| 6u34-pdb | HEADER HYDROLASE 21-AUG-19 6U34
TITLE BINARY COMPLEX OF NATIVE HACHE WITH OXIME REACTIVATOR RS194B
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 OXIME REACTIVATOR, BINARY COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KOVALEVSKY,O.GERLITS,Z.RADIC
REVDAT 1 12-FEB-20 6U34 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.8
REMARK 3 NUMBER OF REFLECTIONS : 76164
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3795
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 6U34 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_1000243831.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
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) : 0.9795
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 : 82527
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 94.1
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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 (%): 75.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20 MM SODIUM CITRATE, 100 MM HEPES,
REMARK 280 PH 7, 8-8.5 % PEG6000 AND 100 MM POTASSIUM NITRATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, 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 43.28133
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 86.56267
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: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 187.46100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 108.23066
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 43.28133
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO B 40 C PRO B 41 N 0.115
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 ALA A 62 52.96 -116.83
REMARK 500 PHE A 158 10.97 -142.16
REMARK 500 SER A 203 -117.31 51.17
REMARK 500 ASP A 306 -82.05 -96.25
REMARK 500 VAL A 367 79.76 -117.79
REMARK 500 VAL A 407 -63.32 -124.71
REMARK 500 ASN A 464 52.38 -105.94
REMARK 500 PHE B 158 12.16 -142.30
REMARK 500 SER B 203 -117.68 54.97
REMARK 500 ASP B 306 -84.69 -104.91
REMARK 500 VAL B 407 -63.80 -124.98
REMARK 500 ASN B 464 51.74 -99.45
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 GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PQV A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PQV B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 605
DBREF 6U34 A 4 547 UNP P22303 ACES_HUMAN 35 578
DBREF 6U34 B 4 547 UNP P22303 ACES_HUMAN 35 578
SEQADV 6U34 GLY A -2 UNP P22303 EXPRESSION TAG
SEQADV 6U34 PRO A -1 UNP P22303 EXPRESSION TAG
SEQADV 6U34 LEU A 0 UNP P22303 EXPRESSION TAG
SEQADV 6U34 GLU A 1 UNP P22303 EXPRESSION TAG
SEQADV 6U34 GLY A 2 UNP P22303 EXPRESSION TAG
SEQADV 6U34 ARG A 3 UNP P22303 EXPRESSION TAG
SEQADV 6U34 GLY B -2 UNP P22303 EXPRESSION TAG
SEQADV 6U34 PRO B -1 UNP P22303 EXPRESSION TAG
SEQADV 6U34 LEU B 0 UNP P22303 EXPRESSION TAG
SEQADV 6U34 GLU B 1 UNP P22303 EXPRESSION TAG
SEQADV 6U34 GLY B 2 UNP P22303 EXPRESSION TAG
SEQADV 6U34 ARG B 3 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 GOL A 601 6
HET GOL A 602 6
HET PQV A 603 15
HET NO3 A 604 4
HET GOL B 601 6
HET GOL B 602 6
HET GOL B 603 6
HET PQV B 604 15
HET NO3 B 605 4
HETNAM GOL GLYCEROL
HETNAM PQV (2E)-N-[2-(AZEPAN-1-YL)ETHYL]-2-(HYDROXYIMINO)ACETAMIDE
HETNAM NO3 NITRATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 5(C3 H8 O3)
FORMUL 5 PQV 2(C10 H19 N3 O2)
FORMUL 6 NO3 2(N O3 1-)
FORMUL 12 HOH *242(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 THR A 275 1 11
HELIX 13 AB4 PRO A 277 ASN A 283 1 7
HELIX 14 AB5 HIS A 284 VAL A 288 5 5
HELIX 15 AB6 THR A 311 ALA A 318 1 8
HELIX 16 AB7 GLY A 335 GLY A 342 5 8
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 THR B 275 1 11
HELIX 39 AE3 PRO B 277 ASN B 283 1 7
HELIX 40 AE4 HIS B 284 VAL B 288 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 THR A 24 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ALA A 62 1 O ALA A 62 N ARG A 18
SHEET 1 AA212 LEU A 9 THR A 11 0
SHEET 2 AA212 ARG A 16 THR A 24 -1 O LEU A 17 N VAL A 10
SHEET 3 AA212 GLY A 27 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 4 AA212 TYR A 98 THR A 103 -1 O THR A 103 N SER A 30
SHEET 5 AA212 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 6 AA212 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 7 AA212 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 8 AA212 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 9 AA212 LEU A 324 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 10 AA212 ALA A 423 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 11 AA212 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 12 AA212 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 VAL B 29 N LEU B 22
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 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 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 ARG B 424 N VAL B 326
SHEET 10 AA411 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA411 GLU B 519 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 2.04
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 2.04
CISPEP 1 TYR A 105 PRO A 106 0 -0.47
CISPEP 2 CYS A 257 PRO A 258 0 -2.21
CISPEP 3 GLY A 260 GLY A 261 0 0.60
CISPEP 4 TYR B 105 PRO B 106 0 1.30
CISPEP 5 CYS B 257 PRO B 258 0 -2.47
SITE 1 AC1 9 GLU A 81 MET A 85 THR A 436 LEU A 437
SITE 2 AC1 9 SER A 438 TYR A 449 GLU A 452 TYR A 465
SITE 3 AC1 9 HOH A 779
SITE 1 AC2 3 TYR A 72 TRP A 286 HOH A 770
SITE 1 AC3 9 TRP A 86 GLY A 121 TYR A 124 GLU A 202
SITE 2 AC3 9 TYR A 337 PHE A 338 HIS A 447 HOH A 701
SITE 3 AC3 9 HOH A 707
SITE 1 AC4 2 ASP A 333 GLU A 396
SITE 1 AC5 8 GLU B 81 MET B 85 THR B 436 LEU B 437
SITE 2 AC5 8 SER B 438 TYR B 449 GLU B 452 TYR B 465
SITE 1 AC6 4 LEU B 178 GLN B 181 TRP B 182 GLU B 185
SITE 1 AC7 2 TYR B 72 TRP B 286
SITE 1 AC8 9 TRP B 86 GLY B 121 TYR B 124 GLU B 202
SITE 2 AC8 9 TYR B 337 PHE B 338 HIS B 447 HOH B 702
SITE 3 AC8 9 HOH B 710
SITE 1 AC9 2 ASP B 333 GLU B 396
CRYST1 124.974 124.974 129.844 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 0.008002 0.004620 0.000000 0.00000
SCALE2 0.000000 0.009240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007702 0.00000
TER 4189 THR A 543
TER 8378 THR B 543
MASTER 310 0 9 52 29 0 16 6 8686 2 80 86
END
|
|---|
