| content |
HEADER HYDROLASE 16-OCT-18 6IKG
TITLE CRYSTAL STRUCTURE OF SUBSTRATE-BOUND S9 PEPTIDASE (S514A MUTANT) FROM
TITLE 2 DEINOCOCCUS RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 2-655;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MET-ALA-ALA;
COMPND 9 CHAIN: E, F;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS R1;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 GENE: DR_0165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 11 ORGANISM_TAXID: 1299
KEYWDS SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.YADAV,A.KUMAR,V.D.GOYAL,R.D.MAKDE
REVDAT 1 14-NOV-18 6IKG 0
JRNL AUTH P.YADAV,V.D.GOYAL,N.K.GAUR,A.KUMAR,S.M.GOKHALE,S.N.JAMDAR,
JRNL AUTH 2 R.D.MAKDE
JRNL TITL CRYSTAL STRUCTURE OF SUBSTRATE-BOUND S9 PEPTIDASE (S514A
JRNL TITL 2 MUTANT) FROM DEINOCOCCUS RADIODURANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 119478
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5981
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 46.9874 - 7.1386 0.98 3750 218 0.1744 0.2111
REMARK 3 2 7.1386 - 5.6692 1.00 3829 206 0.1948 0.2145
REMARK 3 3 5.6692 - 4.9535 1.00 3799 196 0.1730 0.2159
REMARK 3 4 4.9535 - 4.5010 1.00 3754 242 0.1623 0.1896
REMARK 3 5 4.5010 - 4.1786 1.00 3793 186 0.1584 0.1599
REMARK 3 6 4.1786 - 3.9323 1.00 3814 216 0.1731 0.2016
REMARK 3 7 3.9323 - 3.7355 1.00 3777 207 0.1859 0.2261
REMARK 3 8 3.7355 - 3.5729 1.00 3763 183 0.1940 0.2010
REMARK 3 9 3.5729 - 3.4354 1.00 3815 192 0.2056 0.2171
REMARK 3 10 3.4354 - 3.3169 1.00 3794 210 0.2028 0.2324
REMARK 3 11 3.3169 - 3.2132 1.00 3761 219 0.2095 0.2248
REMARK 3 12 3.2132 - 3.1214 1.00 3748 209 0.2160 0.2362
REMARK 3 13 3.1214 - 3.0392 1.00 3792 208 0.2155 0.2544
REMARK 3 14 3.0392 - 2.9651 1.00 3771 187 0.2204 0.2455
REMARK 3 15 2.9651 - 2.8977 1.00 3823 187 0.2295 0.2690
REMARK 3 16 2.8977 - 2.8360 1.00 3778 208 0.2342 0.2679
REMARK 3 17 2.8360 - 2.7793 1.00 3785 173 0.2325 0.2634
REMARK 3 18 2.7793 - 2.7269 1.00 3824 194 0.2335 0.2466
REMARK 3 19 2.7269 - 2.6782 1.00 3741 217 0.2351 0.2784
REMARK 3 20 2.6782 - 2.6328 1.00 3778 168 0.2505 0.2530
REMARK 3 21 2.6328 - 2.5903 1.00 3829 211 0.2571 0.3217
REMARK 3 22 2.5903 - 2.5505 1.00 3732 198 0.2492 0.2945
REMARK 3 23 2.5505 - 2.5130 1.00 3841 180 0.2563 0.2949
REMARK 3 24 2.5130 - 2.4776 1.00 3754 171 0.2536 0.3021
REMARK 3 25 2.4776 - 2.4441 1.00 3845 189 0.2475 0.2800
REMARK 3 26 2.4441 - 2.4124 1.00 3763 189 0.2613 0.2822
REMARK 3 27 2.4124 - 2.3822 1.00 3755 186 0.2662 0.3014
REMARK 3 28 2.3822 - 2.3535 1.00 3793 214 0.2813 0.3277
REMARK 3 29 2.3535 - 2.3261 1.00 3799 207 0.2847 0.3226
REMARK 3 30 2.3261 - 2.3000 1.00 3697 210 0.2971 0.3080
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.00
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 : 0.003 20412
REMARK 3 ANGLE : 0.645 27889
REMARK 3 CHIRALITY : 0.047 2920
REMARK 3 PLANARITY : 0.004 3723
REMARK 3 DIHEDRAL : 3.939 11764
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9239 44.2586 120.1630
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1278
REMARK 3 T33: 0.1117 T12: -0.0089
REMARK 3 T13: 0.0154 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.0292 L22: 0.2263
REMARK 3 L33: 0.0159 L12: 0.0118
REMARK 3 L13: 0.0084 L23: 0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0029 S13: 0.0206
REMARK 3 S21: 0.0051 S22: -0.0104 S23: 0.0629
REMARK 3 S31: -0.0236 S32: 0.0137 S33: -0.0002
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SF FILE CONTAINS FRIEDEL PAIRS UNDER
REMARK 3 I/F_MINUS AND I/F_PLUS COLUMNS.
REMARK 4
REMARK 4 6IKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1300009365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : RRCAT INDUS-2
REMARK 200 BEAMLINE : PX-BL21
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119554
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 46.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.96900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5YZO
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN I/F_PLUS/MINUS
REMARK 200 COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40MM POTASSIUM PHOSPHATE 30 PEG8000,
REMARK 280 20% GLYCEROL, PH 5.4, MICROBATCH, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 107.31800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 THR A 6
REMARK 465 ALA A 98
REMARK 465 GLY A 99
REMARK 465 GLU A 100
REMARK 465 VAL A 101
REMARK 465 LYS A 102
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 PRO B 7
REMARK 465 GLY B 99
REMARK 465 GLU B 100
REMARK 465 THR B 235
REMARK 465 ALA B 236
REMARK 465 ASP B 237
REMARK 465 ALA B 238
REMARK 465 PRO B 239
REMARK 465 ALA B 240
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ASN C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 THR C 6
REMARK 465 ASP C 43
REMARK 465 PRO C 44
REMARK 465 ALA C 45
REMARK 465 LYS C 46
REMARK 465 GLY C 99
REMARK 465 GLU C 100
REMARK 465 ALA C 236
REMARK 465 ASP C 237
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 ASN D 2
REMARK 465 ASN D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 THR D 6
REMARK 465 PRO D 7
REMARK 465 GLY D 99
REMARK 465 GLU D 100
REMARK 465 THR D 235
REMARK 465 ALA D 236
REMARK 465 ASP D 237
REMARK 465 GLY D 343
REMARK 465 GLY D 344
REMARK 465 GLY D 345
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 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 GLU A 146 CG CD OE1 OE2
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 ARG A 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 ARG A 189 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 195 CG CD OE1 OE2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 ASP A 237 CG OD1 OD2
REMARK 470 GLN A 243 CG CD OE1 NE2
REMARK 470 HIS A 253 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 273 CG CD CE NZ
REMARK 470 GLU A 407 CG CD OE1 OE2
REMARK 470 GLN A 424 CG CD OE1 NE2
REMARK 470 ARG A 566 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 ASP B 50 CG OD1 OD2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 ARG B 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 146 CG CD OE1 OE2
REMARK 470 GLU B 173 CG CD OE1 OE2
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 GLU B 195 CG CD OE1 OE2
REMARK 470 GLU B 216 CG CD OE1 OE2
REMARK 470 GLN B 243 CG CD OE1 NE2
REMARK 470 HIS B 253 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 290 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 332 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 385 CG CD OE1 NE2
REMARK 470 GLU B 407 CG CD OE1 OE2
REMARK 470 GLU B 421 CG CD OE1 OE2
REMARK 470 LYS B 425 CG CD CE NZ
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 LYS C 49 CG CD CE NZ
REMARK 470 ASP C 50 CG OD1 OD2
REMARK 470 ARG C 53 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 57 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 102 CG CD CE NZ
REMARK 470 LYS C 111 CG CD CE NZ
REMARK 470 LYS C 122 CE NZ
REMARK 470 ARG C 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 146 CG CD OE1 OE2
REMARK 470 GLU C 173 CG CD OE1 OE2
REMARK 470 ARG C 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 184 CG CD OE1 OE2
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 GLU C 216 CG CD OE1 OE2
REMARK 470 ASP C 247 CG OD1 OD2
REMARK 470 GLN C 262 CG CD OE1 NE2
REMARK 470 LYS C 273 CG CD CE NZ
REMARK 470 LYS C 347 CG CD CE NZ
REMARK 470 ARG C 376 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 566 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 LYS D 46 CG CD CE NZ
REMARK 470 LYS D 49 CG CD CE NZ
REMARK 470 ASP D 50 CG OD1 OD2
REMARK 470 ARG D 69 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 102 CG CD CE NZ
REMARK 470 LYS D 122 CG CD CE NZ
REMARK 470 GLU D 146 CG CD OE1 OE2
REMARK 470 GLU D 173 CG CD OE1 OE2
REMARK 470 ARG D 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 184 CG CD OE1 OE2
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 GLU D 195 CG CD OE1 OE2
REMARK 470 GLU D 216 CG CD OE1 OE2
REMARK 470 GLN D 220 CG CD OE1 NE2
REMARK 470 GLN D 243 CG CD OE1 NE2
REMARK 470 LYS D 244 CG CD CE NZ
REMARK 470 LEU D 245 CG CD1 CD2
REMARK 470 HIS D 253 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 262 CG CD OE1 NE2
REMARK 470 ARG D 269 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 273 CG CD CE NZ
REMARK 470 GLU D 285 CG CD OE1 OE2
REMARK 470 ASN D 286 CG OD1 ND2
REMARK 470 GLN D 288 CG CD OE1 NE2
REMARK 470 ARG D 290 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 323 CG OD1 OD2
REMARK 470 ILE D 342 CG1 CG2 CD1
REMARK 470 VAL D 346 CG1 CG2
REMARK 470 LYS D 347 CG CD CE NZ
REMARK 470 GLN D 354 CG CD OE1 NE2
REMARK 470 GLU D 364 CG CD OE1 OE2
REMARK 470 ARG D 376 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 399 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 421 CG CD OE1 OE2
REMARK 470 GLU D 423 CG CD OE1 OE2
REMARK 470 GLU D 498 CG CD OE1 OE2
REMARK 470 LYS D 507 CG CD CE NZ
REMARK 470 ARG D 566 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 586 CG CD CE NZ
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 GLN C 220 CA - CB - CG ANGL. DEV. = -14.2 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 143 -121.82 61.94
REMARK 500 ASP A 169 -124.47 59.06
REMARK 500 THR A 235 -76.58 -124.86
REMARK 500 ALA A 238 98.80 160.91
REMARK 500 SER A 250 -169.02 -163.12
REMARK 500 ASP A 293 57.98 -92.80
REMARK 500 ASP A 321 -168.45 -160.21
REMARK 500 ASP A 350 85.00 -160.30
REMARK 500 ARG A 480 44.65 -148.63
REMARK 500 THR A 483 -98.09 -110.72
REMARK 500 ALA A 514 -112.21 65.31
REMARK 500 ARG A 537 54.70 37.88
REMARK 500 ARG A 554 -18.27 -141.94
REMARK 500 GLU A 626 -32.54 67.27
REMARK 500 ASN A 628 -161.94 -128.91
REMARK 500 SER A 634 18.81 -155.32
REMARK 500 ALA B 103 75.86 39.51
REMARK 500 ALA B 143 -120.58 61.13
REMARK 500 ASP B 169 -124.04 59.56
REMARK 500 SER B 250 -169.84 -162.28
REMARK 500 ASP B 293 56.53 -91.07
REMARK 500 ASP B 321 -169.11 -160.20
REMARK 500 ASP B 350 85.39 -160.43
REMARK 500 ARG B 480 44.54 -148.28
REMARK 500 THR B 483 -98.08 -109.89
REMARK 500 ALA B 514 -112.89 65.78
REMARK 500 ARG B 537 52.90 38.05
REMARK 500 ARG B 554 -17.39 -142.68
REMARK 500 GLU B 626 -32.88 67.92
REMARK 500 ASN B 628 -162.05 -129.15
REMARK 500 SER B 634 18.49 -155.77
REMARK 500 ALA C 103 75.99 37.79
REMARK 500 ALA C 143 -121.64 61.80
REMARK 500 LYS C 148 31.17 -99.68
REMARK 500 ASP C 169 -123.69 59.54
REMARK 500 ASP C 293 54.60 -92.38
REMARK 500 ASP C 350 85.32 -161.48
REMARK 500 ARG C 480 45.31 -148.05
REMARK 500 THR C 483 -97.74 -110.18
REMARK 500 ALA C 514 -112.49 65.29
REMARK 500 ARG C 537 53.18 38.04
REMARK 500 ARG C 554 -17.29 -142.74
REMARK 500 GLU C 626 -32.25 67.75
REMARK 500 ASN C 628 -161.93 -128.25
REMARK 500 SER C 634 18.63 -156.33
REMARK 500 ALA D 143 -122.20 61.82
REMARK 500 ASP D 169 -121.61 58.70
REMARK 500 SER D 250 -169.35 -161.17
REMARK 500 ASP D 293 57.82 -92.11
REMARK 500 ASP D 321 -169.10 -160.38
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 981 DISTANCE = 5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 701
DBREF 6IKG A 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IKG B 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IKG C 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IKG D 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IKG E 1 3 PDB 6IKG 6IKG 1 3
DBREF 6IKG F 1 3 PDB 6IKG 6IKG 1 3
SEQADV 6IKG GLY A 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG SER A 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG ALA A 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 6IKG GLY B 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG SER B 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG ALA B 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 6IKG GLY C 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG SER C 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG ALA C 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 6IKG GLY D 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG SER D 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IKG ALA D 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQRES 1 A 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 A 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 A 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 A 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 A 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 A 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 A 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 A 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 A 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 A 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 A 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 A 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 A 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 A 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 A 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 A 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 A 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 A 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 A 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 A 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 A 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 A 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 A 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 A 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 A 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 A 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 A 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 A 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 A 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 A 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 A 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 A 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 A 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 A 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 A 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 A 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 A 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 A 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 A 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 A 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 A 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 A 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 A 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 A 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 A 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 A 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 A 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 A 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 A 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 A 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 A 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 B 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 B 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 B 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 B 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 B 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 B 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 B 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 B 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 B 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 B 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 B 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 B 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 B 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 B 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 B 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 B 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 B 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 B 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 B 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 B 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 B 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 B 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 B 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 B 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 B 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 B 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 B 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 B 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 B 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 B 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 B 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 B 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 B 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 B 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 B 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 B 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 B 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 B 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 B 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 B 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 B 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 B 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 B 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 B 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 B 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 B 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 B 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 B 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 B 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 B 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 B 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 C 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 C 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 C 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 C 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 C 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 C 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 C 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 C 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 C 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 C 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 C 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 C 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 C 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 C 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 C 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 C 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 C 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 C 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 C 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 C 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 C 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 C 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 C 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 C 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 C 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 C 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 C 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 C 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 C 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 C 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 C 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 C 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 C 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 C 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 C 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 C 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 C 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 C 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 C 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 C 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 C 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 C 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 C 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 C 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 C 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 C 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 C 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 C 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 C 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 C 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 C 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 D 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 D 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 D 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 D 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 D 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 D 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 D 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 D 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 D 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 D 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 D 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 D 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 D 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 D 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 D 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 D 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 D 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 D 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 D 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 D 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 D 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 D 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 D 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 D 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 D 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 D 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 D 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 D 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 D 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 D 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 D 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 D 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 D 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 D 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 D 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 D 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 D 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 D 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 D 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 D 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 D 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 D 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 D 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 D 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 D 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 D 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 D 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 D 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 D 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 D 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 D 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 E 3 MET ALA ALA
SEQRES 1 F 3 MET ALA ALA
HET GOL A 701 6
HET GOL B 701 6
HET GOL B 702 6
HET GOL C 701 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 11 HOH *758(H2 O)
HELIX 1 AA1 GLY A 10 LEU A 17 5 8
HELIX 2 AA2 LYS A 148 GLY A 153 1 6
HELIX 3 AA3 ASP A 217 GLN A 223 1 7
HELIX 4 AA4 LEU A 390 PHE A 394 5 5
HELIX 5 AA5 THR A 445 ARG A 454 1 10
HELIX 6 AA6 GLY A 470 ALA A 476 1 7
HELIX 7 AA7 THR A 483 VAL A 500 1 18
HELIX 8 AA8 ALA A 514 GLY A 525 1 12
HELIX 9 AA9 ASN A 541 SER A 549 1 9
HELIX 10 AB1 ARG A 554 LEU A 560 1 7
HELIX 11 AB2 ARG A 566 LEU A 576 1 11
HELIX 12 AB3 SER A 577 VAL A 585 5 9
HELIX 13 AB4 VAL A 602 HIS A 615 1 14
HELIX 14 AB5 GLU A 630 GLY A 635 1 6
HELIX 15 AB6 ARG A 636 LEU A 655 1 20
HELIX 16 AB7 GLY B 10 LEU B 17 5 8
HELIX 17 AB8 LYS B 148 GLY B 153 1 6
HELIX 18 AB9 ASP B 217 GLN B 223 1 7
HELIX 19 AC1 ASP B 389 PHE B 394 5 6
HELIX 20 AC2 THR B 445 ARG B 454 1 10
HELIX 21 AC3 GLY B 470 ALA B 476 1 7
HELIX 22 AC4 THR B 483 VAL B 500 1 18
HELIX 23 AC5 ALA B 514 GLY B 525 1 12
HELIX 24 AC6 ASN B 541 SER B 549 1 9
HELIX 25 AC7 ARG B 554 LEU B 560 1 7
HELIX 26 AC8 ARG B 566 LEU B 576 1 11
HELIX 27 AC9 SER B 577 VAL B 585 5 9
HELIX 28 AD1 VAL B 602 HIS B 615 1 14
HELIX 29 AD2 GLU B 630 GLY B 635 1 6
HELIX 30 AD3 ARG B 636 LEU B 655 1 20
HELIX 31 AD4 GLY C 10 LEU C 17 5 8
HELIX 32 AD5 LYS C 148 GLY C 153 1 6
HELIX 33 AD6 ASP C 217 GLN C 223 1 7
HELIX 34 AD7 LEU C 390 PHE C 394 5 5
HELIX 35 AD8 THR C 445 ARG C 454 1 10
HELIX 36 AD9 GLY C 470 ALA C 476 1 7
HELIX 37 AE1 THR C 483 VAL C 500 1 18
HELIX 38 AE2 ALA C 514 GLY C 525 1 12
HELIX 39 AE3 ASN C 541 SER C 549 1 9
HELIX 40 AE4 ARG C 554 LEU C 560 1 7
HELIX 41 AE5 ARG C 566 LEU C 576 1 11
HELIX 42 AE6 SER C 577 VAL C 585 5 9
HELIX 43 AE7 VAL C 602 HIS C 615 1 14
HELIX 44 AE8 GLU C 630 GLY C 635 1 6
HELIX 45 AE9 ARG C 636 LEU C 655 1 20
HELIX 46 AF1 GLY D 10 LEU D 17 5 8
HELIX 47 AF2 LYS D 148 GLY D 153 1 6
HELIX 48 AF3 ASP D 217 GLN D 223 1 7
HELIX 49 AF4 LEU D 390 PHE D 394 5 5
HELIX 50 AF5 THR D 445 ARG D 454 1 10
HELIX 51 AF6 GLY D 470 ALA D 476 1 7
HELIX 52 AF7 THR D 483 VAL D 500 1 18
HELIX 53 AF8 ALA D 514 GLY D 525 1 12
HELIX 54 AF9 ASN D 541 SER D 549 1 9
HELIX 55 AG1 ARG D 554 LEU D 560 1 7
HELIX 56 AG2 ARG D 566 LEU D 576 1 11
HELIX 57 AG3 SER D 577 VAL D 585 5 9
HELIX 58 AG4 VAL D 602 HIS D 615 1 14
HELIX 59 AG5 GLU D 630 GLY D 635 1 6
HELIX 60 AG6 ARG D 636 LEU D 655 1 20
SHEET 1 AA1 4 PHE A 19 VAL A 25 0
SHEET 2 AA1 4 VAL A 32 GLU A 41 -1 O ALA A 33 N GLN A 24
SHEET 3 AA1 4 PRO A 54 SER A 63 -1 O ARG A 55 N SER A 40
SHEET 4 AA1 4 ARG A 69 PRO A 70 -1 O ARG A 69 N LEU A 62
SHEET 1 AA2 4 GLY A 79 TRP A 85 0
SHEET 2 AA2 4 ASN A 91 SER A 97 -1 O ALA A 93 N ARG A 84
SHEET 3 AA2 4 ALA A 104 PRO A 109 -1 O MET A 106 N PHE A 94
SHEET 4 AA2 4 ARG A 116 ARG A 117 -1 O ARG A 116 N LEU A 107
SHEET 1 AA3 4 SER A 126 TRP A 130 0
SHEET 2 AA3 4 PHE A 136 THR A 141 -1 O ALA A 138 N GLN A 129
SHEET 3 AA3 4 ALA A 177 ASP A 182 -1 O TRP A 179 N PHE A 139
SHEET 4 AA3 4 LYS A 187 TYR A 192 -1 O LYS A 187 N ASP A 182
SHEET 1 AA4 9 ARG A 156 LEU A 158 0
SHEET 2 AA4 9 VAL B 619 PHE B 624 -1 O PHE B 621 N LEU A 158
SHEET 3 AA4 9 THR B 589 SER B 594 1 N ILE B 591 O ARG B 620
SHEET 4 AA4 9 ALA B 532 ASP B 536 1 N ALA B 533 O LEU B 590
SHEET 5 AA4 9 LEU B 503 GLY B 513 1 N GLY B 512 O ASP B 536
SHEET 6 AA4 9 VAL B 426 ILE B 432 1 N LEU B 430 O ALA B 509
SHEET 7 AA4 9 GLY B 457 SER B 461 1 O GLY B 457 N LEU B 429
SHEET 8 AA4 9 GLY B 411 LEU B 418 -1 N TRP B 416 O TYR B 460
SHEET 9 AA4 9 GLN B 402 THR B 408 -1 N PHE B 406 O GLY B 413
SHEET 1 AA5 2 ARG A 164 ALA A 165 0
SHEET 2 AA5 2 ASP A 169 TRP A 170 -1 O ASP A 169 N ALA A 165
SHEET 1 AA6 4 LEU A 201 TRP A 203 0
SHEET 2 AA6 4 GLY A 209 GLN A 214 -1 O LEU A 211 N SER A 202
SHEET 3 AA6 4 GLN A 226 PRO A 232 -1 O LEU A 231 N VAL A 210
SHEET 4 AA6 4 GLN A 243 SER A 250 -1 O LEU A 245 N VAL A 228
SHEET 1 AA7 4 ALA A 252 PRO A 257 0
SHEET 2 AA7 4 PHE A 264 GLY A 268 -1 O ILE A 267 N HIS A 253
SHEET 3 AA7 4 HIS A 280 GLU A 285 -1 O ILE A 284 N PHE A 264
SHEET 4 AA7 4 GLN A 288 ARG A 291 -1 O ARG A 290 N LEU A 283
SHEET 1 AA8 4 ARG A 318 TRP A 319 0
SHEET 2 AA8 4 THR A 324 VAL A 331 -1 O LEU A 326 N ARG A 318
SHEET 3 AA8 4 SER A 334 HIS A 341 -1 O PHE A 338 N PHE A 327
SHEET 4 AA8 4 LYS A 347 ASP A 350 -1 O LYS A 347 N THR A 339
SHEET 1 AA9 4 GLY A 355 ALA A 362 0
SHEET 2 AA9 4 VAL A 367 SER A 373 -1 O GLU A 372 N VAL A 356
SHEET 3 AA9 4 GLU A 379 LEU A 382 -1 O GLU A 381 N LEU A 369
SHEET 4 AA9 4 GLN A 385 ARG A 386 -1 O GLN A 385 N LEU A 382
SHEET 1 AB1 9 GLN A 402 THR A 408 0
SHEET 2 AB1 9 GLY A 411 LEU A 418 -1 O VAL A 417 N GLN A 402
SHEET 3 AB1 9 GLY A 457 SER A 461 -1 O TYR A 460 N TRP A 416
SHEET 4 AB1 9 VAL A 426 ILE A 432 1 N LEU A 429 O GLY A 457
SHEET 5 AB1 9 LEU A 503 GLY A 513 1 O ALA A 509 N LEU A 430
SHEET 6 AB1 9 ALA A 532 ASP A 536 1 O ASP A 536 N GLY A 512
SHEET 7 AB1 9 THR A 589 SER A 594 1 O LEU A 590 N THR A 535
SHEET 8 AB1 9 VAL A 619 PHE A 624 1 O ARG A 620 N ILE A 591
SHEET 9 AB1 9 ARG B 156 LEU B 158 -1 O LEU B 158 N PHE A 621
SHEET 1 AB2 4 PHE B 19 VAL B 25 0
SHEET 2 AB2 4 VAL B 32 GLU B 41 -1 O ALA B 37 N PHE B 19
SHEET 3 AB2 4 PRO B 54 SER B 63 -1 O ARG B 55 N SER B 40
SHEET 4 AB2 4 ARG B 69 PRO B 70 -1 O ARG B 69 N LEU B 62
SHEET 1 AB3 4 GLY B 79 TRP B 85 0
SHEET 2 AB3 4 ASN B 91 SER B 97 -1 O ALA B 93 N ARG B 84
SHEET 3 AB3 4 ALA B 104 PRO B 109 -1 O MET B 106 N PHE B 94
SHEET 4 AB3 4 ARG B 116 ARG B 117 -1 O ARG B 116 N LEU B 107
SHEET 1 AB4 4 VAL B 125 TRP B 130 0
SHEET 2 AB4 4 PHE B 136 THR B 141 -1 O ALA B 138 N GLN B 129
SHEET 3 AB4 4 ALA B 177 ASP B 182 -1 O TRP B 179 N PHE B 139
SHEET 4 AB4 4 LYS B 187 TYR B 192 -1 O LYS B 187 N ASP B 182
SHEET 1 AB5 2 ARG B 164 ALA B 165 0
SHEET 2 AB5 2 ASP B 169 TRP B 170 -1 O ASP B 169 N ALA B 165
SHEET 1 AB6 4 LEU B 201 TRP B 203 0
SHEET 2 AB6 4 GLY B 209 GLN B 214 -1 O LEU B 211 N SER B 202
SHEET 3 AB6 4 GLN B 226 PRO B 232 -1 O ASP B 227 N GLN B 214
SHEET 4 AB6 4 GLN B 243 SER B 250 -1 O GLN B 243 N ASP B 230
SHEET 1 AB7 4 ALA B 252 PRO B 257 0
SHEET 2 AB7 4 PHE B 264 GLY B 268 -1 O ILE B 267 N HIS B 253
SHEET 3 AB7 4 HIS B 280 GLU B 285 -1 O ILE B 284 N PHE B 264
SHEET 4 AB7 4 GLN B 288 ARG B 291 -1 O ARG B 290 N LEU B 283
SHEET 1 AB8 4 ARG B 318 TRP B 319 0
SHEET 2 AB8 4 THR B 324 VAL B 331 -1 O LEU B 326 N ARG B 318
SHEET 3 AB8 4 SER B 334 HIS B 341 -1 O PHE B 338 N PHE B 327
SHEET 4 AB8 4 VAL B 346 ASP B 350 -1 O LYS B 347 N THR B 339
SHEET 1 AB9 4 GLY B 355 ALA B 362 0
SHEET 2 AB9 4 VAL B 367 SER B 373 -1 O GLU B 372 N VAL B 356
SHEET 3 AB9 4 GLU B 379 LEU B 382 -1 O GLU B 381 N LEU B 369
SHEET 4 AB9 4 GLN B 385 ARG B 386 -1 O GLN B 385 N LEU B 382
SHEET 1 AC1 4 PHE C 19 VAL C 25 0
SHEET 2 AC1 4 VAL C 32 GLU C 41 -1 O ALA C 37 N PHE C 19
SHEET 3 AC1 4 PRO C 54 SER C 63 -1 O ARG C 55 N SER C 40
SHEET 4 AC1 4 ARG C 69 PRO C 70 -1 O ARG C 69 N LEU C 62
SHEET 1 AC2 4 GLY C 79 TRP C 85 0
SHEET 2 AC2 4 ASN C 91 SER C 97 -1 O SER C 97 N GLY C 79
SHEET 3 AC2 4 ALA C 104 PRO C 109 -1 O MET C 106 N PHE C 94
SHEET 4 AC2 4 ARG C 116 ARG C 117 -1 O ARG C 116 N LEU C 107
SHEET 1 AC3 4 VAL C 125 TRP C 130 0
SHEET 2 AC3 4 PHE C 136 THR C 141 -1 O ALA C 138 N GLN C 129
SHEET 3 AC3 4 ALA C 177 ASP C 182 -1 O TRP C 179 N PHE C 139
SHEET 4 AC3 4 LYS C 187 TYR C 192 -1 O LYS C 187 N ASP C 182
SHEET 1 AC4 9 ARG C 156 LEU C 158 0
SHEET 2 AC4 9 VAL D 619 PHE D 624 -1 O PHE D 621 N LEU C 158
SHEET 3 AC4 9 THR D 589 SER D 594 1 N ILE D 591 O ARG D 620
SHEET 4 AC4 9 ALA D 532 ASP D 536 1 N THR D 535 O LEU D 590
SHEET 5 AC4 9 LEU D 503 GLY D 513 1 N GLY D 512 O ASP D 536
SHEET 6 AC4 9 VAL D 426 ILE D 432 1 N LEU D 430 O ALA D 509
SHEET 7 AC4 9 GLY D 457 SER D 461 1 O GLY D 457 N LEU D 429
SHEET 8 AC4 9 GLY D 411 LEU D 418 -1 N TRP D 416 O TYR D 460
SHEET 9 AC4 9 GLN D 402 THR D 408 -1 N PHE D 406 O GLY D 413
SHEET 1 AC5 2 ARG C 164 ALA C 165 0
SHEET 2 AC5 2 ASP C 169 TRP C 170 -1 O ASP C 169 N ALA C 165
SHEET 1 AC6 4 LEU C 201 TRP C 203 0
SHEET 2 AC6 4 GLY C 209 GLN C 214 -1 O LEU C 211 N SER C 202
SHEET 3 AC6 4 GLN C 226 PRO C 232 -1 O LEU C 231 N VAL C 210
SHEET 4 AC6 4 GLN C 243 SER C 250 -1 O GLN C 243 N ASP C 230
SHEET 1 AC7 4 ALA C 252 PRO C 257 0
SHEET 2 AC7 4 PHE C 264 GLY C 268 -1 O ALA C 265 N ALA C 256
SHEET 3 AC7 4 HIS C 280 GLU C 285 -1 O HIS C 280 N GLY C 268
SHEET 4 AC7 4 GLN C 288 ARG C 291 -1 O ARG C 290 N LEU C 283
SHEET 1 AC8 4 ARG C 318 TRP C 319 0
SHEET 2 AC8 4 THR C 324 VAL C 331 -1 O LEU C 326 N ARG C 318
SHEET 3 AC8 4 SER C 334 HIS C 341 -1 O PHE C 338 N PHE C 327
SHEET 4 AC8 4 LYS C 347 ASP C 350 -1 O LYS C 347 N THR C 339
SHEET 1 AC9 4 GLY C 355 ALA C 362 0
SHEET 2 AC9 4 VAL C 367 SER C 373 -1 O GLU C 372 N VAL C 356
SHEET 3 AC9 4 GLU C 379 LEU C 382 -1 O GLU C 381 N LEU C 369
SHEET 4 AC9 4 GLN C 385 ARG C 386 -1 O GLN C 385 N LEU C 382
SHEET 1 AD1 9 GLN C 402 THR C 408 0
SHEET 2 AD1 9 GLY C 411 LEU C 418 -1 O GLY C 413 N PHE C 406
SHEET 3 AD1 9 GLY C 457 SER C 461 -1 O TYR C 460 N TRP C 416
SHEET 4 AD1 9 VAL C 426 ILE C 432 1 N PRO C 427 O GLY C 457
SHEET 5 AD1 9 LEU C 503 GLY C 513 1 O ALA C 509 N LEU C 430
SHEET 6 AD1 9 ALA C 532 ASP C 536 1 O ASP C 536 N GLY C 512
SHEET 7 AD1 9 THR C 589 SER C 594 1 O LEU C 590 N ALA C 533
SHEET 8 AD1 9 VAL C 619 PHE C 624 1 O ARG C 620 N ILE C 591
SHEET 9 AD1 9 ARG D 156 LEU D 158 -1 O LEU D 158 N PHE C 621
SHEET 1 AD2 4 PHE D 19 VAL D 25 0
SHEET 2 AD2 4 VAL D 32 GLU D 41 -1 O ALA D 37 N PHE D 19
SHEET 3 AD2 4 PRO D 54 SER D 63 -1 O ARG D 55 N SER D 40
SHEET 4 AD2 4 ARG D 69 PRO D 70 -1 O ARG D 69 N LEU D 62
SHEET 1 AD3 4 GLY D 79 TRP D 85 0
SHEET 2 AD3 4 ASN D 91 SER D 97 -1 O VAL D 95 N SER D 81
SHEET 3 AD3 4 ALA D 104 PRO D 109 -1 O LEU D 108 N LEU D 92
SHEET 4 AD3 4 ARG D 116 ARG D 117 -1 O ARG D 116 N LEU D 107
SHEET 1 AD4 4 SER D 126 TRP D 130 0
SHEET 2 AD4 4 PHE D 136 THR D 141 -1 O ALA D 138 N GLN D 129
SHEET 3 AD4 4 ALA D 177 ASP D 182 -1 O TRP D 179 N PHE D 139
SHEET 4 AD4 4 LYS D 187 TYR D 192 -1 O TYR D 192 N LEU D 178
SHEET 1 AD5 2 ARG D 164 ALA D 165 0
SHEET 2 AD5 2 ASP D 169 TRP D 170 -1 O ASP D 169 N ALA D 165
SHEET 1 AD6 4 LEU D 201 TRP D 203 0
SHEET 2 AD6 4 GLY D 209 GLN D 214 -1 O LEU D 211 N SER D 202
SHEET 3 AD6 4 GLN D 226 PRO D 232 -1 O TYR D 229 N ILE D 212
SHEET 4 AD6 4 GLN D 243 SER D 250 -1 O GLN D 243 N ASP D 230
SHEET 1 AD7 4 ALA D 252 PRO D 257 0
SHEET 2 AD7 4 PHE D 264 GLY D 268 -1 O ILE D 267 N HIS D 253
SHEET 3 AD7 4 HIS D 280 GLU D 285 -1 O ILE D 284 N PHE D 264
SHEET 4 AD7 4 GLN D 288 ARG D 291 -1 O GLN D 288 N GLU D 285
SHEET 1 AD8 4 ARG D 318 TRP D 319 0
SHEET 2 AD8 4 THR D 324 VAL D 331 -1 O LEU D 326 N ARG D 318
SHEET 3 AD8 4 SER D 334 HIS D 341 -1 O PHE D 338 N PHE D 327
SHEET 4 AD8 4 LYS D 347 ASP D 350 -1 O LYS D 347 N THR D 339
SHEET 1 AD9 4 GLY D 355 ALA D 362 0
SHEET 2 AD9 4 VAL D 367 SER D 373 -1 O GLU D 372 N VAL D 356
SHEET 3 AD9 4 GLU D 379 LEU D 382 -1 O GLU D 381 N LEU D 369
SHEET 4 AD9 4 GLN D 385 ARG D 386 -1 O GLN D 385 N LEU D 382
CISPEP 1 GLY A 435 PRO A 436 0 5.65
CISPEP 2 GLY B 435 PRO B 436 0 5.60
CISPEP 3 GLY C 435 PRO C 436 0 5.56
CISPEP 4 GLY D 435 PRO D 436 0 5.94
SITE 1 AC1 7 TYR A 349 ASP A 350 VAL A 367 LEU A 369
SITE 2 AC1 7 GLU A 381 ASN A 383 GLY A 384
SITE 1 AC2 8 TYR B 349 ASP B 350 VAL B 367 LEU B 369
SITE 2 AC2 8 GLU B 381 ASN B 383 GLY B 384 HOH B 851
SITE 1 AC3 5 ALA B 374 GLY B 443 THR B 445 GLN B 449
SITE 2 AC3 5 TYR B 460
SITE 1 AC4 6 TYR C 349 ASP C 350 LEU C 369 GLU C 381
SITE 2 AC4 6 ASN C 383 GLY C 384
CRYST1 71.649 214.636 92.022 90.00 102.98 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013957 0.000000 0.003217 0.00000
SCALE2 0.000000 0.004659 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011152 0.00000
TER 4983 LEU A 655
TER 9929 LEU B 655
TER 14877 LEU C 655
TER 19756 LEU D 655
TER 19776 ALA E 3
TER 19796 ALA F 3
MASTER 523 0 4 60 156 0 8 620572 6 24 206
END |