HEADER HYDROLASE 29-AUG-17 5OVR
TITLE X-RAY CHARACTERIZATION OF STRIATAL-ENRICHED PROTEIN TYROSINE
TITLE 2 PHOSPHATASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEURAL-SPECIFIC PROTEIN-TYROSINE PHOSPHATASE,STRIATUM-
COMPND 5 ENRICHED PROTEIN-TYROSINE PHOSPHATASE,STEP;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTPN5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHATASE ALZHEIMER'S DISEASE INHIBITOR STEP, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KACK,L.WISSLER
REVDAT 3 17-JAN-24 5OVR 1 REMARK
REVDAT 2 29-NOV-17 5OVR 1 JRNL
REVDAT 1 22-NOV-17 5OVR 0
JRNL AUTH M.R.WITTEN,L.WISSLER,M.SNOW,S.GESCHWINDNER,J.A.READ,
JRNL AUTH 2 N.J.BRANDON,A.C.NAIRN,P.J.LOMBROSO,H.KACK,J.A.ELLMAN
JRNL TITL X-RAY CHARACTERIZATION AND STRUCTURE-BASED OPTIMIZATION OF
JRNL TITL 2 STRIATAL-ENRICHED PROTEIN TYROSINE PHOSPHATASE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 9299 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29116812
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01292
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 18980
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.420
REMARK 3 FREE R VALUE TEST SET COUNT : 1028
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.03
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2522
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE : 0.4500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.25
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 168
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.16690
REMARK 3 B22 (A**2) : 1.12870
REMARK 3 B33 (A**2) : 1.03810
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.277
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.338
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.255
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.269
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.237
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 : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2429 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3306 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 837 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 66 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 354 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2429 ; 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 : 312 ; 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 : 3030 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.48
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.89
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19180
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 100.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.76500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2BV5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-28% PEG3350, 0.1M BIS-TRIS PH5.5,
REMARK 280 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 26.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.21500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.21500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.16000
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 235
REMARK 465 HIS A 236
REMARK 465 HIS A 237
REMARK 465 HIS A 238
REMARK 465 HIS A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 SER A 242
REMARK 465 SER A 243
REMARK 465 GLY A 244
REMARK 465 VAL A 245
REMARK 465 ASP A 246
REMARK 465 LEU A 247
REMARK 465 GLY A 248
REMARK 465 THR A 249
REMARK 465 GLU A 250
REMARK 465 GLN A 538
REMARK 465 SER A 539
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 294 76.82 -118.90
REMARK 500 ILE A 374 76.73 -108.07
REMARK 500 GLU A 391 -64.65 -136.84
REMARK 500 ILE A 476 -50.97 -128.99
REMARK 500 ILE A 515 82.10 74.72
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 A1079 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A1080 DISTANCE = 6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AXK A 601
DBREF 5OVR A 258 537 UNP P54829 PTN5_HUMAN 250 529
SEQADV 5OVR MET A 235 UNP P54829 INITIATING METHIONINE
SEQADV 5OVR HIS A 236 UNP P54829 EXPRESSION TAG
SEQADV 5OVR HIS A 237 UNP P54829 EXPRESSION TAG
SEQADV 5OVR HIS A 238 UNP P54829 EXPRESSION TAG
SEQADV 5OVR HIS A 239 UNP P54829 EXPRESSION TAG
SEQADV 5OVR HIS A 240 UNP P54829 EXPRESSION TAG
SEQADV 5OVR HIS A 241 UNP P54829 EXPRESSION TAG
SEQADV 5OVR SER A 242 UNP P54829 EXPRESSION TAG
SEQADV 5OVR SER A 243 UNP P54829 EXPRESSION TAG
SEQADV 5OVR GLY A 244 UNP P54829 EXPRESSION TAG
SEQADV 5OVR VAL A 245 UNP P54829 EXPRESSION TAG
SEQADV 5OVR ASP A 246 UNP P54829 EXPRESSION TAG
SEQADV 5OVR LEU A 247 UNP P54829 EXPRESSION TAG
SEQADV 5OVR GLY A 248 UNP P54829 EXPRESSION TAG
SEQADV 5OVR THR A 249 UNP P54829 EXPRESSION TAG
SEQADV 5OVR GLU A 250 UNP P54829 EXPRESSION TAG
SEQADV 5OVR ASN A 251 UNP P54829 EXPRESSION TAG
SEQADV 5OVR LEU A 252 UNP P54829 EXPRESSION TAG
SEQADV 5OVR TYR A 253 UNP P54829 EXPRESSION TAG
SEQADV 5OVR PHE A 254 UNP P54829 EXPRESSION TAG
SEQADV 5OVR GLN A 255 UNP P54829 EXPRESSION TAG
SEQADV 5OVR SER A 256 UNP P54829 EXPRESSION TAG
SEQADV 5OVR MET A 257 UNP P54829 EXPRESSION TAG
SEQADV 5OVR GLN A 538 UNP P54829 EXPRESSION TAG
SEQADV 5OVR SER A 539 UNP P54829 EXPRESSION TAG
SEQRES 1 A 305 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 305 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ARG VAL
SEQRES 3 A 305 LEU GLN ALA GLU GLU LEU HIS GLU LYS ALA LEU ASP PRO
SEQRES 4 A 305 PHE LEU LEU GLN ALA GLU PHE PHE GLU ILE PRO MET ASN
SEQRES 5 A 305 PHE VAL ASP PRO LYS GLU TYR ASP ILE PRO GLY LEU VAL
SEQRES 6 A 305 ARG LYS ASN ARG TYR LYS THR ILE LEU PRO ASN PRO HIS
SEQRES 7 A 305 SER ARG VAL CYS LEU THR SER PRO ASP PRO ASP ASP PRO
SEQRES 8 A 305 LEU SER SER TYR ILE ASN ALA ASN TYR ILE ARG GLY TYR
SEQRES 9 A 305 GLY GLY GLU GLU LYS VAL TYR ILE ALA THR GLN GLY PRO
SEQRES 10 A 305 ILE VAL SER THR VAL ALA ASP PHE TRP ARG MET VAL TRP
SEQRES 11 A 305 GLN GLU HIS THR PRO ILE ILE VAL MET ILE THR ASN ILE
SEQRES 12 A 305 GLU GLU MET ASN GLU LYS CYS THR GLU TYR TRP PRO GLU
SEQRES 13 A 305 GLU GLN VAL ALA TYR ASP GLY VAL GLU ILE THR VAL GLN
SEQRES 14 A 305 LYS VAL ILE HIS THR GLU ASP TYR ARG LEU ARG LEU ILE
SEQRES 15 A 305 SER LEU LYS SER GLY THR GLU GLU ARG GLY LEU LYS HIS
SEQRES 16 A 305 TYR TRP PHE THR SER TRP PRO ASP GLN LYS THR PRO ASP
SEQRES 17 A 305 ARG ALA PRO PRO LEU LEU HIS LEU VAL ARG GLU VAL GLU
SEQRES 18 A 305 GLU ALA ALA GLN GLN GLU GLY PRO HIS CYS ALA PRO ILE
SEQRES 19 A 305 ILE VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY CYS
SEQRES 20 A 305 PHE ILE ALA THR SER ILE CYS CYS GLN GLN LEU ARG GLN
SEQRES 21 A 305 GLU GLY VAL VAL ASP ILE LEU LYS THR THR CYS GLN LEU
SEQRES 22 A 305 ARG GLN ASP ARG GLY GLY MET ILE GLN THR CSO GLU GLN
SEQRES 23 A 305 TYR GLN PHE VAL HIS HIS VAL MET SER LEU TYR GLU LYS
SEQRES 24 A 305 GLN LEU SER HIS GLN SER
MODRES 5OVR CSO A 518 CYS MODIFIED RESIDUE
HET CSO A 518 7
HET AXK A 601 28
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM AXK [(~{S})-[4-[3-[(~{R})-(3,4-DICHLOROPHENYL)-OXIDANYL-
HETNAM 2 AXK METHYL]PHENYL]PHENYL]-OXIDANYL-METHYL]PHOSPHONIC ACID
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 2 AXK C20 H17 CL2 O5 P
FORMUL 3 HOH *380(H2 O)
HELIX 1 AA1 GLN A 262 ALA A 270 1 9
HELIX 2 AA2 ASP A 272 PHE A 281 1 10
HELIX 3 AA3 ASP A 289 TYR A 293 5 5
HELIX 4 AA4 GLY A 297 ASN A 302 5 6
HELIX 5 AA5 ASN A 310 ARG A 314 5 5
HELIX 6 AA6 GLY A 337 GLU A 341 5 5
HELIX 7 AA7 ILE A 352 SER A 354 5 3
HELIX 8 AA8 THR A 355 HIS A 367 1 13
HELIX 9 AA9 ASN A 376 MET A 380 5 5
HELIX 10 AB1 THR A 440 ASP A 442 5 3
HELIX 11 AB2 ARG A 443 GLN A 460 1 18
HELIX 12 AB3 ILE A 476 GLY A 496 1 21
HELIX 13 AB4 ASP A 499 ARG A 511 1 13
HELIX 14 AB5 THR A 517 HIS A 537 1 21
SHEET 1 AA1 8 ALA A 332 ILE A 335 0
SHEET 2 AA1 8 TYR A 345 GLN A 349 -1 O TYR A 345 N ILE A 335
SHEET 3 AA1 8 ILE A 468 CYS A 472 1 O VAL A 470 N ILE A 346
SHEET 4 AA1 8 ILE A 370 ILE A 374 1 N ILE A 374 O HIS A 471
SHEET 5 AA1 8 GLU A 423 PHE A 432 1 O TYR A 430 N ILE A 371
SHEET 6 AA1 8 TYR A 411 SER A 420 -1 N ILE A 416 O LEU A 427
SHEET 7 AA1 8 VAL A 398 HIS A 407 -1 N ILE A 406 O LEU A 413
SHEET 8 AA1 8 GLN A 392 TYR A 395 -1 N VAL A 393 O ILE A 400
LINK C THR A 517 N CSO A 518 1555 1555 1.35
LINK C CSO A 518 N GLU A 519 1555 1555 1.35
CISPEP 1 SER A 319 PRO A 320 0 6.87
CISPEP 2 MET A 380 ASN A 381 0 4.97
SITE 1 AC1 14 ASN A 376 GLU A 378 GLU A 379 SER A 434
SITE 2 AC1 14 TRP A 435 PRO A 436 ASP A 437 LYS A 439
SITE 3 AC1 14 ARG A 443 ARG A 478 GLN A 520 HOH A 720
SITE 4 AC1 14 HOH A 734 HOH A 774
CRYST1 52.500 64.320 100.430 90.00 90.00 90.00 P 21 21 21 4
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 0.019048 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009957 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
