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HEADER HYDROLASE 09-SEP-16 5LUK
TITLE STRUCTURE OF A DOUBLE VARIANT OF CUTINASE 2 FROM THERMOBIFIDA
TITLE 2 CELLULOSILYTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA CELLULOSILYTICA;
SOURCE 3 ORGANISM_TAXID: 144786;
SOURCE 4 GENE: CUT2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: GOLD
KEYWDS CUTINASE, ALPHA/BETA HYDROLASE, POLY(ETHYLENETEREPHTHLATE) (PET),
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HROMIC,A.LYSKOWSKI,K.GRUBER
REVDAT 1 12-JUL-17 5LUK 0
JRNL AUTH D.RIBITSCH,A.HROMIC,S.ZITZENBACHER,B.ZARTL,C.GAMERITH,
JRNL AUTH 2 A.PELLIS,A.JUNGBAUER,A.YSKOWSKI,G.STEINKELLNER,K.GRUBER,
JRNL AUTH 3 R.TSCHELIESSNIG,E.H.ACERO,G.M.GUEBITZ
JRNL TITL SMALL CAUSE, LARGE EFFECT: STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 CUTINASES FROM THERMOBIFIDA CELLULOSILYTICA.
JRNL REF BIOTECHNOL. BIOENG. 2017
JRNL REFN ESSN 1097-0290
JRNL PMID 28671263
JRNL DOI 10.1002/BIT.26372
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4-1496
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 38429
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 1888
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 37.8989 - 3.4049 0.99 3053 152 0.1467 0.1625
REMARK 3 2 3.4049 - 2.7028 1.00 2955 146 0.1488 0.1311
REMARK 3 3 2.7028 - 2.3612 1.00 2927 145 0.1490 0.1794
REMARK 3 4 2.3612 - 2.1453 1.00 2880 140 0.1408 0.1698
REMARK 3 5 2.1453 - 1.9916 1.00 2875 161 0.1373 0.1568
REMARK 3 6 1.9916 - 1.8741 1.00 2837 158 0.1415 0.1809
REMARK 3 7 1.8741 - 1.7803 1.00 2870 151 0.1379 0.1748
REMARK 3 8 1.7803 - 1.7028 1.00 2839 138 0.1421 0.1795
REMARK 3 9 1.7028 - 1.6372 1.00 2857 152 0.1398 0.1635
REMARK 3 10 1.6372 - 1.5807 1.00 2821 152 0.1404 0.1706
REMARK 3 11 1.5807 - 1.5313 0.97 2788 125 0.1434 0.1728
REMARK 3 12 1.5313 - 1.4875 0.90 2542 143 0.1460 0.1633
REMARK 3 13 1.4875 - 1.4484 0.82 2297 125 0.1545 0.1737
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.740
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 : 0.006 2118
REMARK 3 ANGLE : 0.943 2897
REMARK 3 CHIRALITY : 0.084 316
REMARK 3 PLANARITY : 0.007 385
REMARK 3 DIHEDRAL : 14.171 787
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 5LUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-13
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 : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38429
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 37.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.22600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1JFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M SODIUM MALONATE PH 7.0, 0.1 M
REMARK 280 HEPES PH 7.0, AND 0.5% V/V JEFFAMINE ED-2001 PH 7.0, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 20.29750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.73850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.25600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.73850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.29750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.25600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 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 MET A 1
REMARK 465 GLU A 265
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 OE2 GLU A 27 O HOH A 401 2.18
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 435 O HOH A 441 1455 2.07
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 SER A 131 -120.69 63.13
REMARK 500 THR A 154 58.84 33.26
REMARK 500 HIS A 185 -84.15 -124.06
REMARK 500 GLU A 252 -76.91 -127.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 25 O
REMARK 620 2 HOH A 534 O 94.2
REMARK 620 3 HOH A 404 O 98.7 105.8
REMARK 620 4 HOH A 507 O 83.5 162.6 91.5
REMARK 620 5 ASP A 111 O 30.2 120.6 77.7 62.9
REMARK 620 6 ALA A 112 O 22.9 115.6 84.7 65.7 7.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 305 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 32 O
REMARK 620 2 ALA A 35 O 94.4
REMARK 620 3 PHE A 38 O 105.4 84.0
REMARK 620 4 HOH A 518 O 173.2 89.2 80.7
REMARK 620 5 HOH A 530 O 105.1 157.9 80.9 72.6
REMARK 620 6 HOH A 580 O 92.4 87.8 160.9 81.9 101.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 305
DBREF 5LUK A 1 262 UNP E9LVH9 E9LVH9_9ACTN 1 262
SEQADV 5LUK ASN A 29 UNP E9LVH9 ARG 29 ENGINEERED MUTATION
SEQADV 5LUK VAL A 30 UNP E9LVH9 ALA 30 ENGINEERED MUTATION
SEQADV 5LUK ALA A 263 UNP E9LVH9 EXPRESSION TAG
SEQADV 5LUK LEU A 264 UNP E9LVH9 EXPRESSION TAG
SEQADV 5LUK GLU A 265 UNP E9LVH9 EXPRESSION TAG
SEQRES 1 A 265 MET ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP
SEQRES 2 A 265 ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER
SEQRES 3 A 265 GLU GLU ASN VAL SER ARG PHE GLY ALA ASP GLY PHE GLY
SEQRES 4 A 265 GLY GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR
SEQRES 5 A 265 GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLN
SEQRES 6 A 265 ALA SER VAL ALA TRP LEU GLY GLU ARG ILE ALA SER HIS
SEQRES 7 A 265 GLY PHE VAL VAL ILE THR ILE ASP THR ASN THR THR LEU
SEQRES 8 A 265 ASP GLN PRO ASP SER ARG ALA ARG GLN LEU ASN ALA ALA
SEQRES 9 A 265 LEU ASP TYR MET ILE ASN ASP ALA SER SER ALA VAL ARG
SEQRES 10 A 265 SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 A 265 SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER GLN
SEQRES 12 A 265 ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP
SEQRES 13 A 265 HIS LEU ASN LYS ASN TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 A 265 LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 265 LEU THR HIS ALA ARG PRO PHE TYR ASN SER LEU PRO THR
SEQRES 16 A 265 SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR
SEQRES 17 A 265 HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS
SEQRES 18 A 265 TYR SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP
SEQRES 19 A 265 THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP
SEQRES 20 A 265 GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 265 PRO PHE ALA LEU GLU
HET CL A 301 1
HET CL A 302 1
HET CL A 303 1
HET MG A 304 1
HET MG A 305 1
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 2 CL 3(CL 1-)
FORMUL 5 MG 2(MG 2+)
FORMUL 7 HOH *198(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 SER A 31 ALA A 35 5 5
HELIX 3 AA3 THR A 64 SER A 67 5 4
HELIX 4 AA4 VAL A 68 SER A 77 1 10
HELIX 5 AA5 GLN A 93 ASP A 111 1 19
HELIX 6 AA6 SER A 113 SER A 118 1 6
HELIX 7 AA7 SER A 131 ARG A 144 1 14
HELIX 8 AA8 HIS A 185 LEU A 193 1 9
HELIX 9 AA9 PHE A 210 ILE A 214 5 5
HELIX 10 AB1 ASN A 216 ASP A 232 1 17
HELIX 11 AB2 ASP A 234 ARG A 236 5 3
HELIX 12 AB3 TYR A 237 CYS A 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O TYR A 45 N SER A 26
SHEET 3 AA1 6 VAL A 81 ILE A 85 -1 O VAL A 82 N TYR A 44
SHEET 4 AA1 6 TYR A 52 SER A 58 1 N VAL A 55 O VAL A 81
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N TYR A 52
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O LEU A 204 N GLY A 173
SHEET 3 AA2 3 VAL A 253 SER A 258 -1 O GLU A 255 N GLU A 203
SSBOND 1 CYS A 242 CYS A 260 1555 1555 2.03
LINK O VAL A 25 MG MG A 304 1555 1555 2.33
LINK O ARG A 32 MG MG A 305 1555 1555 2.37
LINK O ALA A 35 MG MG A 305 1555 1555 2.28
LINK O PHE A 38 MG MG A 305 1555 1555 2.34
LINK MG MG A 304 O HOH A 534 1555 1555 2.59
LINK MG MG A 304 O HOH A 404 1555 1555 2.34
LINK MG MG A 304 O HOH A 507 1555 1555 2.44
LINK MG MG A 305 O HOH A 518 1555 1555 2.72
LINK MG MG A 305 O HOH A 530 1555 1555 2.45
LINK MG MG A 305 O HOH A 580 1555 1555 2.40
LINK O ASP A 111 MG MG A 304 1555 4455 2.39
LINK O ALA A 112 MG MG A 304 1555 4455 2.43
CISPEP 1 CYS A 242 PRO A 243 0 2.62
CISPEP 2 CYS A 260 PRO A 261 0 -1.08
SITE 1 AC1 4 ARG A 187 ASN A 191 GLN A 239 ARG A 257
SITE 1 AC2 2 THR A 178 HIS A 209
SITE 1 AC3 4 TYR A 61 SER A 131 MET A 132 HOH A 495
SITE 1 AC4 6 VAL A 25 ASP A 111 ALA A 112 HOH A 404
SITE 2 AC4 6 HOH A 507 HOH A 534
SITE 1 AC5 6 ARG A 32 ALA A 35 PHE A 38 HOH A 518
SITE 2 AC5 6 HOH A 530 HOH A 580
CRYST1 40.595 50.512 105.477 90.00 90.00 90.00 P 21 21 21 4
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 0.024634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019797 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009481 0.00000
TER 2059 LEU A 264
MASTER 311 0 5 12 9 0 7 6 2220 1 15 21
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