HEADER CHAPERONE 02-DEC-15 5FPM
TITLE STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
TITLE 2 LIGAND 5-PHENYL-1,3,4-OXADIAZOLE-2-THIOL (AT809) IN AN ALTERNATE
TITLE 3 BINDING SITE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK-RELATED 70KDA PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS HEAT SHOCK-RELATED PROTEIN, HEAT SHOCK, CHAPERONE, HSP70, HSPA2,
KEYWDS 2 PROTEIN-LIGAND COMPLEX, FRAGMENT SCREENING, ALTERNATE BINDING SITE,
KEYWDS 3 AT809.
EXPDTA X-RAY DIFFRACTION
AUTHOR H.JHOTI,R.F.LUDLOW,S.PATEL,H.K.SAINI,I.J.TICKLE,M.VERDONK
REVDAT 4 10-JAN-24 5FPM 1 REMARK
REVDAT 3 13-JAN-16 5FPM 1 JRNL
REVDAT 2 23-DEC-15 5FPM 1 JRNL
REVDAT 1 16-DEC-15 5FPM 0
JRNL AUTH R.F.LUDLOW,M.L.VERDONK,H.K.SAINI,I.J.TICKLE,H.JHOTI
JRNL TITL DETECTION OF SECONDARY BINDING SITES IN PROTEINS USING
JRNL TITL 2 FRAGMENT SCREENING.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 15910 2015
JRNL REFN ISSN 0027-8424
JRNL PMID 26655740
JRNL DOI 10.1073/PNAS.1518946112
REMARK 2
REMARK 2 RESOLUTION. 1.96 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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 52336
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2660
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.01
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.29
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3367
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1790
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3220
REMARK 3 BIN R VALUE (WORKING SET) : 0.1763
REMARK 3 BIN FREE R VALUE : 0.2385
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5776
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 1093
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.11370
REMARK 3 B22 (A**2) : -0.16820
REMARK 3 B33 (A**2) : -1.94550
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.40790
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.191
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.206
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.166
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.177
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.156
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 : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5904 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7982 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2068 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 155 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 890 ; 16.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5904 ; 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 : 803 ; 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 : 8099 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 5.60
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.80
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4990 -9.2813 2.7160
REMARK 3 T TENSOR
REMARK 3 T11: -0.0321 T22: -0.0586
REMARK 3 T33: -0.0525 T12: 0.0126
REMARK 3 T13: -0.0170 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.5316 L22: 0.8735
REMARK 3 L33: 0.7546 L12: -0.1745
REMARK 3 L13: 0.3313 L23: -0.3131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -0.0170 S13: 0.0067
REMARK 3 S21: 0.0283 S22: 0.0044 S23: -0.0561
REMARK 3 S31: 0.0198 S32: 0.0424 S33: 0.0086
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4639 8.3550 -8.1831
REMARK 3 T TENSOR
REMARK 3 T11: -0.0251 T22: -0.0584
REMARK 3 T33: 0.0007 T12: 0.0037
REMARK 3 T13: -0.0410 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 1.1567 L22: 0.8265
REMARK 3 L33: 1.5827 L12: 0.0090
REMARK 3 L13: 0.5686 L23: 0.0774
REMARK 3 S TENSOR
REMARK 3 S11: -0.0532 S12: 0.1591 S13: 0.2153
REMARK 3 S21: -0.0853 S22: 0.0093 S23: 0.0099
REMARK 3 S31: -0.0441 S32: 0.0114 S33: 0.0439
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0139 16.3165 19.0281
REMARK 3 T TENSOR
REMARK 3 T11: -0.0258 T22: -0.0573
REMARK 3 T33: 0.0116 T12: 0.0313
REMARK 3 T13: -0.0313 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.8228 L22: 0.9890
REMARK 3 L33: 3.0000 L12: 0.3530
REMARK 3 L13: 2.1135 L23: 0.1306
REMARK 3 S TENSOR
REMARK 3 S11: -0.2275 S12: -0.3186 S13: 0.3136
REMARK 3 S21: 0.0612 S22: -0.0897 S23: 0.1697
REMARK 3 S31: -0.2516 S32: -0.2246 S33: 0.3172
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6623 0.1050 38.2440
REMARK 3 T TENSOR
REMARK 3 T11: -0.0369 T22: -0.0562
REMARK 3 T33: -0.0602 T12: -0.0156
REMARK 3 T13: 0.0030 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.4459 L22: 0.8808
REMARK 3 L33: 0.7992 L12: 0.1756
REMARK 3 L13: -0.2081 L23: -0.2922
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: 0.0811 S13: -0.0371
REMARK 3 S21: -0.0157 S22: 0.0098 S23: -0.0311
REMARK 3 S31: -0.0470 S32: 0.0002 S33: 0.0327
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6568 -17.7412 48.7625
REMARK 3 T TENSOR
REMARK 3 T11: -0.0211 T22: -0.0670
REMARK 3 T33: 0.0136 T12: -0.0215
REMARK 3 T13: 0.0453 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.3674 L22: 1.1528
REMARK 3 L33: 1.6452 L12: -0.7424
REMARK 3 L13: -0.3159 L23: 0.4953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: -0.1305 S13: -0.3119
REMARK 3 S21: 0.1196 S22: 0.0270 S23: 0.1735
REMARK 3 S31: 0.1037 S32: -0.0469 S33: 0.0201
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 49.3237 -25.2287 21.8448
REMARK 3 T TENSOR
REMARK 3 T11: -0.0154 T22: -0.0573
REMARK 3 T33: -0.0045 T12: -0.0131
REMARK 3 T13: -0.0128 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 2.5110 L22: 1.1409
REMARK 3 L33: 1.8628 L12: 0.5830
REMARK 3 L13: -1.2098 L23: -0.1999
REMARK 3 S TENSOR
REMARK 3 S11: -0.1555 S12: 0.2178 S13: -0.0951
REMARK 3 S21: -0.0856 S22: -0.0186 S23: 0.0446
REMARK 3 S31: 0.0953 S32: -0.0753 S33: 0.1741
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1290065673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53541
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 38.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CSEARCH
REMARK 200 STARTING MODEL: PDB ENTRY 5FPD
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M NACL, 0.1M TRIS/HCL PH=8, 20.0%
REMARK 280 W/V PEG 8000. PROTEIN CONC. = 11MG/ML., PH 8
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 47.48000
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 ARG A 3
REMARK 465 ALA A 191
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 ARG B 3
REMARK 465 ALA B 191
REMARK 465 GLY B 192
REMARK 465 ASP B 385
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 25 CE NZ
REMARK 470 LYS A 77 CE NZ
REMARK 470 LYS A 88 CD CE NZ
REMARK 470 LYS A 100 CE NZ
REMARK 470 LYS A 138 NZ
REMARK 470 LYS A 187 NZ
REMARK 470 CYS A 190 CA C O CB SG
REMARK 470 LYS A 195 CD CE NZ
REMARK 470 LYS A 222 CE NZ
REMARK 470 GLU A 233 CG CD OE1 OE2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 GLU A 317 CD OE1 OE2
REMARK 470 LYS A 321 CE NZ
REMARK 470 LYS A 350 CE NZ
REMARK 470 GLU A 360 OE1 OE2
REMARK 470 ASP A 385 CA C O CB CG OD1 OD2
REMARK 470 LYS B 77 NZ
REMARK 470 LYS B 88 CD CE NZ
REMARK 470 LYS B 100 CE NZ
REMARK 470 LYS B 138 CD CE NZ
REMARK 470 LYS B 222 CD CE NZ
REMARK 470 LYS B 248 CE NZ
REMARK 470 ARG B 249 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 252 CD CE NZ
REMARK 470 LYS B 253 CE NZ
REMARK 470 LYS B 321 CE NZ
REMARK 470 LYS B 327 CD CE NZ
REMARK 470 LYS B 350 CE NZ
REMARK 470 GLU B 360 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2205 O HOH A 2206 1.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 306 O HOH B 2270 2746 1.90
REMARK 500 OD2 ASP B 329 O HOH A 2464 2646 2.08
REMARK 500 O HOH A 2304 O HOH B 2312 1554 2.09
REMARK 500 O HOH A 2411 O HOH B 2511 2656 2.09
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 ASN A 62 51.77 -146.49
REMARK 500 SER A 288 64.82 39.07
REMARK 500 ASN B 62 53.44 -143.84
REMARK 500 SER B 288 63.47 38.01
REMARK 500 LYS B 363 1.77 -153.85
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 A2216 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A2274 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B2033 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B2086 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH B2161 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B2165 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B2252 DISTANCE = 5.85 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 5-PHENYL-1,3,4-OXADIAZOLE-2-THIOL (IWT): ASTEX COMPOUND
REMARK 600 REGISTRY AT809.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IWT B 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IWT A 1385
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FP5 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL- MOLECULE LIGAND
REMARK 900 4-FLUOROBENZOIC ACID (AT222) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FP6 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL- MOLECULE LIGAND
REMARK 900 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP -2-YN-1-OL (AT17833) IN AN
REMARK 900 ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPD RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND PYRAZINE-2-CARBOXAMIDE (AT513) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPE RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND 1H-1,2,4-TRIAZOL-3-AMINE ( AT485) IN AN ALTERNATE BINDING
REMARK 900 SITE.
REMARK 900 RELATED ID: 5FPN RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND 3,5-DIMETHYL-1H-PYRAZOLE-4- CARBOXYLIC ACID (AT9084) IN AN
REMARK 900 ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPO RELATED DB: PDB
REMARK 900 STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE LIGAND 1H-
REMARK 900 INDAZOL-7-AMINE (AT4213) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPR RELATED DB: PDB
REMARK 900 STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE LIGAND
REMARK 900 PYRIMIDIN-2-AMINE (AT371) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPS RELATED DB: PDB
REMARK 900 STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
REMARK 900 SMALL-MOLECULE LIGAND 3-AMINOBENZENE-1,2 -DICARBOXYLIC ACID (AT1246)
REMARK 900 IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPT RELATED DB: PDB
REMARK 900 STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
REMARK 900 SMALL-MOLECULE LIGAND 2-(1-METHYL-1H- INDOL-3-YL)ACETIC ACID
REMARK 900 (AT3437) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPY RELATED DB: PDB
REMARK 900 STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
REMARK 900 SMALL-MOLECULE LIGAND 5-BROMO-1-METHYL- 1H-INDOLE-2-CARBOXYLIC ACID
REMARK 900 (AT21457) IN AN ALTERNATE BINDING SITE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 3 EXTRA RESIDUES AT N TERM ARE REMAINS OF HIS TAG AFTER
REMARK 999 THROMBIN CLEAVAGE. RESIDUES 2-3 DELETED. RESIDUES 386-639
REMARK 999 DELETED.
DBREF 5FPM A 0 385 UNP P54652 HSP72_HUMAN 1 386
DBREF 5FPM B 0 385 UNP P54652 HSP72_HUMAN 1 386
SEQADV 5FPM GLY A -3 UNP P54652 EXPRESSION TAG
SEQADV 5FPM SER A -2 UNP P54652 EXPRESSION TAG
SEQADV 5FPM HIS A -1 UNP P54652 EXPRESSION TAG
SEQADV 5FPM A UNP P54652 SER 2 DELETION
SEQADV 5FPM A UNP P54652 ALA 3 DELETION
SEQADV 5FPM GLY B -3 UNP P54652 EXPRESSION TAG
SEQADV 5FPM SER B -2 UNP P54652 EXPRESSION TAG
SEQADV 5FPM HIS B -1 UNP P54652 EXPRESSION TAG
SEQADV 5FPM B UNP P54652 SER 2 DELETION
SEQADV 5FPM B UNP P54652 ALA 3 DELETION
SEQRES 1 A 387 GLY SER HIS MET ARG GLY PRO ALA ILE GLY ILE ASP LEU
SEQRES 2 A 387 GLY THR THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY
SEQRES 3 A 387 LYS VAL GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR
SEQRES 4 A 387 THR PRO SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU
SEQRES 5 A 387 ILE GLY ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO
SEQRES 6 A 387 THR ASN THR ILE PHE ASP ALA LYS ARG LEU ILE GLY ARG
SEQRES 7 A 387 LYS PHE GLU ASP ALA THR VAL GLN SER ASP MET LYS HIS
SEQRES 8 A 387 TRP PRO PHE ARG VAL VAL SER GLU GLY GLY LYS PRO LYS
SEQRES 9 A 387 VAL GLN VAL GLU TYR LYS GLY GLU THR LYS THR PHE PHE
SEQRES 10 A 387 PRO GLU GLU ILE SER SER MET VAL LEU THR LYS MET LYS
SEQRES 11 A 387 GLU ILE ALA GLU ALA TYR LEU GLY GLY LYS VAL HIS SER
SEQRES 12 A 387 ALA VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN
SEQRES 13 A 387 ARG GLN ALA THR LYS ASP ALA GLY THR ILE THR GLY LEU
SEQRES 14 A 387 ASN VAL LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA
SEQRES 15 A 387 ILE ALA TYR GLY LEU ASP LYS LYS GLY CYS ALA GLY GLY
SEQRES 16 A 387 GLU LYS ASN VAL LEU ILE PHE ASP LEU GLY GLY GLY THR
SEQRES 17 A 387 PHE ASP VAL SER ILE LEU THR ILE GLU ASP GLY ILE PHE
SEQRES 18 A 387 GLU VAL LYS SER THR ALA GLY ASP THR HIS LEU GLY GLY
SEQRES 19 A 387 GLU ASP PHE ASP ASN ARG MET VAL SER HIS LEU ALA GLU
SEQRES 20 A 387 GLU PHE LYS ARG LYS HIS LYS LYS ASP ILE GLY PRO ASN
SEQRES 21 A 387 LYS ARG ALA VAL ARG ARG LEU ARG THR ALA CYS GLU ARG
SEQRES 22 A 387 ALA LYS ARG THR LEU SER SER SER THR GLN ALA SER ILE
SEQRES 23 A 387 GLU ILE ASP SER LEU TYR GLU GLY VAL ASP PHE TYR THR
SEQRES 24 A 387 SER ILE THR ARG ALA ARG PHE GLU GLU LEU ASN ALA ASP
SEQRES 25 A 387 LEU PHE ARG GLY THR LEU GLU PRO VAL GLU LYS ALA LEU
SEQRES 26 A 387 ARG ASP ALA LYS LEU ASP LYS GLY GLN ILE GLN GLU ILE
SEQRES 27 A 387 VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS ILE GLN
SEQRES 28 A 387 LYS LEU LEU GLN ASP PHE PHE ASN GLY LYS GLU LEU ASN
SEQRES 29 A 387 LYS SER ILE ASN PRO ASP GLU ALA VAL ALA TYR GLY ALA
SEQRES 30 A 387 ALA VAL GLN ALA ALA ILE LEU ILE GLY ASP
SEQRES 1 B 387 GLY SER HIS MET ARG GLY PRO ALA ILE GLY ILE ASP LEU
SEQRES 2 B 387 GLY THR THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY
SEQRES 3 B 387 LYS VAL GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR
SEQRES 4 B 387 THR PRO SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU
SEQRES 5 B 387 ILE GLY ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO
SEQRES 6 B 387 THR ASN THR ILE PHE ASP ALA LYS ARG LEU ILE GLY ARG
SEQRES 7 B 387 LYS PHE GLU ASP ALA THR VAL GLN SER ASP MET LYS HIS
SEQRES 8 B 387 TRP PRO PHE ARG VAL VAL SER GLU GLY GLY LYS PRO LYS
SEQRES 9 B 387 VAL GLN VAL GLU TYR LYS GLY GLU THR LYS THR PHE PHE
SEQRES 10 B 387 PRO GLU GLU ILE SER SER MET VAL LEU THR LYS MET LYS
SEQRES 11 B 387 GLU ILE ALA GLU ALA TYR LEU GLY GLY LYS VAL HIS SER
SEQRES 12 B 387 ALA VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN
SEQRES 13 B 387 ARG GLN ALA THR LYS ASP ALA GLY THR ILE THR GLY LEU
SEQRES 14 B 387 ASN VAL LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA
SEQRES 15 B 387 ILE ALA TYR GLY LEU ASP LYS LYS GLY CYS ALA GLY GLY
SEQRES 16 B 387 GLU LYS ASN VAL LEU ILE PHE ASP LEU GLY GLY GLY THR
SEQRES 17 B 387 PHE ASP VAL SER ILE LEU THR ILE GLU ASP GLY ILE PHE
SEQRES 18 B 387 GLU VAL LYS SER THR ALA GLY ASP THR HIS LEU GLY GLY
SEQRES 19 B 387 GLU ASP PHE ASP ASN ARG MET VAL SER HIS LEU ALA GLU
SEQRES 20 B 387 GLU PHE LYS ARG LYS HIS LYS LYS ASP ILE GLY PRO ASN
SEQRES 21 B 387 LYS ARG ALA VAL ARG ARG LEU ARG THR ALA CYS GLU ARG
SEQRES 22 B 387 ALA LYS ARG THR LEU SER SER SER THR GLN ALA SER ILE
SEQRES 23 B 387 GLU ILE ASP SER LEU TYR GLU GLY VAL ASP PHE TYR THR
SEQRES 24 B 387 SER ILE THR ARG ALA ARG PHE GLU GLU LEU ASN ALA ASP
SEQRES 25 B 387 LEU PHE ARG GLY THR LEU GLU PRO VAL GLU LYS ALA LEU
SEQRES 26 B 387 ARG ASP ALA LYS LEU ASP LYS GLY GLN ILE GLN GLU ILE
SEQRES 27 B 387 VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS ILE GLN
SEQRES 28 B 387 LYS LEU LEU GLN ASP PHE PHE ASN GLY LYS GLU LEU ASN
SEQRES 29 B 387 LYS SER ILE ASN PRO ASP GLU ALA VAL ALA TYR GLY ALA
SEQRES 30 B 387 ALA VAL GLN ALA ALA ILE LEU ILE GLY ASP
HET IWT A1385 18
HET IWT B1385 18
HETNAM IWT 5-PHENYL-1,3,4-OXADIAZOLE-2-THIOL
FORMUL 3 IWT 2(C8 H6 N2 O S)
FORMUL 5 HOH *1093(H2 O)
HELIX 1 1 GLY A 52 GLN A 58 1 7
HELIX 2 2 ASN A 62 THR A 64 5 3
HELIX 3 3 ASP A 69 LEU A 73 5 5
HELIX 4 4 ASP A 80 LYS A 88 1 9
HELIX 5 5 PHE A 115 GLY A 136 1 22
HELIX 6 6 ASN A 151 GLY A 166 1 16
HELIX 7 7 GLU A 175 TYR A 183 1 9
HELIX 8 8 GLY A 231 LYS A 252 1 22
HELIX 9 9 ASN A 258 SER A 277 1 20
HELIX 10 10 ARG A 301 ASN A 308 1 8
HELIX 11 11 ASN A 308 THR A 315 1 8
HELIX 12 12 THR A 315 LYS A 327 1 13
HELIX 13 13 ASP A 329 ILE A 333 5 5
HELIX 14 14 GLY A 340 ARG A 344 5 5
HELIX 15 15 ILE A 345 PHE A 356 1 12
HELIX 16 16 GLU A 369 GLY A 384 1 16
HELIX 17 17 GLY B 52 GLN B 58 1 7
HELIX 18 18 ASN B 62 THR B 64 5 3
HELIX 19 19 ASP B 69 LEU B 73 5 5
HELIX 20 20 ASP B 80 LYS B 88 1 9
HELIX 21 21 PHE B 115 GLY B 136 1 22
HELIX 22 22 ASN B 151 GLY B 166 1 16
HELIX 23 23 GLU B 175 TYR B 183 1 9
HELIX 24 24 GLY B 231 LYS B 252 1 22
HELIX 25 25 ASN B 258 LEU B 276 1 19
HELIX 26 26 ARG B 301 ASN B 308 1 8
HELIX 27 27 ASN B 308 GLY B 314 1 7
HELIX 28 28 THR B 315 LYS B 327 1 13
HELIX 29 29 ASP B 329 ILE B 333 5 5
HELIX 30 30 GLY B 340 ARG B 344 5 5
HELIX 31 31 ILE B 345 PHE B 356 1 12
HELIX 32 32 GLU B 369 GLY B 384 1 16
SHEET 1 AA 2 LYS A 25 ILE A 28 0
SHEET 2 AA 2 TYR A 15 GLN A 22 1 O VAL A 20 N GLU A 27
SHEET 1 AB 2 THR A 38 PRO A 39 0
SHEET 2 AB 2 TYR A 15 GLN A 22 -1 O SER A 16 N THR A 38
SHEET 1 AC 5 ASN A 168 ASN A 174 0
SHEET 2 AC 5 SER A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 AC 5 ALA A 6 ASP A 10 1 O ILE A 7 N VAL A 143
SHEET 4 AC 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 AC 5 LYS A 25 ILE A 28 1 O LYS A 25 N GLN A 22
SHEET 1 AD 5 ASN A 168 ASN A 174 0
SHEET 2 AD 5 SER A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 AD 5 ALA A 6 ASP A 10 1 O ILE A 7 N VAL A 143
SHEET 4 AD 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 AD 5 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 AE 3 ARG A 49 ILE A 51 0
SHEET 2 AE 3 VAL A 42 PHE A 44 -1 O ALA A 43 N LEU A 50
SHEET 3 AE 3 THR A 66 ILE A 67 -1 O ILE A 67 N VAL A 42
SHEET 1 AF 3 ARG A 93 GLU A 97 0
SHEET 2 AF 3 LYS A 100 TYR A 107 -1 O LYS A 100 N GLU A 97
SHEET 3 AF 3 GLU A 110 PHE A 114 -1 O GLU A 110 N TYR A 107
SHEET 1 AG 4 ILE A 218 ASP A 227 0
SHEET 2 AG 4 PHE A 207 GLU A 215 -1 O PHE A 207 N ASP A 227
SHEET 3 AG 4 GLU A 194 LEU A 202 -1 O LYS A 195 N ILE A 214
SHEET 4 AG 4 GLU A 335 VAL A 339 1 O GLU A 335 N LEU A 198
SHEET 1 AH 2 GLN A 281 TYR A 290 0
SHEET 2 AH 2 VAL A 293 THR A 300 -1 O VAL A 293 N LEU A 289
SHEET 1 BA 2 LYS B 25 ILE B 28 0
SHEET 2 BA 2 TYR B 15 GLN B 22 1 O VAL B 20 N GLU B 27
SHEET 1 BB 2 THR B 38 PRO B 39 0
SHEET 2 BB 2 TYR B 15 GLN B 22 -1 O SER B 16 N THR B 38
SHEET 1 BC 5 ASN B 168 ASN B 174 0
SHEET 2 BC 5 SER B 141 VAL B 146 1 O ALA B 142 N LEU B 170
SHEET 3 BC 5 ALA B 6 ASP B 10 1 O ILE B 7 N VAL B 143
SHEET 4 BC 5 TYR B 15 GLN B 22 -1 O CYS B 17 N ASP B 10
SHEET 5 BC 5 LYS B 25 ILE B 28 1 O LYS B 25 N GLN B 22
SHEET 1 BD 5 ASN B 168 ASN B 174 0
SHEET 2 BD 5 SER B 141 VAL B 146 1 O ALA B 142 N LEU B 170
SHEET 3 BD 5 ALA B 6 ASP B 10 1 O ILE B 7 N VAL B 143
SHEET 4 BD 5 TYR B 15 GLN B 22 -1 O CYS B 17 N ASP B 10
SHEET 5 BD 5 THR B 38 PRO B 39 -1 O THR B 38 N SER B 16
SHEET 1 BE 3 ARG B 49 ILE B 51 0
SHEET 2 BE 3 VAL B 42 PHE B 44 -1 O ALA B 43 N LEU B 50
SHEET 3 BE 3 THR B 66 ILE B 67 -1 O ILE B 67 N VAL B 42
SHEET 1 BF 3 ARG B 93 GLU B 97 0
SHEET 2 BF 3 LYS B 100 TYR B 107 -1 O LYS B 100 N GLU B 97
SHEET 3 BF 3 GLU B 110 PHE B 114 -1 O GLU B 110 N TYR B 107
SHEET 1 BG 4 ILE B 218 ASP B 227 0
SHEET 2 BG 4 PHE B 207 GLU B 215 -1 O PHE B 207 N ASP B 227
SHEET 3 BG 4 LYS B 195 LEU B 202 -1 O LYS B 195 N ILE B 214
SHEET 4 BG 4 GLU B 335 VAL B 339 1 O GLU B 335 N LEU B 198
SHEET 1 BH 2 GLN B 281 TYR B 290 0
SHEET 2 BH 2 VAL B 293 THR B 300 -1 O VAL B 293 N LEU B 289
CISPEP 1 GLY A 4 PRO A 5 0 -3.31
CISPEP 2 GLY B 4 PRO B 5 0 -11.95
SITE 1 AC1 10 ASP B 152 ARG B 155 GLN B 156 LYS B 159
SITE 2 AC1 10 VAL B 169 LEU B 170 ARG B 171 ILE B 172
SITE 3 AC1 10 HOH B2533 HOH B2534
SITE 1 AC2 8 ASP A 152 ARG A 155 GLN A 156 LYS A 159
SITE 2 AC2 8 VAL A 169 ARG A 171 ILE A 172 HOH A2559
CRYST1 48.860 94.960 81.540 90.00 89.98 90.00 P 1 21 1 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 0.020467 0.000000 -0.000007 0.00000
SCALE2 0.000000 0.010531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012264 0.00000
MTRIX1 1 0.999990 0.001740 0.005150 24.18900 1
MTRIX2 1 0.001690 -0.999950 0.009590 -9.25700 1
MTRIX3 1 0.005170 -0.009580 -0.999940 40.72400 1
(ATOM LINES ARE NOT SHOWN.)
END
