 202 1 8
HELIX 12 12 GLY A 211 LEU A 222 1 12
HELIX 13 13 LYS A 223 GLN A 225 5 3
HELIX 14 14 ASP A 241 ALA A 253 1 13
HELIX 15 15 THR A 260 ALA A 267 1 8
HELIX 16 16 PRO A 272 ALA A 276 5 5
HELIX 17 17 SER A 320 HIS A 326 1 7
HELIX 18 18 SER B 48 LYS B 53 1 6
HELIX 19 19 HIS B 54 ASN B 65 1 12
HELIX 20 20 ILE B 67 GLU B 69 5 3
HELIX 21 21 TYR B 70 GLY B 83 1 14
HELIX 22 22 SER B 93 GLY B 97 5 5
HELIX 23 23 ASP B 104 GLN B 126 1 23
HELIX 24 24 ASP B 130 GLY B 141 1 12
HELIX 25 25 GLY B 142 GLY B 150 1 9
HELIX 26 26 THR B 156 GLY B 169 1 14
HELIX 27 27 ASN B 177 GLY B 185 1 9
HELIX 28 28 PHE B 195 GLN B 202 1 8
HELIX 29 29 GLY B 211 LEU B 222 1 12
HELIX 30 30 LYS B 223 GLN B 225 5 3
HELIX 31 31 ASP B 241 ALA B 253 1 13
HELIX 32 32 THR B 260 ALA B 267 1 8
HELIX 33 33 PRO B 272 ALA B 276 5 5
HELIX 34 34 SER B 320 HIS B 326 1 7
HELIX 35 35 SER C 48 LYS C 53 1 6
HELIX 36 36 HIS C 54 ASN C 65 1 12
HELIX 37 37 ILE C 67 GLU C 69 5 3
HELIX 38 38 TYR C 70 GLY C 83 1 14
HELIX 39 39 SER C 93 GLY C 97 5 5
HELIX 40 40 ASP C 104 GLN C 126 1 23
HELIX 41 41 ASP C 130 GLY C 141 1 12
HELIX 42 42 GLY C 142 GLY C 150 1 9
HELIX 43 43 THR C 156 GLY C 169 1 14
HELIX 44 44 ASN C 177 GLY C 185 1 9
HELIX 45 45 PHE C 195 GLN C 202 1 8
HELIX 46 46 GLY C 211 LEU C 222 1 12
HELIX 47 47 LYS C 223 GLN C 225 5 3
HELIX 48 48 ASP C 241 ALA C 253 1 13
HELIX 49 49 THR C 260 ALA C 267 1 8
HELIX 50 50 PRO C 272 ALA C 276 5 5
HELIX 51 51 SER C 320 HIS C 326 1 7
HELIX 52 52 SER D 48 LYS D 53 1 6
HELIX 53 53 HIS D 54 ASN D 65 1 12
HELIX 54 54 ILE D 67 GLU D 69 5 3
HELIX 55 55 TYR D 70 GLY D 83 1 14
HELIX 56 56 SER D 93 GLY D 97 5 5
HELIX 57 57 ASP D 104 GLN D 126 1 23
HELIX 58 58 ASP D 130 GLY D 141 1 12
HELIX 59 59 GLY D 142 GLY D 150 1 9
HELIX 60 60 THR D 156 GLY D 169 1 14
HELIX 61 61 ASN D 177 GLY D 185 1 9
HELIX 62 62 PHE D 195 GLN D 202 1 8
HELIX 63 63 GLY D 211 LEU D 222 1 12
HELIX 64 64 LYS D 223 GLN D 225 5 3
HELIX 65 65 ASP D 241 ALA D 253 1 13
HELIX 66 66 THR D 260 ALA D 267 1 8
HELIX 67 67 PRO D 272 ALA D 276 5 5
HELIX 68 68 SER D 320 HIS D 326 1 7
HELIX 69 69 SER E 48 LYS E 53 1 6
HELIX 70 70 HIS E 54 ASN E 65 1 12
HELIX 71 71 ILE E 67 GLU E 69 5 3
HELIX 72 72 TYR E 70 SER E 82 1 13
HELIX 73 73 SER E 93 GLY E 97 5 5
HELIX 74 74 ASP E 104 GLN E 126 1 23
HELIX 75 75 ASP E 130 GLY E 141 1 12
HELIX 76 76 GLY E 142 GLY E 150 1 9
HELIX 77 77 THR E 156 GLY E 169 1 14
HELIX 78 78 ASN E 177 GLY E 185 1 9
HELIX 79 79 PHE E 195 GLN E 202 1 8
HELIX 80 80 GLY E 211 LEU E 222 1 12
HELIX 81 81 LYS E 223 GLN E 225 5 3
HELIX 82 82 ASP E 241 ALA E 253 1 13
HELIX 83 83 THR E 260 ALA E 267 1 8
HELIX 84 84 PRO E 272 ALA E 276 5 5
HELIX 85 85 SER E 320 HIS E 326 1 7
HELIX 86 86 SER F 48 LYS F 53 1 6
HELIX 87 87 HIS F 54 ASN F 65 1 12
HELIX 88 88 ILE F 67 GLU F 69 5 3
HELIX 89 89 TYR F 70 GLY F 83 1 14
HELIX 90 90 SER F 93 GLY F 97 5 5
HELIX 91 91 ASP F 104 GLN F 126 1 23
HELIX 92 92 ASP F 130 GLY F 141 1 12
HELIX 93 93 GLY F 142 GLY F 150 1 9
HELIX 94 94 THR F 156 GLY F 169 1 14
HELIX 95 95 ASN F 177 GLY F 185 1 9
HELIX 96 96 PHE F 195 GLN F 202 1 8
HELIX 97 97 GLY F 211 LEU F 222 1 12
HELIX 98 98 LYS F 223 GLN F 225 5 3
HELIX 99 99 ASP F 241 ALA F 253 1 13
HELIX 100 100 THR F 260 ALA F 267 1 8
HELIX 101 101 PRO F 272 ALA F 276 5 5
HELIX 102 102 SER F 320 HIS F 326 1 7
SHEET 1 A 2 LYS A 172 THR A 174 0
SHEET 2 A 2 TRP A 187 TRP A 189 -1 O ARG A 188 N VAL A 173
SHEET 1 B 2 SER A 234 ASN A 235 0
SHEET 2 B 2 SER A 239 PHE A 240 -1 O SER A 239 N ASN A 235
SHEET 1 C 6 GLN A 269 LEU A 271 0
SHEET 2 C 6 LEU A 327 ARG A 332 -1 O ARG A 332 N GLN A 269
SHEET 3 C 6 LEU A 281 HIS A 285 -1 N PHE A 283 O GLY A 329
SHEET 4 C 6 VAL A 294 TYR A 300 -1 O THR A 295 N PHE A 284
SHEET 5 C 6 GLN A 305 HIS A 308 -1 O TYR A 307 N ILE A 299
SHEET 6 C 6 GLY A 314 ASP A 317 -1 O GLY A 314 N HIS A 308
SHEET 1 D 2 LYS B 172 THR B 174 0
SHEET 2 D 2 TRP B 187 TRP B 189 -1 O ARG B 188 N VAL B 173
SHEET 1 E 2 SER B 234 ASN B 235 0
SHEET 2 E 2 SER B 239 PHE B 240 -1 O SER B 239 N ASN B 235
SHEET 1 F 6 GLN B 269 LEU B 271 0
SHEET 2 F 6 LEU B 327 ARG B 332 -1 O ARG B 332 N GLN B 269
SHEET 3 F 6 LEU B 281 HIS B 285 -1 N PHE B 283 O GLY B 329
SHEET 4 F 6 VAL B 294 TYR B 300 -1 O HIS B 296 N PHE B 284
SHEET 5 F 6 GLN B 305 HIS B 308 -1 O TYR B 307 N ILE B 299
SHEET 6 F 6 GLY B 314 ASP B 317 -1 O GLY B 314 N HIS B 308
SHEET 1 G 2 LYS C 172 THR C 174 0
SHEET 2 G 2 TRP C 187 TRP C 189 -1 O ARG C 188 N VAL C 173
SHEET 1 H 2 SER C 234 ASN C 235 0
SHEET 2 H 2 SER C 239 PHE C 240 -1 O SER C 239 N ASN C 235
SHEET 1 I 6 GLN C 269 LEU C 271 0
SHEET 2 I 6 LEU C 327 ARG C 332 -1 O ARG C 332 N GLN C 269
SHEET 3 I 6 LEU C 281 HIS C 285 -1 N LEU C 281 O GLY C 331
SHEET 4 I 6 VAL C 294 TYR C 300 -1 O THR C 295 N PHE C 284
SHEET 5 I 6 GLN C 305 HIS C 308 -1 O TYR C 307 N ILE C 299
SHEET 6 I 6 GLY C 314 ASP C 317 -1 O GLY C 314 N HIS C 308
SHEET 1 J 2 LYS D 172 THR D 174 0
SHEET 2 J 2 TRP D 187 TRP D 189 -1 O ARG D 188 N VAL D 173
SHEET 1 K 2 SER D 234 ASN D 235 0
SHEET 2 K 2 SER D 239 PHE D 240 -1 O SER D 239 N ASN D 235
SHEET 1 L 6 GLN D 269 LEU D 271 0
SHEET 2 L 6 LEU D 327 ARG D 332 -1 O ARG D 332 N GLN D 269
SHEET 3 L 6 LEU D 281 HIS D 285 -1 N LEU D 281 O GLY D 331
SHEET 4 L 6 VAL D 294 TYR D 300 -1 O HIS D 296 N PHE D 284
SHEET 5 L 6 GLN D 305 HIS D 308 -1 O TYR D 307 N ILE D 299
SHEET 6 L 6 GLY D 314 ASP D 317 -1 O GLY D 314 N HIS D 308
SHEET 1 M 2 LYS E 172 THR E 174 0
SHEET 2 M 2 TRP E 187 TRP E 189 -1 O ARG E 188 N VAL E 173
SHEET 1 N 2 SER E 234 ASN E 235 0
SHEET 2 N 2 SER E 239 PHE E 240 -1 O SER E 239 N ASN E 235
SHEET 1 O 6 GLN E 269 LEU E 271 0
SHEET 2 O 6 LEU E 327 ARG E 332 -1 O ARG E 332 N GLN E 269
SHEET 3 O 6 LEU E 281 HIS E 285 -1 N LEU E 281 O GLY E 331
SHEET 4 O 6 VAL E 294 GLY E 302 -1 O THR E 295 N PHE E 284
SHEET 5 O 6 GLN E 305 HIS E 308 -1 O TYR E 307 N ILE E 299
SHEET 6 O 6 GLY E 314 ASP E 317 -1 O GLY E 314 N HIS E 308
SHEET 1 P 2 LYS F 172 THR F 174 0
SHEET 2 P 2 TRP F 187 TRP F 189 -1 O ARG F 188 N VAL F 173
SHEET 1 Q 2 SER F 234 ASN F 235 0
SHEET 2 Q 2 SER F 239 PHE F 240 -1 O SER F 239 N ASN F 235
SHEET 1 R 6 GLN F 269 LEU F 271 0
SHEET 2 R 6 LEU F 327 ARG F 332 -1 O ARG F 332 N GLN F 269
SHEET 3 R 6 LEU F 281 HIS F 285 -1 N PHE F 283 O GLY F 329
SHEET 4 R 6 VAL F 294 TYR F 300 -1 O THR F 295 N PHE F 284
SHEET 5 R 6 GLN F 305 HIS F 308 -1 O TYR F 307 N ILE F 299
SHEET 6 R 6 GLY F 314 ASP F 317 -1 O GLY F 314 N HIS F 308
LINK C GLY A 44 N MSE A 45 1555 1555 1.35
LINK C MSE A 45 N ASN A 46 1555 1555 1.36
LINK C PRO A 56 N MSE A 57 1555 1555 1.34
LINK C MSE A 57 N VAL A 58 1555 1555 1.35
LINK C VAL A 89 N MSE A 90 1555 1555 1.33
LINK C MSE A 90 N GLN A 91 1555 1555 1.38
LINK C ASN A 193 N MSE A 194 1555 1555 1.37
LINK C MSE A 194 N PHE A 195 1555 1555 1.34
LINK C VAL A 217 N MSE A 218 1555 1555 1.35
LINK C MSE A 218 N ASN A 219 1555 1555 1.36
LINK C ASP A 241 N OCS A 242 1555 1555 1.33
LINK C OCS A 242 N SER A 243 1555 1555 1.35
LINK C GLN A 305 N MSE A 306 1555 1555 1.32
LINK C MSE A 306 N TYR A 307 1555 1555 1.33
LINK C GLY B 44 N MSE B 45 1555 1555 1.35
LINK C MSE B 45 N ASN B 46 1555 1555 1.36
LINK C PRO B 56 N MSE B 57 1555 1555 1.35
LINK C MSE B 57 N VAL B 58 1555 1555 1.33
LINK C VAL B 89 N MSE B 90 1555 1555 1.33
LINK C MSE B 90 N GLN B 91 1555 1555 1.36
LINK C ASN B 193 N MSE B 194 1555 1555 1.34
LINK C MSE B 194 N PHE B 195 1555 1555 1.35
LINK C VAL B 217 N MSE B 218 1555 1555 1.35
LINK C MSE B 218 N ASN B 219 1555 1555 1.35
LINK C ASP B 241 N OCS B 242 1555 1555 1.34
LINK C OCS B 242 N SER B 243 1555 1555 1.33
LINK C GLN B 305 N MSE B 306 1555 1555 1.33
LINK C MSE B 306 N TYR B 307 1555 1555 1.33
LINK C GLY C 44 N MSE C 45 1555 1555 1.35
LINK C MSE C 45 N ASN C 46 1555 1555 1.35
LINK C PRO C 56 N MSE C 57 1555 1555 1.36
LINK C MSE C 57 N VAL C 58 1555 1555 1.33
LINK C VAL C 89 N MSE C 90 1555 1555 1.33
LINK C MSE C 90 N GLN C 91 1555 1555 1.36
LINK C ASN C 193 N MSE C 194 1555 1555 1.36
LINK C MSE C 194 N PHE C 195 1555 1555 1.36
LINK C VAL C 217 N MSE C 218 1555 1555 1.35
LINK C MSE C 218 N ASN C 219 1555 1555 1.35
LINK C ASP C 241 N OCS C 242 1555 1555 1.34
LINK C OCS C 242 N SER C 243 1555 1555 1.35
LINK C GLN C 305 N MSE C 306 1555 1555 1.34
LINK C MSE C 306 N TYR C 307 1555 1555 1.34
LINK C GLY D 44 N MSE D 45 1555 1555 1.35
LINK C MSE D 45 N ASN D 46 1555 1555 1.35
LINK C PRO D 56 N MSE D 57 1555 1555 1.35
LINK C MSE D 57 N VAL D 58 1555 1555 1.32
LINK C VAL D 89 N MSE D 90 1555 1555 1.34
LINK C MSE D 90 N GLN D 91 1555 1555 1.36
LINK C ASN D 193 N MSE D 194 1555 1555 1.35
LINK C MSE D 194 N PHE D 195 1555 1555 1.35
LINK C VAL D 217 N MSE D 218 1555 1555 1.35
LINK C MSE D 218 N ASN D 219 1555 1555 1.35
LINK C ASP D 241 N OCS D 242 1555 1555 1.32
LINK C OCS D 242 N SER D 243 1555 1555 1.34
LINK C GLN D 305 N MSE D 306 1555 1555 1.34
LINK C MSE D 306 N TYR D 307 1555 1555 1.33
LINK C GLY E 44 N MSE E 45 1555 1555 1.35
LINK C MSE E 45 N ASN E 46 1555 1555 1.36
LINK C PRO E 56 N MSE E 57 1555 1555 1.35
LINK C MSE E 57 N VAL E 58 1555 1555 1.33
LINK C VAL E 89 N MSE E 90 1555 1555 1.35
LINK C MSE E 90 N GLN E 91 1555 1555 1.36
LINK C ASN E 193 N MSE E 194 1555 1555 1.34
LINK C MSE E 194 N PHE E 195 1555 1555 1.36
LINK C VAL E 217 N MSE E 218 1555 1555 1.33
LINK C MSE E 218 N ASN E 219 1555 1555 1.35
LINK C ASP E 241 N OCS E 242 1555 1555 1.32
LINK C OCS E 242 N SER E 243 1555 1555 1.34
LINK C GLN E 305 N MSE E 306 1555 1555 1.33
LINK C MSE E 306 N TYR E 307 1555 1555 1.34
LINK C GLY F 44 N MSE F 45 1555 1555 1.36
LINK C MSE F 45 N ASN F 46 1555 1555 1.35
LINK C PRO F 56 N MSE F 57 1555 1555 1.35
LINK C MSE F 57 N VAL F 58 1555 1555 1.33
LINK C VAL F 89 N MSE F 90 1555 1555 1.34
LINK C MSE F 90 N GLN F 91 1555 1555 1.38
LINK C ASN F 193 N MSE F 194 1555 1555 1.36
LINK C MSE F 194 N PHE F 195 1555 1555 1.35
LINK C VAL F 217 N MSE F 218 1555 1555 1.35
LINK C MSE F 218 N ASN F 219 1555 1555 1.36
LINK C ASP F 241 N OCS F 242 1555 1555 1.33
LINK C OCS F 242 N SER F 243 1555 1555 1.35
LINK C GLN F 305 N MSE F 306 1555 1555 1.34
LINK C MSE F 306 N TYR F 307 1555 1555 1.33
CISPEP 1 ALA A 309 GLY A 310 0 6.13
CISPEP 2 ASP A 311 PRO A 312 0 2.35
CISPEP 3 ALA B 309 GLY B 310 0 7.16
CISPEP 4 ASP B 311 PRO B 312 0 2.14
CISPEP 5 ALA C 309 GLY C 310 0 9.39
CISPEP 6 ASP C 311 PRO C 312 0 -1.60
CISPEP 7 ALA D 309 GLY D 310 0 7.32
CISPEP 8 ASP D 311 PRO D 312 0 5.70
CISPEP 9 ALA E 309 GLY E 310 0 4.29
CISPEP 10 ASP E 311 PRO E 312 0 5.19
CISPEP 11 ALA F 309 GLY F 310 0 5.67
CISPEP 12 ASP F 311 PRO F 312 0 2.36
SITE 1 AC1 2 LYS A 172 LYS C 172
SITE 1 AC2 2 ARG A 165 ARG E 63
SITE 1 AC3 1 GLY A 310
SITE 1 AC4 6 SER A 286 ASN A 289 HIS A 326 VAL B 80
SITE 2 AC4 6 ASN B 139 ASN B 193
SITE 1 AC5 6 GLU A 81 GLN A 91 ASN A 139 TYR B 288
SITE 2 AC5 6 ASN B 289 GOL B 402
SITE 1 AC6 1 GLY B 310
SITE 1 AC7 8 VAL A 80 ASN A 139 ASN A 193 GOL A 406
SITE 2 AC7 8 SER B 286 ASN B 289 HIS B 326 HOH B 519
SITE 1 AC8 1 GLY C 310
SITE 1 AC9 2 GLY D 310 HOH D 537
SITE 1 BC1 7 SER D 286 ASN D 289 HIS D 326 HOH D 527
SITE 2 BC1 7 HOH D 529 VAL E 80 ASN E 193
SITE 1 BC2 2 GLY E 310 HOH E 519
SITE 1 BC3 2 GLY F 310 HOH F 535
CRYST1 65.522 101.211 101.436 109.71 108.86 101.36 P 1 6
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 0.015262 0.003066 0.007251 0.00000
SCALE2 0.000000 0.010078 0.004829 0.00000
SCALE3 0.000000 0.000000 0.011552 0.00000
(ATOM LINES ARE NOT SHOWN.)
END