7rb6-pdb | HEADER HYDROLASE 05-JUL-21 7RB6
TITLE LOW TEMPERATURE STRUCTURE OF HACHE IN COMPLEX WITH SUBSTRATE ANALOG
TITLE 2 4K-TMA
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 ACETYLCHOLINE ESTERASE, SERINE HYDROLASE, TETRAHEDRAL INTERMEDIATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KOVALEVSKY,O.GERLITS,Z.RADIC
REVDAT 1 22-SEP-21 7RB6 0
JRNL AUTH O.GERLITS,M.P.BLAKELEY,D.A.KEEN,Z.RADIC,A.KOVALEVSKY
JRNL TITL ROOM TEMPERATURE CRYSTALLOGRAPHY OF HUMAN
JRNL TITL 2 ACETYLCHOLINESTERASE BOUND TO A SUBSTRATE ANALOGUE 4K-TMA:
JRNL TITL 3 TOWARDS A NEUTRON STRUCTURE
JRNL REF CURR RES STRUCT BIOL V. 3 206 2021
JRNL REFN ESSN 2665-928X
JRNL DOI 10.1016/J.CRSTBI.2021.08.003
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.17.1_3660: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 84333
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 4111
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 38.9800 - 5.1600 0.97 8222 381 0.1558 0.1709
REMARK 3 2 5.1600 - 4.1000 0.98 8320 445 0.1357 0.1591
REMARK 3 3 4.1000 - 3.5800 0.98 8277 410 0.1621 0.1889
REMARK 3 4 3.5800 - 3.2500 0.99 8462 339 0.1878 0.2171
REMARK 3 5 3.2500 - 3.0200 0.97 8204 440 0.1907 0.2316
REMARK 3 6 3.0200 - 2.8400 0.98 8242 457 0.2098 0.2570
REMARK 3 7 2.8400 - 2.7000 0.98 8318 495 0.2351 0.2792
REMARK 3 8 2.7000 - 2.5800 0.98 8264 428 0.2444 0.2850
REMARK 3 9 2.5800 - 2.4800 0.87 7356 390 0.2591 0.3093
REMARK 3 10 2.4800 - 2.4000 0.78 6557 326 0.2809 0.3493
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.660
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 8697
REMARK 3 ANGLE : 0.560 11885
REMARK 3 CHIRALITY : 0.043 1257
REMARK 3 PLANARITY : 0.005 1573
REMARK 3 DIHEDRAL : 10.534 1212
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 7RB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-21.
REMARK 100 THE DEPOSITION ID IS D_1000257979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-17
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) : 0.987
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 : 87262
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
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: PDB ENTRY 6O5R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.5, 10 MM SODIUM
REMARK 280 CITRATE, 6-8% PEG6000, 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 43.38967
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 86.77933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 43.38967
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 SER A 203 -116.98 51.43
REMARK 500 ASP A 306 -84.69 -101.23
REMARK 500 ALA A 318 31.23 -93.46
REMARK 500 VAL A 407 -63.09 -125.10
REMARK 500 ASN A 464 42.81 -100.90
REMARK 500 ARG A 493 -34.28 -130.83
REMARK 500 SER B 203 -119.27 52.28
REMARK 500 ASP B 306 -82.40 -97.19
REMARK 500 VAL B 407 -63.48 -124.58
REMARK 500 ASN B 464 45.97 -107.35
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 A 997 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 998 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A 999 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1000 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH B1013 DISTANCE = 5.85 ANGSTROMS
DBREF 7RB6 A 1 547 UNP P22303 ACES_HUMAN 32 578
DBREF 7RB6 B 1 547 UNP P22303 ACES_HUMAN 32 578
SEQADV 7RB6 GLY A -2 UNP P22303 EXPRESSION TAG
SEQADV 7RB6 PRO A -1 UNP P22303 EXPRESSION TAG
SEQADV 7RB6 LEU A 0 UNP P22303 EXPRESSION TAG
SEQADV 7RB6 GLY B -2 UNP P22303 EXPRESSION TAG
SEQADV 7RB6 PRO B -1 UNP P22303 EXPRESSION TAG
SEQADV 7RB6 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 NWA A 601 10
HET GOL A 602 6
HET GOL A 603 6
HET NO3 A 604 4
HET NWA B 601 10
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET NO3 B 605 4
HETNAM NWA 4,4-DIHYDROXY-N,N,N-TRIMETHYLPENTAN-1-AMINIUM
HETNAM GOL GLYCEROL
HETNAM NO3 NITRATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NWA 2(C8 H20 N O2 1+)
FORMUL 4 GOL 5(C3 H8 O3)
FORMUL 6 NO3 2(N O3 1-)
FORMUL 12 HOH *613(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 276 1 12
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 ALA A 318 1 8
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 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 GLU B 4 GLU B 7 5 4
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 276 1 12
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 ALA B 318 1 8
HELIX 42 AE6 GLY B 335 GLY B 342 5 8
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 GLY A 15 N VAL A 12
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 SER A 148 N ASN A 100
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 3 LEU B 9 VAL B 12 0
SHEET 2 AA3 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
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 LEU B 22 0
SHEET 2 AA411 VAL B 29 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 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 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 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.02
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.03
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK OG SER A 203 C5 NWA A 601 1555 1555 1.39
LINK OG SER B 203 C5 NWA B 601 1555 1555 1.40
CISPEP 1 TYR A 105 PRO A 106 0 -0.80
CISPEP 2 CYS A 257 PRO A 258 0 -2.98
CISPEP 3 GLY A 260 GLY A 261 0 -0.60
CISPEP 4 TYR B 105 PRO B 106 0 -1.77
CISPEP 5 CYS B 257 PRO B 258 0 -3.67
CRYST1 124.800 124.800 130.169 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 0.008013 0.004626 0.000000 0.00000
SCALE2 0.000000 0.009252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007682 0.00000
TER 4189 THR A 543
TER 8388 THR B 543
MASTER 273 0 9 52 28 0 0 6 9047 2 72 86
END
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