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HEADER HYDROLASE 04-MAR-19 6O5V
TITLE BINARY COMPLEX OF NATIVE HACHE WITH OXIME REACTIVATOR RS-170B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 32-578;
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 OXIME REACTIVATOR, IMIDAZOLE-BASED OXIME, RS-170B, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.GERLITS,A.KOVALEVSKY,Z.RADIC
REVDAT 1 29-MAY-19 6O5V 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. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 107187
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5358
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 27.6412 - 6.6570 0.73 2839 123 0.1556 0.1586
REMARK 3 2 6.6570 - 5.2961 0.84 3247 174 0.1597 0.1960
REMARK 3 3 5.2961 - 4.6302 0.86 3331 167 0.1393 0.1694
REMARK 3 4 4.6302 - 4.2084 0.89 3427 175 0.1352 0.1438
REMARK 3 5 4.2084 - 3.9077 0.91 3535 185 0.1462 0.1791
REMARK 3 6 3.9077 - 3.6778 0.92 3565 185 0.1557 0.1880
REMARK 3 7 3.6778 - 3.4940 0.93 3585 185 0.1733 0.2089
REMARK 3 8 3.4940 - 3.3422 0.95 3628 210 0.1829 0.2337
REMARK 3 9 3.3422 - 3.2137 0.94 3661 185 0.1929 0.2197
REMARK 3 10 3.2137 - 3.1030 0.95 3640 205 0.1938 0.2449
REMARK 3 11 3.1030 - 3.0061 0.96 3765 203 0.1938 0.2565
REMARK 3 12 3.0061 - 2.9202 0.96 3723 175 0.2011 0.2223
REMARK 3 13 2.9202 - 2.8435 0.96 3694 204 0.1973 0.2354
REMARK 3 14 2.8435 - 2.7741 0.96 3714 172 0.2116 0.2655
REMARK 3 15 2.7741 - 2.7111 0.97 3756 201 0.2247 0.2713
REMARK 3 16 2.7111 - 2.6535 0.97 3709 206 0.2276 0.2963
REMARK 3 17 2.6535 - 2.6004 0.96 3687 190 0.2377 0.2765
REMARK 3 18 2.6004 - 2.5514 0.97 3773 195 0.2322 0.2584
REMARK 3 19 2.5514 - 2.5059 0.96 3692 200 0.2287 0.2719
REMARK 3 20 2.5059 - 2.4634 0.96 3714 183 0.2390 0.2581
REMARK 3 21 2.4634 - 2.4237 0.95 3640 205 0.2410 0.2935
REMARK 3 22 2.4237 - 2.3864 0.95 3726 174 0.2640 0.2985
REMARK 3 23 2.3864 - 2.3514 0.93 3607 188 0.2680 0.2900
REMARK 3 24 2.3514 - 2.3183 0.91 3482 206 0.2703 0.3133
REMARK 3 25 2.3183 - 2.2869 0.87 3316 186 0.2707 0.2716
REMARK 3 26 2.2869 - 2.2573 0.81 3142 165 0.2728 0.2999
REMARK 3 27 2.2573 - 2.2291 0.75 2858 164 0.2735 0.3131
REMARK 3 28 2.2291 - 2.2022 0.65 2499 152 0.2824 0.3210
REMARK 3 29 2.2022 - 2.1766 0.56 2141 110 0.2822 0.2763
REMARK 3 30 2.1766 - 2.1522 0.45 1733 85 0.2740 0.3028
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.800
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 : 0.008 8782
REMARK 3 ANGLE : 0.956 12001
REMARK 3 CHIRALITY : 0.054 1261
REMARK 3 PLANARITY : 0.007 1593
REMARK 3 DIHEDRAL : 15.541 5153
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 6O5V 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_1000240073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.97
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 : 107187
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 93.6
REMARK 200 DATA REDUNDANCY : 1.400
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
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 (%): 74.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.90
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 43.26800
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 86.53600
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: 3410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 124.44200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 43.26800
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 -1.55 80.88
REMARK 500 ALA A 167 78.87 -152.92
REMARK 500 SER A 203 -117.94 51.91
REMARK 500 ASP A 306 -84.85 -104.52
REMARK 500 HIS A 387 55.64 -141.54
REMARK 500 VAL A 407 -59.73 -127.03
REMARK 500 ASP A 494 108.87 -50.10
REMARK 500 SER B 203 -116.02 53.87
REMARK 500 ASP B 306 -87.09 -96.53
REMARK 500 VAL B 407 -59.15 -125.90
REMARK 500 ALA B 542 20.30 -78.81
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 A1162 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A1163 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B1158 DISTANCE = 5.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LND A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LND B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6O5R RELATED DB: PDB
REMARK 900 RELATED ID: 6O5S RELATED DB: PDB
DBREF 6O5V A 1 547 UNP P22303 ACES_HUMAN 32 578
DBREF 6O5V B 1 547 UNP P22303 ACES_HUMAN 32 578
SEQADV 6O5V GLY A -2 UNP P22303 EXPRESSION TAG
SEQADV 6O5V PRO A -1 UNP P22303 EXPRESSION TAG
SEQADV 6O5V LEU A 0 UNP P22303 EXPRESSION TAG
SEQADV 6O5V GLY B -2 UNP P22303 EXPRESSION TAG
SEQADV 6O5V PRO B -1 UNP P22303 EXPRESSION TAG
SEQADV 6O5V 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 LND A 601 40
HET NO3 A 602 4
HET NO3 A 603 4
HET GOL A 604 6
HET GOL A 605 6
HET LND B 601 40
HET GOL B 602 6
HET GOL B 603 6
HETNAM LND 4-CARBAMOYL-1-(3-{2-[(E)-(HYDROXYIMINO)METHYL]-1H-
HETNAM 2 LND IMIDAZOL-1-YL}PROPYL)PYRIDIN-1-IUM
HETNAM NO3 NITRATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 LND 2(C13 H16 N5 O2 1+)
FORMUL 4 NO3 2(N O3 1-)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 11 HOH *921(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 VAL A 153 LEU A 159 1 7
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 MET A 241 VAL A 255 1 15
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 LEU A 289 5 6
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
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 VAL B 153 LEU B 159 1 7
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 MET B 241 VAL B 255 1 15
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 LEU B 289 5 6
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
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 GLN B 421 1 15
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 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 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 LEU A 22 0
SHEET 2 AA211 VAL A 29 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 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 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 2 VAL A 239 GLY A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA611 ILE B 20 LEU B 22 0
SHEET 2 AA611 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA611 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA611 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 145
SHEET 6 AA611 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA611 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA7 2 VAL B 68 CYS B 69 0
SHEET 2 AA7 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA8 2 VAL B 239 GLY B 240 0
SHEET 2 AA8 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.08
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.09
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.07
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
CISPEP 1 TYR A 105 PRO A 106 0 -5.44
CISPEP 2 CYS A 257 PRO A 258 0 0.21
CISPEP 3 GLY A 260 GLY A 261 0 -5.70
CISPEP 4 TYR B 105 PRO B 106 0 -3.37
CISPEP 5 CYS B 257 PRO B 258 0 -2.73
SITE 1 AC1 11 TYR A 72 TYR A 124 TRP A 286 VAL A 294
SITE 2 AC1 11 PHE A 295 PHE A 297 PHE A 338 TYR A 341
SITE 3 AC1 11 GOL A 604 HOH A 718 HOH A 741
SITE 1 AC2 3 ASP A 333 TRP A 442 HOH A 784
SITE 1 AC3 4 GLY A 43 PRO A 44 ARG A 274 HOH A 887
SITE 1 AC4 4 GLU A 202 LND A 601 HOH A 718 HOH A 803
SITE 1 AC5 8 GLU A 81 MET A 85 THR A 436 LEU A 437
SITE 2 AC5 8 SER A 438 TYR A 449 GLU A 452 HOH A1011
SITE 1 AC6 11 TYR B 72 TYR B 124 TRP B 286 VAL B 294
SITE 2 AC6 11 PHE B 295 PHE B 297 TYR B 337 PHE B 338
SITE 3 AC6 11 TYR B 341 GOL B 602 HOH B 710
SITE 1 AC7 5 GLU B 202 TYR B 337 LND B 601 HOH B 744
SITE 2 AC7 5 HOH B 893
SITE 1 AC8 8 GLU B 81 MET B 85 ALA B 434 THR B 436
SITE 2 AC8 8 LEU B 437 SER B 438 TYR B 449 GLU B 452
CRYST1 124.442 124.442 129.804 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 0.008036 0.004640 0.000000 0.00000
SCALE2 0.000000 0.009279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007704 0.00000
TER 4194 THR A 543
TER 8405 THR B 543
MASTER 335 0 8 52 36 0 15 6 9369 2 124 86
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