| 6u3p-pdb | HEADER HYDROLASE 22-AUG-19 6U3P
TITLE BINARY COMPLEX OF NATIVE HACHE WITH OXIME REACTIVATOR LG-703
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 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: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS REACTIVATOR COMPLEX, BIS-OXIME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KOVALEVSKY,O.GERLITS,Z.RADIC
REVDAT 1 12-FEB-20 6U3P 0
JRNL AUTH L.GORECKI,O.GERLITS,X.KONG,X.CHENG,D.BLUMENTHAL,P.TAYLOR,
JRNL AUTH 2 C.BALLATORE,A.KOVALEVSKY,Z.RADIC
JRNL TITL RATIONAL DESIGN, SYNTHESIS AND EVALUATION OF UNCHARGED,
JRNL TITL 2 "SMART" BIS-OXIME ANTIDOTES OF ORGANOPHOSPHATE-INHIBITED
JRNL TITL 3 HUMAN ACETYLCHOLINESTERASE
JRNL REF J.BIOL.CHEM. 2020
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.2
REMARK 3 NUMBER OF REFLECTIONS : 38127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2030
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6U3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1000243859.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44284
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 6O5V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM POTASSIUM NITRATE, 100 MM HEPES
REMARK 280 PH 7.5, 10.5 % PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.27533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.55067
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -43.27533
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 -2
REMARK 465 PRO A -1
REMARK 465 LEU A 0
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 ASP A 544
REMARK 465 THR A 545
REMARK 465 LEU A 546
REMARK 465 ASP A 547
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 LEU B 0
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 ASP B 544
REMARK 465 THR B 545
REMARK 465 LEU B 546
REMARK 465 ASP B 547
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 GLN A 66 -166.01 -78.62
REMARK 500 PHE A 123 12.18 58.47
REMARK 500 PHE A 158 12.87 -143.42
REMARK 500 ALA A 167 79.51 -156.55
REMARK 500 SER A 196 57.84 -144.90
REMARK 500 SER A 203 -118.93 54.10
REMARK 500 ASP A 306 -66.83 -106.47
REMARK 500 TYR A 341 41.13 -92.69
REMARK 500 GLN A 369 73.32 53.43
REMARK 500 PRO A 446 -177.69 -65.40
REMARK 500 ASN A 464 53.29 -106.39
REMARK 500 GLN B 66 -158.39 -79.25
REMARK 500 PHE B 158 12.37 -144.18
REMARK 500 SER B 196 22.55 -152.13
REMARK 500 SER B 203 -120.83 53.50
REMARK 500 ASP B 306 -83.44 -106.57
REMARK 500 ALA B 318 35.27 -97.55
REMARK 500 ASN B 350 -164.48 -121.36
REMARK 500 VAL B 407 -63.34 -124.73
REMARK 500 PRO B 446 -179.57 -68.70
REMARK 500 TYR B 449 30.73 -99.07
REMARK 500 ARG B 493 41.45 -95.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PQY A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 601
DBREF 6U3P A 1 547 UNP P22303 ACES_HUMAN 32 578
DBREF 6U3P B 1 547 UNP P22303 ACES_HUMAN 32 578
SEQADV 6U3P GLY A -2 UNP P22303 EXPRESSION TAG
SEQADV 6U3P PRO A -1 UNP P22303 EXPRESSION TAG
SEQADV 6U3P LEU A 0 UNP P22303 EXPRESSION TAG
SEQADV 6U3P GLY B -2 UNP P22303 EXPRESSION TAG
SEQADV 6U3P PRO B -1 UNP P22303 EXPRESSION TAG
SEQADV 6U3P LEU B 0 UNP P22303 EXPRESSION TAG
SEQRES 1 A 550 GLY PRO LEU GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL
SEQRES 2 A 550 THR VAL ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS
SEQRES 3 A 550 THR PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO
SEQRES 4 A 550 PHE ALA GLU PRO PRO MET GLY PRO ARG ARG PHE LEU PRO
SEQRES 5 A 550 PRO GLU PRO LYS GLN PRO TRP SER GLY VAL VAL ASP ALA
SEQRES 6 A 550 THR THR PHE GLN SER VAL CYS TYR GLN TYR VAL ASP THR
SEQRES 7 A 550 LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO
SEQRES 8 A 550 ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL
SEQRES 9 A 550 TRP THR PRO TYR PRO ARG PRO THR SER PRO THR PRO VAL
SEQRES 10 A 550 LEU VAL TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA
SEQRES 11 A 550 SER SER LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN
SEQRES 12 A 550 ALA GLU ARG THR VAL LEU VAL SER MET ASN TYR ARG VAL
SEQRES 13 A 550 GLY ALA PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU
SEQRES 14 A 550 ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA
SEQRES 15 A 550 LEU GLN TRP VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY
SEQRES 16 A 550 ASP PRO THR SER VAL THR LEU PHE GLY GLU SER ALA GLY
SEQRES 17 A 550 ALA ALA SER VAL GLY MET HIS LEU LEU SER PRO PRO SER
SEQRES 18 A 550 ARG GLY LEU PHE HIS ARG ALA VAL LEU GLN SER GLY ALA
SEQRES 19 A 550 PRO ASN GLY PRO TRP ALA THR VAL GLY MET GLY GLU ALA
SEQRES 20 A 550 ARG ARG ARG ALA THR GLN LEU ALA HIS LEU VAL GLY CYS
SEQRES 21 A 550 PRO PRO GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL
SEQRES 22 A 550 ALA CYS LEU ARG THR ARG PRO ALA GLN VAL LEU VAL ASN
SEQRES 23 A 550 HIS GLU TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG
SEQRES 24 A 550 PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER
SEQRES 25 A 550 ASP THR PRO GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS
SEQRES 26 A 550 GLY LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY
SEQRES 27 A 550 SER TYR PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 28 A 550 ASP ASN GLU SER LEU ILE SER ARG ALA GLU PHE LEU ALA
SEQRES 29 A 550 GLY VAL ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA
SEQRES 30 A 550 ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS
SEQRES 31 A 550 PRO GLU ASP PRO ALA ARG LEU ARG GLU ALA LEU SER ASP
SEQRES 32 A 550 VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN
SEQRES 33 A 550 LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR
SEQRES 34 A 550 ALA TYR VAL PHE GLU HIS ARG ALA SER THR LEU SER TRP
SEQRES 35 A 550 PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU
SEQRES 36 A 550 PHE ILE PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR
SEQRES 37 A 550 THR ALA GLU GLU LYS ILE PHE ALA GLN ARG LEU MET ARG
SEQRES 38 A 550 TYR TRP ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU
SEQRES 39 A 550 PRO ARG ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR
SEQRES 40 A 550 ALA GLY ALA GLN GLN TYR VAL SER LEU ASP LEU ARG PRO
SEQRES 41 A 550 LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA
SEQRES 42 A 550 PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 43 A 550 ASP THR LEU ASP
SEQRES 1 B 550 GLY PRO LEU GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL
SEQRES 2 B 550 THR VAL ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS
SEQRES 3 B 550 THR PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO
SEQRES 4 B 550 PHE ALA GLU PRO PRO MET GLY PRO ARG ARG PHE LEU PRO
SEQRES 5 B 550 PRO GLU PRO LYS GLN PRO TRP SER GLY VAL VAL ASP ALA
SEQRES 6 B 550 THR THR PHE GLN SER VAL CYS TYR GLN TYR VAL ASP THR
SEQRES 7 B 550 LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO
SEQRES 8 B 550 ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL
SEQRES 9 B 550 TRP THR PRO TYR PRO ARG PRO THR SER PRO THR PRO VAL
SEQRES 10 B 550 LEU VAL TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA
SEQRES 11 B 550 SER SER LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN
SEQRES 12 B 550 ALA GLU ARG THR VAL LEU VAL SER MET ASN TYR ARG VAL
SEQRES 13 B 550 GLY ALA PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU
SEQRES 14 B 550 ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA
SEQRES 15 B 550 LEU GLN TRP VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY
SEQRES 16 B 550 ASP PRO THR SER VAL THR LEU PHE GLY GLU SER ALA GLY
SEQRES 17 B 550 ALA ALA SER VAL GLY MET HIS LEU LEU SER PRO PRO SER
SEQRES 18 B 550 ARG GLY LEU PHE HIS ARG ALA VAL LEU GLN SER GLY ALA
SEQRES 19 B 550 PRO ASN GLY PRO TRP ALA THR VAL GLY MET GLY GLU ALA
SEQRES 20 B 550 ARG ARG ARG ALA THR GLN LEU ALA HIS LEU VAL GLY CYS
SEQRES 21 B 550 PRO PRO GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL
SEQRES 22 B 550 ALA CYS LEU ARG THR ARG PRO ALA GLN VAL LEU VAL ASN
SEQRES 23 B 550 HIS GLU TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG
SEQRES 24 B 550 PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER
SEQRES 25 B 550 ASP THR PRO GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS
SEQRES 26 B 550 GLY LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY
SEQRES 27 B 550 SER TYR PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 28 B 550 ASP ASN GLU SER LEU ILE SER ARG ALA GLU PHE LEU ALA
SEQRES 29 B 550 GLY VAL ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA
SEQRES 30 B 550 ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS
SEQRES 31 B 550 PRO GLU ASP PRO ALA ARG LEU ARG GLU ALA LEU SER ASP
SEQRES 32 B 550 VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN
SEQRES 33 B 550 LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR
SEQRES 34 B 550 ALA TYR VAL PHE GLU HIS ARG ALA SER THR LEU SER TRP
SEQRES 35 B 550 PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU
SEQRES 36 B 550 PHE ILE PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR
SEQRES 37 B 550 THR ALA GLU GLU LYS ILE PHE ALA GLN ARG LEU MET ARG
SEQRES 38 B 550 TYR TRP ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU
SEQRES 39 B 550 PRO ARG ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR
SEQRES 40 B 550 ALA GLY ALA GLN GLN TYR VAL SER LEU ASP LEU ARG PRO
SEQRES 41 B 550 LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA
SEQRES 42 B 550 PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 43 B 550 ASP THR LEU ASP
HET PQY A 601 23
HET DMS B 601 4
HETNAM PQY (2E,2'E)-N,N'-[1,4-DIAZEPANE-1,4-DIYLDI(ETHANE-2,1-
HETNAM 2 PQY DIYL)]BIS[2-(HYDROXYIMINO)ACETAMIDE]
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 PQY C13 H24 N6 O4
FORMUL 4 DMS C2 H6 O S
FORMUL 5 HOH *70(H2 O)
HELIX 1 AA1 MET A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 GLU A 142 1 8
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 VAL A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 SER A 215 1 13
HELIX 9 AA9 SER A 215 GLY A 220 1 6
HELIX 10 AB1 GLY A 240 VAL A 255 1 16
HELIX 11 AB2 ASN A 265 ARG A 276 1 12
HELIX 12 AB3 PRO A 277 ASN A 283 1 7
HELIX 13 AB4 HIS A 284 LEU A 289 5 6
HELIX 14 AB5 THR A 311 ALA A 318 1 8
HELIX 15 AB6 TYR A 337 GLY A 342 5 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 TYR A 382 1 12
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 ALA A 420 1 14
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASP A 460 5 5
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 ALA A 542 1 9
HELIX 26 AC8 ASP B 5 GLU B 7 5 3
HELIX 27 AC9 MET B 42 ARG B 46 5 5
HELIX 28 AD1 PHE B 80 MET B 85 1 6
HELIX 29 AD2 LEU B 130 ASP B 134 5 5
HELIX 30 AD3 GLY B 135 ARG B 143 1 9
HELIX 31 AD4 GLY B 154 LEU B 159 1 6
HELIX 32 AD5 ASN B 170 VAL B 187 1 18
HELIX 33 AD6 ALA B 188 GLY B 191 5 4
HELIX 34 AD7 SER B 203 LEU B 214 1 12
HELIX 35 AD8 SER B 215 GLY B 220 1 6
HELIX 36 AD9 GLY B 240 GLY B 256 1 17
HELIX 37 AE1 ASN B 265 THR B 275 1 11
HELIX 38 AE2 PRO B 277 ASN B 283 1 7
HELIX 39 AE3 HIS B 284 LEU B 289 5 6
HELIX 40 AE4 THR B 311 ALA B 318 1 8
HELIX 41 AE5 TYR B 337 GLY B 342 5 6
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 TYR B 382 1 12
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 ALA B 420 1 14
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASP B 460 5 5
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 THR B 543 1 10
SHEET 1 AA1 3 LEU A 9 THR A 11 0
SHEET 2 AA1 3 ARG A 16 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 THR A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 AA211 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AA211 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 11 AA211 VAL A 520 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 3 LEU B 9 THR B 11 0
SHEET 2 AA3 3 ARG B 16 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA3 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA411 ILE B 20 THR B 24 0
SHEET 2 AA411 GLY B 27 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA411 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA411 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA411 VAL B 114 ILE B 118 1 N LEU B 115 O VAL B 145
SHEET 6 AA411 THR B 198 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 AA411 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA411 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA411 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 AA411 GLN B 509 LEU B 513 1 O VAL B 511 N VAL B 429
SHEET 11 AA411 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA5 2 VAL B 68 CYS B 69 0
SHEET 2 AA5 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.03
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.03
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
CISPEP 1 TYR A 105 PRO A 106 0 -0.62
CISPEP 2 CYS A 257 PRO A 258 0 0.29
CISPEP 3 GLY A 260 GLY A 261 0 -1.08
CISPEP 4 GLY A 263 GLY A 264 0 0.48
CISPEP 5 TYR B 105 PRO B 106 0 0.70
CISPEP 6 CYS B 257 PRO B 258 0 -1.07
SITE 1 AC1 8 TYR A 72 TYR A 124 GLU A 202 TRP A 286
SITE 2 AC1 8 TYR A 337 PHE A 338 TYR A 341 HOH A 712
SITE 1 AC2 2 GLU B 202 HIS B 447
CRYST1 125.407 125.407 129.826 90.00 90.00 120.00 P 31 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007974 0.004604 0.000000 0.00000
SCALE2 0.000000 0.009208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007703 0.00000
TER 4189 THR A 543
TER 8378 THR B 543
MASTER 273 0 2 51 30 0 3 6 8473 2 39 86
END
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