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HEADER HYDROLASE 04-MAR-19 6O5S
TITLE ROOM TEMPERATURE STRUCTURE OF VX-PHOSPHONYLATED HACHE IN COMPLEX WITH
TITLE 2 OXIME REACTIVATOR RS-170B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 33-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
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: 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 VX-PHOSPHONYLATED, VX-HACHE, OXIME REACTIVATOR, IMIDAZOLE-BASED
KEYWDS 2 OXIME, RS-170B, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.GERLITS,A.KOVALEVSKY,Z.RADIC
REVDAT 1 29-MAY-19 6O5S 0
JRNL AUTH O.GERLITS,X.KONG,X.CHENG,T.WYMORE,D.K.BLUMENTHAL,P.TAYLOR,
JRNL AUTH 2 Z.RADIC,A.KOVALEVSKY
JRNL TITL PRODUCTIVE REORIENTATION OF BOUND OXIME REACTIVATOR REVEALED
JRNL TITL 2 IN ROOM-TEMPERATURE X-RAY STRUCTURES OF NATIVE AND
JRNL TITL 3 VX-INHIBITED HUMAN ACETYLCHOLINESTERASE
JRNL REF J.BIOL.CHEM. 2019
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11_2567)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 52095
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2584
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 39.2138 - 7.3244 0.96 2897 127 0.1237 0.1738
REMARK 3 2 7.3244 - 5.8197 0.94 2827 129 0.1521 0.1961
REMARK 3 3 5.8197 - 5.0858 0.99 2955 148 0.1465 0.1814
REMARK 3 4 5.0858 - 4.6216 0.95 2828 147 0.1337 0.1525
REMARK 3 5 4.6216 - 4.2908 0.96 2881 143 0.1298 0.1436
REMARK 3 6 4.2908 - 4.0381 0.98 2958 140 0.1363 0.1360
REMARK 3 7 4.0381 - 3.8360 0.98 2902 198 0.1465 0.1523
REMARK 3 8 3.8360 - 3.6692 0.99 3008 128 0.1641 0.1734
REMARK 3 9 3.6692 - 3.5280 0.93 2774 152 0.1808 0.2005
REMARK 3 10 3.5280 - 3.4064 0.96 2848 168 0.1832 0.2037
REMARK 3 11 3.4064 - 3.2999 0.97 2875 140 0.2063 0.2319
REMARK 3 12 3.2999 - 3.2056 0.97 2972 141 0.2152 0.2734
REMARK 3 13 3.2056 - 3.1213 0.97 2911 141 0.2401 0.2337
REMARK 3 14 3.1213 - 3.0451 0.97 2929 167 0.2602 0.3200
REMARK 3 15 3.0451 - 2.9759 0.96 2899 117 0.2745 0.2848
REMARK 3 16 2.9759 - 2.9126 0.89 2630 172 0.2829 0.3264
REMARK 3 17 2.9126 - 2.8544 0.66 1964 124 0.2961 0.3513
REMARK 3 18 2.8544 - 2.8005 0.49 1453 102 0.3262 0.3716
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.810
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 : 0.002 8729
REMARK 3 ANGLE : 0.472 11939
REMARK 3 CHIRALITY : 0.042 1258
REMARK 3 PLANARITY : 0.005 1582
REMARK 3 DIHEDRAL : 13.091 5109
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 6O5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7
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) : 0.92
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 : 52095
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 : 2.700
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.73900
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM SODIUM CITRATE, 100 MM HEPES, PH
REMARK 280 7, AND 6-8 % PEG6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 43.62033
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 87.24067
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: 3460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 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 350 APPLY THE FOLLOWING TO CHAINS: B
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 -43.62033
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 PHE A 47 -0.97 71.91
REMARK 500 ALA A 62 53.06 -119.77
REMARK 500 PHE A 123 12.89 59.71
REMARK 500 PHE A 158 11.35 -144.57
REMARK 500 ALA A 167 73.98 -150.45
REMARK 500 ASN A 186 -10.43 -141.00
REMARK 500 SER A 203 -118.59 52.97
REMARK 500 ASP A 306 -74.95 -101.05
REMARK 500 ALA A 318 56.30 -106.96
REMARK 500 VAL A 407 -61.45 -124.49
REMARK 500 ASN A 464 54.41 -90.51
REMARK 500 PHE B 47 -1.99 75.08
REMARK 500 ALA B 62 52.13 -116.34
REMARK 500 PHE B 123 13.98 59.61
REMARK 500 PHE B 158 12.47 -143.94
REMARK 500 ASN B 170 19.77 59.38
REMARK 500 PRO B 194 0.26 -68.10
REMARK 500 SER B 203 -119.93 59.24
REMARK 500 ASP B 306 -76.37 -100.00
REMARK 500 ALA B 318 37.71 -98.91
REMARK 500 ASP B 333 79.23 -108.71
REMARK 500 VAL B 407 -64.28 -120.60
REMARK 500 ASN B 464 44.64 -99.03
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 VX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LND A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LND B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6O5R RELATED DB: PDB
DBREF 6O5S A 1 547 UNP P22303 ACES_HUMAN 32 578
DBREF 6O5S B 1 547 UNP P22303 ACES_HUMAN 32 578
SEQADV 6O5S GLY A -2 UNP P22303 EXPRESSION TAG
SEQADV 6O5S PRO A -1 UNP P22303 EXPRESSION TAG
SEQADV 6O5S LEU A 0 UNP P22303 EXPRESSION TAG
SEQADV 6O5S GLY B -2 UNP P22303 EXPRESSION TAG
SEQADV 6O5S PRO B -1 UNP P22303 EXPRESSION TAG
SEQADV 6O5S 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 VX A 601 6
HET LND A 602 20
HET VX A 603 7
HET VX B 601 6
HET LND B 602 20
HET VX B 603 7
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM LND 4-CARBAMOYL-1-(3-{2-[(E)-(HYDROXYIMINO)METHYL]-1H-
HETNAM 2 LND IMIDAZOL-1-YL}PROPYL)PYRIDIN-1-IUM
FORMUL 3 VX 4(C3 H9 O3 P)
FORMUL 4 LND 2(C13 H16 N5 O2 1+)
FORMUL 9 HOH *166(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 GLY A 154 LEU A 159 1 6
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASN A 265 ARG A 274 1 10
HELIX 13 AB4 PRO A 277 HIS A 284 1 8
HELIX 14 AB5 GLU A 285 LEU A 289 5 5
HELIX 15 AB6 THR A 311 ALA A 318 1 8
HELIX 16 AB7 SER A 336 GLY A 342 5 7
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 TYR A 382 1 12
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 ALA A 420 1 14
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 ALA A 542 1 9
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 GLY B 154 LEU B 159 1 6
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 GLY B 240 VAL B 255 1 16
HELIX 38 AE2 ASN B 265 ARG B 274 1 10
HELIX 39 AE3 PRO B 277 HIS B 284 1 8
HELIX 40 AE4 GLU B 285 LEU B 289 5 5
HELIX 41 AE5 THR B 311 ALA B 318 1 8
HELIX 42 AE6 SER B 336 GLY B 342 5 7
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 ALA B 420 1 14
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 ALA B 542 1 9
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 LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
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 ARG A 224 N LEU A 199
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N ALA A 225
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 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 VAL B 101 N PHE B 32
SHEET 4 AA411 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA411 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 145
SHEET 6 AA411 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA411 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
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 PHE B 430 N VAL B 330
SHEET 10 AA411 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA411 VAL B 520 ARG B 522 -1 O ARG B 521 N TYR B 510
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
LINK OG SER A 203 P1 VX A 601 1555 1555 1.62
LINK OG SER B 203 P1 VX B 601 1555 1555 1.62
CISPEP 1 TYR A 105 PRO A 106 0 1.44
CISPEP 2 CYS A 257 PRO A 258 0 -2.33
CISPEP 3 GLY A 260 GLY A 261 0 0.30
CISPEP 4 TYR B 105 PRO B 106 0 3.08
CISPEP 5 CYS B 257 PRO B 258 0 -2.18
SITE 1 AC1 9 GLY A 121 GLY A 122 SER A 203 ALA A 204
SITE 2 AC1 9 TRP A 236 PHE A 295 HIS A 447 LND A 602
SITE 3 AC1 9 VX A 603
SITE 1 AC2 10 TYR A 72 TYR A 124 TRP A 286 VAL A 294
SITE 2 AC2 10 PHE A 295 TYR A 337 PHE A 338 TYR A 341
SITE 3 AC2 10 VX A 601 VX A 603
SITE 1 AC3 8 TRP A 86 GLY A 120 GLU A 202 SER A 203
SITE 2 AC3 8 TYR A 337 HIS A 447 VX A 601 LND A 602
SITE 1 AC4 11 TYR B 72 TYR B 124 TRP B 286 VAL B 294
SITE 2 AC4 11 PHE B 295 TYR B 337 PHE B 338 TYR B 341
SITE 3 AC4 11 VX B 601 VX B 603 HOH B 732
SITE 1 AC5 9 TRP B 86 GLY B 120 GLY B 121 GLU B 202
SITE 2 AC5 9 TYR B 337 HIS B 447 GLY B 448 VX B 601
SITE 3 AC5 9 LND B 602
CRYST1 125.557 125.557 130.861 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 0.007965 0.004598 0.000000 0.00000
SCALE2 0.000000 0.009197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007642 0.00000
TER 4199 THR A 543
TER 8398 THR B 543
MASTER 307 0 6 52 28 0 14 6 8608 2 80 86
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