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HEADER HYDROLASE 14-DEC-21 7WAM
TITLE CRYSTAL STRUCTURE OF HALOTAG COMPLEXED WITH VL1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HALOTAG, HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PRATYUSH,M.KANG,H.LEE,C.LEE,H.RHEE
REVDAT 1 02-FEB-22 7WAM 0
JRNL AUTH P.K.MISHRA,M.G.KANG,H.LEE,S.KIM,S.CHOI,N.SHARMA,C.M.PARK,
JRNL AUTH 2 J.KO,C.LEE,J.K.SEO,H.W.RHEE
JRNL TITL A CHEMICAL TOOL FOR BLUE LIGHT-INDUCIBLE PROXIMITY
JRNL TITL 2 PHOTO-CROSSLINKING IN LIVE CELLS
JRNL REF CHEM SCI 2022
JRNL REFN ESSN 2041-6539
JRNL DOI 10.1039/D1SC04871F
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 54433
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.670
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 27.8020 - 3.5886 0.98 4023 154 0.1453 0.1724
REMARK 3 2 3.5886 - 2.8493 1.00 3876 148 0.1529 0.1714
REMARK 3 3 2.8493 - 2.4894 0.99 3820 145 0.1573 0.1930
REMARK 3 4 2.4894 - 2.2619 1.00 3789 144 0.1465 0.2000
REMARK 3 5 2.2619 - 2.0998 0.99 3767 144 0.1417 0.2078
REMARK 3 6 2.0998 - 1.9761 0.99 3735 142 0.1372 0.1719
REMARK 3 7 1.9761 - 1.8771 0.99 3744 144 0.1379 0.1849
REMARK 3 8 1.8771 - 1.7954 0.99 3693 140 0.1403 0.1681
REMARK 3 9 1.7954 - 1.7263 0.99 3720 142 0.1414 0.1984
REMARK 3 10 1.7263 - 1.6668 0.99 3680 141 0.1417 0.1953
REMARK 3 11 1.6668 - 1.6147 0.98 3653 139 0.1498 0.2007
REMARK 3 12 1.6147 - 1.5685 0.98 3644 139 0.1553 0.2093
REMARK 3 13 1.5685 - 1.5272 0.98 3687 140 0.1798 0.2576
REMARK 3 14 1.5272 - 1.4900 0.97 3602 138 0.2037 0.2818
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
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 : 0.013 2470
REMARK 3 ANGLE : 1.493 3374
REMARK 3 CHIRALITY : 0.062 354
REMARK 3 PLANARITY : 0.008 439
REMARK 3 DIHEDRAL : 13.192 901
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 7WAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-22.
REMARK 100 THE DEPOSITION ID IS D_1300025913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-16
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97960
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54493
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.79900
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: PHENIX
REMARK 200 STARTING MODEL: 5Y2X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 0.1 M CITRIC
REMARK 280 ACID PH 5.3, AND 1% MPD, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.05600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.53900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.53900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 123.08400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.53900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.53900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.02800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.53900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.53900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 123.08400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.53900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.53900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.02800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.05600
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11420 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 703 LIES ON A SPECIAL POSITION.
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 SER A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 106 C32 8MH A 301 1.40
REMARK 500 O HOH A 422 O HOH A 540 1.77
REMARK 500 O HOH A 656 O HOH A 714 2.07
REMARK 500 OE2 GLU A 191 O HOH A 401 2.12
REMARK 500 O HOH A 524 O HOH A 711 2.13
REMARK 500 NE ARG A 86 O HOH A 402 2.16
REMARK 500 O HOH A 750 O HOH A 754 2.18
REMARK 500 O HOH A 532 O HOH A 653 2.18
REMARK 500 NH2 ARG A 86 O HOH A 403 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 426 O HOH A 690 3544 1.91
REMARK 500 O HOH A 601 O HOH A 653 7645 2.11
REMARK 500 O HOH A 401 O HOH A 548 7645 2.13
REMARK 500 O HOH A 401 O HOH A 605 7645 2.14
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 PRO A 9 52.89 -91.90
REMARK 500 PRO A 42 45.90 -109.22
REMARK 500 THR A 43 -162.81 -100.09
REMARK 500 GLU A 98 -93.06 -108.16
REMARK 500 ASP A 106 -128.63 52.85
REMARK 500 ARG A 153 43.25 -89.33
REMARK 500 VAL A 245 -67.46 -132.55
REMARK 500 LEU A 271 -99.79 -118.38
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 753 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 754 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 755 DISTANCE = 6.39 ANGSTROMS
DBREF 7WAM A 2 293 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 7WAM SER A -1 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM GLY A 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM SER A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM ALA A 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 7WAM VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7WAM THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7WAM GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7WAM PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7WAM MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7WAM PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7WAM THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7WAM LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7WAM VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7WAM THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7WAM CYS A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7WAM GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7WAM ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7WAM GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7WAM ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7WAM LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7WAM ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7WAM ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7WAM LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7WAM SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7WAM THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7WAM GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7WAM GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 299 SER GLY SER ALA GLU ILE GLY THR GLY PHE PRO PHE ASP
SEQRES 2 A 299 PRO HIS TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR
SEQRES 3 A 299 VAL ASP VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE
SEQRES 4 A 299 LEU HIS GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN
SEQRES 5 A 299 ILE ILE PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA
SEQRES 6 A 299 PRO ASP LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP
SEQRES 7 A 299 LEU GLY TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP
SEQRES 8 A 299 ALA PHE ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU
SEQRES 9 A 299 VAL ILE HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP
SEQRES 10 A 299 ALA LYS ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE
SEQRES 11 A 299 MET GLU PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP
SEQRES 12 A 299 PRO GLU PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR
SEQRES 13 A 299 THR ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL
SEQRES 14 A 299 PHE ILE GLU GLY THR LEU PRO CYS GLY VAL VAL ARG PRO
SEQRES 15 A 299 LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE
SEQRES 16 A 299 LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO
SEQRES 17 A 299 ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL
SEQRES 18 A 299 ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER
SEQRES 19 A 299 PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL
SEQRES 20 A 299 LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER
SEQRES 21 A 299 LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU
SEQRES 22 A 299 ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER
SEQRES 23 A 299 GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY
HET 8MH A 301 35
HET CL A 302 1
HETNAM 8MH 3-[6-(2-AZANYLHYDRAZINYL)-1,3-BIS(OXIDANYLIDENE)
HETNAM 2 8MH BENZO[DE]ISOQUINOLIN-2-YL]-N-[2-(2-HEXOXYETHOXY)
HETNAM 3 8MH ETHYL]PROPANAMIDE
HETNAM CL CHLORIDE ION
FORMUL 2 8MH C25 H35 N5 O5
FORMUL 3 CL CL 1-
FORMUL 4 HOH *355(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 THR A 155 ILE A 163 1 9
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 LEU A 173 VAL A 177 5 5
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 LEU A 293 1 16
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
CISPEP 1 ASN A 41 PRO A 42 0 3.49
CISPEP 2 GLU A 214 PRO A 215 0 -10.01
CISPEP 3 THR A 242 PRO A 243 0 5.58
CRYST1 63.078 63.078 164.112 90.00 90.00 90.00 P 43 21 2 8
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 0.015853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006093 0.00000
TER 2354 GLY A 297
MASTER 322 0 2 17 8 0 0 6 2744 1 35 23
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