HEADER MEMBRANE PROTEIN 31-JUL-15 5CYY
TITLE STRUCTURE OF THE C-TERMINAL DOMAINS OF DIPZ FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DIPZ;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 361-695;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 GENE: DIPZ, RV2874, MTCY274.05;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOREDOXIN, CARBOHYDRATE BINDING MODULE, REDOX, STRUCTURAL GENOMICS,
KEYWDS 2 PSI-BIOLOGY, MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS
KEYWDS 3 PROJECT, XMTB, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.GOLDSTONE,P.METCALF,E.N.BAKER,MYCOBACTERIUM TUBERCULOSIS
AUTHOR 2 STRUCTURAL PROTEOMICS PROJECT (XMTB)
REVDAT 2 18-APR-18 5CYY 1 JRNL REMARK
REVDAT 1 13-JAN-16 5CYY 0
JRNL AUTH D.C.GOLDSTONE,P.METCALF,E.N.BAKER
JRNL TITL STRUCTURE OF THE ECTODOMAIN OF THE ELECTRON TRANSPORTER
JRNL TITL 2 RV2874 FROM MYCOBACTERIUM TUBERCULOSIS REVEALS A
JRNL TITL 3 THIOREDOXIN-LIKE DOMAIN COMBINED WITH A CARBOHYDRATE-BINDING
JRNL TITL 4 MODULE.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 72 40 2016
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 26894533
JRNL DOI 10.1107/S2059798315021488
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 73019
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.990
REMARK 3 FREE R VALUE TEST SET COUNT : 7296
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 42.4011 - 6.8267 0.83 2170 249 0.1522 0.1750
REMARK 3 2 6.8267 - 5.4221 0.86 2170 239 0.1441 0.1891
REMARK 3 3 5.4221 - 4.7378 0.87 2151 246 0.1314 0.1893
REMARK 3 4 4.7378 - 4.3051 0.87 2165 231 0.1202 0.1740
REMARK 3 5 4.3051 - 3.9967 0.88 2165 241 0.1396 0.1791
REMARK 3 6 3.9967 - 3.7613 0.88 2157 244 0.1570 0.1982
REMARK 3 7 3.7613 - 3.5730 0.89 2177 236 0.1692 0.2277
REMARK 3 8 3.5730 - 3.4175 0.89 2193 228 0.1829 0.2623
REMARK 3 9 3.4175 - 3.2860 0.90 2199 246 0.1872 0.2215
REMARK 3 10 3.2860 - 3.1727 0.90 2196 244 0.1802 0.2472
REMARK 3 11 3.1727 - 3.0735 0.90 2172 255 0.1954 0.2289
REMARK 3 12 3.0735 - 2.9857 0.91 2194 228 0.1996 0.2475
REMARK 3 13 2.9857 - 2.9071 0.91 2204 265 0.1975 0.2586
REMARK 3 14 2.9071 - 2.8362 0.91 2193 239 0.2055 0.2622
REMARK 3 15 2.8362 - 2.7717 0.92 2222 249 0.1977 0.2848
REMARK 3 16 2.7717 - 2.7127 0.92 2207 263 0.2043 0.2814
REMARK 3 17 2.7127 - 2.6585 0.92 2203 244 0.2127 0.2931
REMARK 3 18 2.6585 - 2.6083 0.92 2229 223 0.2057 0.2868
REMARK 3 19 2.6083 - 2.5617 0.92 2230 253 0.2091 0.2711
REMARK 3 20 2.5617 - 2.5183 0.92 2212 260 0.2034 0.2689
REMARK 3 21 2.5183 - 2.4777 0.92 2228 245 0.2100 0.3117
REMARK 3 22 2.4777 - 2.4396 0.92 2205 252 0.2086 0.2571
REMARK 3 23 2.4396 - 2.4037 0.92 2242 221 0.2138 0.2904
REMARK 3 24 2.4037 - 2.3699 0.92 2207 268 0.2266 0.2899
REMARK 3 25 2.3699 - 2.3378 0.92 2214 236 0.2309 0.3149
REMARK 3 26 2.3378 - 2.3075 0.92 2201 253 0.2435 0.3302
REMARK 3 27 2.3075 - 2.2786 0.91 2182 260 0.2481 0.2931
REMARK 3 28 2.2786 - 2.2512 0.90 2165 240 0.2843 0.3350
REMARK 3 29 2.2512 - 2.2250 0.88 2095 218 0.3864 0.4504
REMARK 3 30 2.2250 - 2.2000 0.89 2175 220 0.3331 0.3967
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.38
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 : 0.008 10246
REMARK 3 ANGLE : 1.088 14018
REMARK 3 CHIRALITY : 0.041 1567
REMARK 3 PLANARITY : 0.005 1836
REMARK 3 DIHEDRAL : 11.694 3601
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73550
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.62800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.570
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 0.1M NA-CITRATE PH 5.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 54.98600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.21900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.76250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.21900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.98600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.76250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 336
REMARK 465 SER A 337
REMARK 465 TYR A 338
REMARK 465 TYR A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 ASP A 346
REMARK 465 TYR A 347
REMARK 465 ASP A 348
REMARK 465 ILE A 349
REMARK 465 PRO A 350
REMARK 465 THR A 351
REMARK 465 THR A 352
REMARK 465 GLU A 353
REMARK 465 ASN A 354
REMARK 465 LEU A 355
REMARK 465 TYR A 356
REMARK 465 PHE A 357
REMARK 465 GLN A 358
REMARK 465 GLY A 359
REMARK 465 ALA A 360
REMARK 465 ILE A 361
REMARK 465 SER A 362
REMARK 465 MET B 336
REMARK 465 SER B 337
REMARK 465 TYR B 338
REMARK 465 TYR B 339
REMARK 465 HIS B 340
REMARK 465 HIS B 341
REMARK 465 HIS B 342
REMARK 465 HIS B 343
REMARK 465 HIS B 344
REMARK 465 HIS B 345
REMARK 465 ASP B 346
REMARK 465 TYR B 347
REMARK 465 ASP B 348
REMARK 465 ILE B 349
REMARK 465 PRO B 350
REMARK 465 THR B 351
REMARK 465 THR B 352
REMARK 465 GLU B 353
REMARK 465 ASN B 354
REMARK 465 LEU B 355
REMARK 465 TYR B 356
REMARK 465 PHE B 357
REMARK 465 GLN B 358
REMARK 465 GLY B 359
REMARK 465 ALA B 360
REMARK 465 ILE B 361
REMARK 465 SER B 362
REMARK 465 ARG B 650
REMARK 465 ASP B 651
REMARK 465 GLY B 652
REMARK 465 LYS B 653
REMARK 465 PRO B 654
REMARK 465 MET C 336
REMARK 465 SER C 337
REMARK 465 TYR C 338
REMARK 465 TYR C 339
REMARK 465 HIS C 340
REMARK 465 HIS C 341
REMARK 465 HIS C 342
REMARK 465 HIS C 343
REMARK 465 HIS C 344
REMARK 465 HIS C 345
REMARK 465 ASP C 346
REMARK 465 TYR C 347
REMARK 465 ASP C 348
REMARK 465 ILE C 349
REMARK 465 PRO C 350
REMARK 465 THR C 351
REMARK 465 THR C 352
REMARK 465 GLU C 353
REMARK 465 ASN C 354
REMARK 465 LEU C 355
REMARK 465 TYR C 356
REMARK 465 PHE C 357
REMARK 465 GLN C 358
REMARK 465 GLY C 359
REMARK 465 ALA C 360
REMARK 465 ILE C 361
REMARK 465 SER C 362
REMARK 465 MET D 336
REMARK 465 SER D 337
REMARK 465 TYR D 338
REMARK 465 TYR D 339
REMARK 465 HIS D 340
REMARK 465 HIS D 341
REMARK 465 HIS D 342
REMARK 465 HIS D 343
REMARK 465 HIS D 344
REMARK 465 HIS D 345
REMARK 465 ASP D 346
REMARK 465 TYR D 347
REMARK 465 ASP D 348
REMARK 465 ILE D 349
REMARK 465 PRO D 350
REMARK 465 THR D 351
REMARK 465 THR D 352
REMARK 465 GLU D 353
REMARK 465 ASN D 354
REMARK 465 LEU D 355
REMARK 465 TYR D 356
REMARK 465 PHE D 357
REMARK 465 GLN D 358
REMARK 465 GLY D 359
REMARK 465 ALA D 360
REMARK 465 ILE D 361
REMARK 465 ARG D 650
REMARK 465 ASP D 651
REMARK 465 GLY D 652
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 ARG A 564 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 628 CE NZ
REMARK 470 LYS A 653 CE NZ
REMARK 470 ARG A 673 NE CZ NH1 NH2
REMARK 470 GLN B 393 CD OE1 NE2
REMARK 470 LYS B 416 CE NZ
REMARK 470 LYS B 480 CD CE NZ
REMARK 470 ARG B 564 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 672 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 682 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 685 CG CD CE NZ
REMARK 470 ARG C 564 CD NE CZ NH1 NH2
REMARK 470 TYR C 672 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN D 452 CD OE1 NE2
REMARK 470 ASP D 624 CG OD1 OD2
REMARK 470 LYS D 653 CG CD CE NZ
REMARK 470 TYR D 672 CD1 CD2 CE1 CE2 CZ OH
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP C 543 O HOH C 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 494 54.50 -102.37
REMARK 500 TYR A 497 18.69 56.54
REMARK 500 ASN A 580 36.91 -140.41
REMARK 500 THR A 664 -165.96 -162.64
REMARK 500 ASN B 372 66.41 -100.42
REMARK 500 CYS B 397 51.93 -141.27
REMARK 500 ASP B 494 55.08 -106.03
REMARK 500 TYR B 497 18.88 57.00
REMARK 500 ARG B 506 -18.92 -140.50
REMARK 500 LYS B 545 78.50 -153.64
REMARK 500 ALA B 565 45.78 -75.62
REMARK 500 ALA B 566 47.33 -141.52
REMARK 500 ASP B 621 -88.42 -96.76
REMARK 500 ALA B 633 -179.28 -171.97
REMARK 500 CYS C 397 61.41 -154.25
REMARK 500 ASP C 494 57.25 -103.44
REMARK 500 ALA C 565 44.63 -75.00
REMARK 500 ALA C 566 34.17 -140.26
REMARK 500 ASP C 614 -156.61 -145.86
REMARK 500 CYS D 397 57.40 -140.70
REMARK 500 ASP D 494 50.51 -108.34
REMARK 500 LYS D 545 83.60 -152.80
REMARK 500 PRO D 553 132.81 -36.13
REMARK 500 THR D 556 30.69 -93.76
REMARK 500 THR D 557 1.48 -159.93
REMARK 500 ASN D 580 35.44 -140.04
REMARK 500 PRO D 663 127.20 -39.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HYX RELATED DB: PDB
REMARK 900 2HYX IS A SHORTER CONSTRUCT
DBREF 5CYY A 361 695 UNP P9WG63 DIPZ_MYCTU 361 695
DBREF 5CYY B 361 695 UNP P9WG63 DIPZ_MYCTU 361 695
DBREF 5CYY C 361 695 UNP P9WG63 DIPZ_MYCTU 361 695
DBREF 5CYY D 361 695 UNP P9WG63 DIPZ_MYCTU 361 695
SEQADV 5CYY MET A 336 UNP P9WG63 INITIATING METHIONINE
SEQADV 5CYY SER A 337 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR A 338 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR A 339 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 340 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 341 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 342 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 343 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 344 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS A 345 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP A 346 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR A 347 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP A 348 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ILE A 349 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PRO A 350 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR A 351 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR A 352 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLU A 353 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASN A 354 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY LEU A 355 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR A 356 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PHE A 357 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLN A 358 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLY A 359 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ALA A 360 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY MET B 336 UNP P9WG63 INITIATING METHIONINE
SEQADV 5CYY SER B 337 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR B 338 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR B 339 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 340 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 341 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 342 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 343 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 344 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS B 345 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP B 346 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR B 347 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP B 348 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ILE B 349 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PRO B 350 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR B 351 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR B 352 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLU B 353 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASN B 354 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY LEU B 355 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR B 356 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PHE B 357 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLN B 358 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLY B 359 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ALA B 360 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY MET C 336 UNP P9WG63 INITIATING METHIONINE
SEQADV 5CYY SER C 337 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR C 338 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR C 339 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 340 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 341 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 342 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 343 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 344 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS C 345 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP C 346 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR C 347 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP C 348 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ILE C 349 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PRO C 350 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR C 351 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR C 352 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLU C 353 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASN C 354 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY LEU C 355 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR C 356 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PHE C 357 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLN C 358 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLY C 359 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ALA C 360 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY MET D 336 UNP P9WG63 INITIATING METHIONINE
SEQADV 5CYY SER D 337 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR D 338 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR D 339 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 340 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 341 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 342 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 343 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 344 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY HIS D 345 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP D 346 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR D 347 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASP D 348 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ILE D 349 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PRO D 350 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR D 351 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY THR D 352 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLU D 353 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ASN D 354 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY LEU D 355 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY TYR D 356 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY PHE D 357 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLN D 358 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY GLY D 359 UNP P9WG63 EXPRESSION TAG
SEQADV 5CYY ALA D 360 UNP P9WG63 EXPRESSION TAG
SEQRES 1 A 360 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 360 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE
SEQRES 3 A 360 SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY
SEQRES 4 A 360 GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS
SEQRES 5 A 360 SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA
SEQRES 6 A 360 PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO
SEQRES 7 A 360 GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS
SEQRES 8 A 360 VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN
SEQRES 9 A 360 CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN
SEQRES 10 A 360 ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS
SEQRES 11 A 360 THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL
SEQRES 12 A 360 ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE
SEQRES 13 A 360 ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG
SEQRES 14 A 360 ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR
SEQRES 15 A 360 GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR
SEQRES 16 A 360 ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP
SEQRES 17 A 360 ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR
SEQRES 18 A 360 THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO
SEQRES 19 A 360 GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY
SEQRES 20 A 360 GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP
SEQRES 21 A 360 TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG
SEQRES 22 A 360 GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP
SEQRES 23 A 360 GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS
SEQRES 24 A 360 ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR
SEQRES 25 A 360 VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER
SEQRES 26 A 360 GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG
SEQRES 27 A 360 LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY
SEQRES 28 A 360 LEU GLN VAL PHE SER PHE THR TYR GLY
SEQRES 1 B 360 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 360 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE
SEQRES 3 B 360 SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY
SEQRES 4 B 360 GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS
SEQRES 5 B 360 SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA
SEQRES 6 B 360 PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO
SEQRES 7 B 360 GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS
SEQRES 8 B 360 VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN
SEQRES 9 B 360 CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN
SEQRES 10 B 360 ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS
SEQRES 11 B 360 THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL
SEQRES 12 B 360 ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE
SEQRES 13 B 360 ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG
SEQRES 14 B 360 ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR
SEQRES 15 B 360 GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR
SEQRES 16 B 360 ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP
SEQRES 17 B 360 ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR
SEQRES 18 B 360 THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO
SEQRES 19 B 360 GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY
SEQRES 20 B 360 GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP
SEQRES 21 B 360 TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG
SEQRES 22 B 360 GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP
SEQRES 23 B 360 GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS
SEQRES 24 B 360 ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR
SEQRES 25 B 360 VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER
SEQRES 26 B 360 GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG
SEQRES 27 B 360 LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY
SEQRES 28 B 360 LEU GLN VAL PHE SER PHE THR TYR GLY
SEQRES 1 C 360 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 C 360 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE
SEQRES 3 C 360 SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY
SEQRES 4 C 360 GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS
SEQRES 5 C 360 SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA
SEQRES 6 C 360 PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO
SEQRES 7 C 360 GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS
SEQRES 8 C 360 VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN
SEQRES 9 C 360 CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN
SEQRES 10 C 360 ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS
SEQRES 11 C 360 THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL
SEQRES 12 C 360 ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE
SEQRES 13 C 360 ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG
SEQRES 14 C 360 ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR
SEQRES 15 C 360 GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR
SEQRES 16 C 360 ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP
SEQRES 17 C 360 ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR
SEQRES 18 C 360 THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO
SEQRES 19 C 360 GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY
SEQRES 20 C 360 GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP
SEQRES 21 C 360 TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG
SEQRES 22 C 360 GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP
SEQRES 23 C 360 GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS
SEQRES 24 C 360 ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR
SEQRES 25 C 360 VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER
SEQRES 26 C 360 GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG
SEQRES 27 C 360 LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY
SEQRES 28 C 360 LEU GLN VAL PHE SER PHE THR TYR GLY
SEQRES 1 D 360 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 D 360 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE
SEQRES 3 D 360 SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY
SEQRES 4 D 360 GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS
SEQRES 5 D 360 SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA
SEQRES 6 D 360 PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO
SEQRES 7 D 360 GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS
SEQRES 8 D 360 VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN
SEQRES 9 D 360 CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN
SEQRES 10 D 360 ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS
SEQRES 11 D 360 THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL
SEQRES 12 D 360 ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE
SEQRES 13 D 360 ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG
SEQRES 14 D 360 ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR
SEQRES 15 D 360 GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR
SEQRES 16 D 360 ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP
SEQRES 17 D 360 ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR
SEQRES 18 D 360 THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO
SEQRES 19 D 360 GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY
SEQRES 20 D 360 GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP
SEQRES 21 D 360 TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG
SEQRES 22 D 360 GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP
SEQRES 23 D 360 GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS
SEQRES 24 D 360 ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR
SEQRES 25 D 360 VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER
SEQRES 26 D 360 GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG
SEQRES 27 D 360 LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY
SEQRES 28 D 360 LEU GLN VAL PHE SER PHE THR TYR GLY
FORMUL 5 HOH *486(H2 O)
HELIX 1 AA1 GLN A 383 CYS A 387 5 5
HELIX 2 AA2 THR A 412 LYS A 416 5 5
HELIX 3 AA3 ASP A 419 ARG A 424 5 6
HELIX 4 AA4 CYS A 437 LYS A 455 1 19
HELIX 5 AA5 TYR A 469 LYS A 473 5 5
HELIX 6 AA6 VAL A 474 LEU A 485 1 12
HELIX 7 AA7 TYR A 497 TYR A 503 1 7
HELIX 8 AA8 ASP A 529 LYS A 545 1 17
HELIX 9 AA9 PRO A 553 THR A 557 5 5
HELIX 10 AB1 GLN B 383 CYS B 387 5 5
HELIX 11 AB2 THR B 412 LYS B 416 5 5
HELIX 12 AB3 ASP B 419 ARG B 424 5 6
HELIX 13 AB4 CYS B 437 LYS B 455 1 19
HELIX 14 AB5 TYR B 469 LYS B 473 5 5
HELIX 15 AB6 VAL B 474 LEU B 485 1 12
HELIX 16 AB7 TYR B 497 TYR B 503 1 7
HELIX 17 AB8 ASP B 529 LYS B 545 1 17
HELIX 18 AB9 PRO B 553 THR B 557 5 5
HELIX 19 AC1 GLN C 383 CYS C 387 5 5
HELIX 20 AC2 THR C 412 LYS C 416 5 5
HELIX 21 AC3 ASP C 419 ARG C 424 5 6
HELIX 22 AC4 CYS C 437 LYS C 455 1 19
HELIX 23 AC5 TYR C 469 LYS C 473 5 5
HELIX 24 AC6 VAL C 474 GLY C 486 1 13
HELIX 25 AC7 TYR C 497 TYR C 503 1 7
HELIX 26 AC8 ASP C 529 LYS C 545 1 17
HELIX 27 AC9 PRO C 553 THR C 557 5 5
HELIX 28 AD1 GLN D 383 CYS D 387 5 5
HELIX 29 AD2 THR D 412 LYS D 416 5 5
HELIX 30 AD3 ASP D 419 ARG D 424 5 6
HELIX 31 AD4 CYS D 437 LYS D 455 1 19
HELIX 32 AD5 TYR D 469 LYS D 473 5 5
HELIX 33 AD6 VAL D 474 GLY D 486 1 13
HELIX 34 AD7 TYR D 497 TYR D 503 1 7
HELIX 35 AD8 ASP D 529 LYS D 545 1 17
HELIX 36 AD9 PRO D 553 THR D 557 5 5
SHEET 1 AA1 2 GLY A 364 THR A 365 0
SHEET 2 AA1 2 TYR B 507 TRP B 508 1 O TRP B 508 N GLY A 364
SHEET 1 AA2 6 GLY A 408 LEU A 410 0
SHEET 2 AA2 6 ILE A 491 LEU A 493 -1 O LEU A 493 N GLY A 408
SHEET 3 AA2 6 LEU A 459 HIS A 465 1 N GLY A 463 O ALA A 492
SHEET 4 AA2 6 VAL A 427 TRP A 433 1 N VAL A 427 O ALA A 460
SHEET 5 AA2 6 ALA A 510 ILE A 514 -1 O ILE A 514 N VAL A 428
SHEET 6 AA2 6 VAL A 520 PHE A 525 -1 O HIS A 522 N LEU A 513
SHEET 1 AA3 2 TYR A 507 TRP A 508 0
SHEET 2 AA3 2 GLY B 364 THR B 365 1 O GLY B 364 N TRP A 508
SHEET 1 AA4 4 GLY A 590 PHE A 594 0
SHEET 2 AA4 4 ALA A 618 SER A 620 0
SHEET 3 AA4 4 GLN A 688 GLY A 695 -1 O VAL A 689 N ALA A 618
SHEET 4 AA4 4 THR A 571 TYR A 572 -1 N THR A 571 O PHE A 692
SHEET 1 AA5 6 GLY A 590 PHE A 594 0
SHEET 2 AA5 6 PHE A 605 LEU A 613 -1 O TRP A 611 N ALA A 592
SHEET 3 AA5 6 ALA A 626 GLY A 641 -1 O LYS A 628 N ALA A 606
SHEET 4 AA5 6 THR A 664 PRO A 683 -1 O VAL A 668 N VAL A 636
SHEET 5 AA5 6 GLY A 644 ARG A 650 -1 N VAL A 649 O GLU A 680
SHEET 6 AA5 6 LYS A 653 ILE A 659 -1 O LEU A 657 N LEU A 646
SHEET 1 AA6 6 THR A 571 TYR A 572 0
SHEET 2 AA6 6 GLN A 688 GLY A 695 -1 O PHE A 692 N THR A 571
SHEET 3 AA6 6 ALA A 626 GLY A 641 -1 N VAL A 639 O PHE A 690
SHEET 4 AA6 6 THR A 664 PRO A 683 -1 O VAL A 668 N VAL A 636
SHEET 5 AA6 6 GLY A 644 ARG A 650 -1 N VAL A 649 O GLU A 680
SHEET 6 AA6 6 LYS A 653 ILE A 659 -1 O LEU A 657 N LEU A 646
SHEET 1 AA7 6 GLY B 408 LEU B 410 0
SHEET 2 AA7 6 ILE B 491 LEU B 493 -1 O LEU B 493 N GLY B 408
SHEET 3 AA7 6 LEU B 459 HIS B 465 1 N HIS B 465 O ALA B 492
SHEET 4 AA7 6 VAL B 427 TRP B 433 1 N VAL B 427 O ALA B 460
SHEET 5 AA7 6 ALA B 510 ILE B 514 -1 O ILE B 514 N VAL B 428
SHEET 6 AA7 6 VAL B 520 PHE B 525 -1 O ARG B 521 N LEU B 513
SHEET 1 AA8 4 GLY B 590 PHE B 594 0
SHEET 2 AA8 4 ALA B 618 SER B 620 0
SHEET 3 AA8 4 GLN B 688 GLY B 695 -1 O VAL B 689 N ALA B 618
SHEET 4 AA8 4 THR B 571 TYR B 572 -1 N THR B 571 O PHE B 692
SHEET 1 AA9 6 GLY B 590 PHE B 594 0
SHEET 2 AA9 6 SER B 604 LEU B 613 -1 O GLY B 609 N PHE B 594
SHEET 3 AA9 6 ALA B 626 GLY B 641 -1 O ASN B 630 N SER B 604
SHEET 4 AA9 6 THR B 664 PRO B 683 -1 O ALA B 675 N ALA B 633
SHEET 5 AA9 6 GLY B 644 VAL B 648 -1 N THR B 647 O ARG B 682
SHEET 6 AA9 6 THR B 656 ILE B 659 -1 O ILE B 659 N GLY B 644
SHEET 1 AB1 6 THR B 571 TYR B 572 0
SHEET 2 AB1 6 GLN B 688 GLY B 695 -1 O PHE B 692 N THR B 571
SHEET 3 AB1 6 ALA B 626 GLY B 641 -1 N VAL B 639 O PHE B 690
SHEET 4 AB1 6 THR B 664 PRO B 683 -1 O ALA B 675 N ALA B 633
SHEET 5 AB1 6 GLY B 644 VAL B 648 -1 N THR B 647 O ARG B 682
SHEET 6 AB1 6 THR B 656 ILE B 659 -1 O ILE B 659 N GLY B 644
SHEET 1 AB2 2 GLY C 364 THR C 365 0
SHEET 2 AB2 2 TYR D 507 TRP D 508 1 O TRP D 508 N GLY C 364
SHEET 1 AB3 5 ILE C 491 LEU C 493 0
SHEET 2 AB3 5 LEU C 459 HIS C 465 1 N HIS C 465 O ALA C 492
SHEET 3 AB3 5 VAL C 427 TRP C 433 1 N VAL C 427 O ALA C 460
SHEET 4 AB3 5 ALA C 510 ILE C 514 -1 O ILE C 514 N VAL C 428
SHEET 5 AB3 5 VAL C 520 PHE C 525 -1 O ARG C 521 N LEU C 513
SHEET 1 AB4 2 TYR C 507 TRP C 508 0
SHEET 2 AB4 2 GLY D 364 THR D 365 1 O GLY D 364 N TRP C 508
SHEET 1 AB5 4 GLY C 590 PHE C 594 0
SHEET 2 AB5 4 ALA C 618 SER C 620 0
SHEET 3 AB5 4 GLN C 688 GLY C 695 -1 O VAL C 689 N ALA C 618
SHEET 4 AB5 4 THR C 571 TYR C 572 -1 N THR C 571 O PHE C 692
SHEET 1 AB6 6 GLY C 590 PHE C 594 0
SHEET 2 AB6 6 SER C 604 LEU C 613 -1 O LEU C 613 N GLY C 590
SHEET 3 AB6 6 ALA C 626 GLY C 641 -1 O ALA C 626 N ARG C 608
SHEET 4 AB6 6 THR C 664 PRO C 683 -1 O VAL C 668 N VAL C 636
SHEET 5 AB6 6 GLY C 644 ARG C 650 -1 N VAL C 649 O GLU C 680
SHEET 6 AB6 6 LYS C 653 ILE C 659 -1 O ILE C 659 N GLY C 644
SHEET 1 AB7 6 THR C 571 TYR C 572 0
SHEET 2 AB7 6 GLN C 688 GLY C 695 -1 O PHE C 692 N THR C 571
SHEET 3 AB7 6 ALA C 626 GLY C 641 -1 N TYR C 637 O THR C 693
SHEET 4 AB7 6 THR C 664 PRO C 683 -1 O VAL C 668 N VAL C 636
SHEET 5 AB7 6 GLY C 644 ARG C 650 -1 N VAL C 649 O GLU C 680
SHEET 6 AB7 6 LYS C 653 ILE C 659 -1 O ILE C 659 N GLY C 644
SHEET 1 AB8 6 GLY D 408 LEU D 410 0
SHEET 2 AB8 6 ILE D 491 LEU D 493 -1 O LEU D 493 N GLY D 408
SHEET 3 AB8 6 LEU D 459 HIS D 465 1 N HIS D 465 O ALA D 492
SHEET 4 AB8 6 VAL D 427 TRP D 433 1 N VAL D 427 O ALA D 460
SHEET 5 AB8 6 ALA D 510 ILE D 514 -1 O ILE D 514 N VAL D 428
SHEET 6 AB8 6 VAL D 520 PHE D 525 -1 O ARG D 521 N LEU D 513
SHEET 1 AB9 4 GLY D 590 PHE D 594 0
SHEET 2 AB9 4 ALA D 618 SER D 620 0
SHEET 3 AB9 4 GLN D 688 GLY D 695 -1 O VAL D 689 N ALA D 618
SHEET 4 AB9 4 THR D 571 TYR D 572 -1 N THR D 571 O PHE D 692
SHEET 1 AC1 6 GLY D 590 PHE D 594 0
SHEET 2 AC1 6 SER D 604 LEU D 613 -1 O GLY D 609 N PHE D 594
SHEET 3 AC1 6 ALA D 626 GLY D 641 -1 O LYS D 628 N ALA D 606
SHEET 4 AC1 6 THR D 664 PRO D 683 -1 O LEU D 679 N LEU D 629
SHEET 5 AC1 6 GLY D 644 VAL D 649 -1 N THR D 647 O ARG D 682
SHEET 6 AC1 6 ALA D 655 ILE D 659 -1 O ILE D 659 N GLY D 644
SHEET 1 AC2 6 THR D 571 TYR D 572 0
SHEET 2 AC2 6 GLN D 688 GLY D 695 -1 O PHE D 692 N THR D 571
SHEET 3 AC2 6 ALA D 626 GLY D 641 -1 N VAL D 639 O SER D 691
SHEET 4 AC2 6 THR D 664 PRO D 683 -1 O LEU D 679 N LEU D 629
SHEET 5 AC2 6 GLY D 644 VAL D 649 -1 N THR D 647 O ARG D 682
SHEET 6 AC2 6 ALA D 655 ILE D 659 -1 O ILE D 659 N GLY D 644
SSBOND 1 CYS A 387 CYS A 397 1555 1555 2.03
SSBOND 2 CYS B 387 CYS B 397 1555 1555 2.03
SSBOND 3 CYS C 387 CYS C 397 1555 1555 2.03
SSBOND 4 CYS C 437 CYS C 440 1555 1555 2.05
SSBOND 5 CYS D 387 CYS D 397 1555 1555 2.03
SSBOND 6 CYS D 437 CYS D 440 1555 1555 2.05
CISPEP 1 TRP A 508 PRO A 509 0 -12.18
CISPEP 2 TRP B 508 PRO B 509 0 -12.87
CISPEP 3 TRP C 508 PRO C 509 0 -10.91
CISPEP 4 TRP D 508 PRO D 509 0 -8.61
CRYST1 109.972 117.525 122.438 90.00 90.00 90.00 P 21 21 21 16
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 0.009093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END