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HEADER HYDROLASE 28-JUN-21 7OZM
TITLE CRYSTAL STRUCTURE OF MTBMGL K74A (CLOSED CAP CONFORMATION)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MGL;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: RV0183, LH57_01015;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MYCOBACTERIUM TUBERCULOSIS, MONOACYLGLYCEROL LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GRININGER,P.ASCHAUER,T.PAVKOV-KELLER,M.OBERER
REVDAT 1 15-SEP-21 7OZM 0
JRNL AUTH C.GRININGER,M.LEYPOLD,P.ASCHAUER,T.PAVKOV-KELLER,
JRNL AUTH 2 L.RIEGLER-BERKET,R.BREINBAUER,M.OBERER
JRNL TITL STRUCTURAL CHANGES IN THE CAP OF RV0183/MTBMGL MODULATE THE
JRNL TITL 2 SHAPE OF THE BINDING POCKET
JRNL REF BIOMOLECULES V. 11 2021
JRNL REFN ESSN 2218-273X
JRNL DOI 10.3390/BIOM11091299
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.830
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 16657
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2964
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 39.7700 - 5.9300 0.89 1211 141 0.1595 0.1771
REMARK 3 2 5.9300 - 4.7100 0.88 1217 129 0.1500 0.1829
REMARK 3 3 4.7100 - 4.1100 0.90 1224 129 0.1311 0.1743
REMARK 3 4 4.1100 - 3.7400 0.93 1273 145 0.1504 0.1909
REMARK 3 5 3.7400 - 3.4700 0.91 1250 138 0.1561 0.2265
REMARK 3 6 3.4700 - 3.2700 0.92 1264 138 0.1761 0.2206
REMARK 3 7 3.2700 - 3.1000 0.94 1267 145 0.1964 0.2967
REMARK 3 8 3.1000 - 2.9700 0.95 1303 143 0.2034 0.2825
REMARK 3 9 2.9700 - 2.8500 0.95 1282 146 0.2107 0.2784
REMARK 3 10 2.8500 - 2.7500 0.96 1310 142 0.2128 0.2757
REMARK 3 11 2.7500 - 2.6700 0.91 1232 134 0.2328 0.3065
REMARK 3 12 2.6700 - 2.5900 0.93 1295 146 0.2380 0.3200
REMARK 3 13 2.5900 - 2.5200 0.95 1269 142 0.2388 0.3356
REMARK 3 14 2.5200 - 2.4600 0.94 1312 145 0.2479 0.2874
REMARK 3 15 2.4600 - 2.4100 0.96 1285 142 0.2543 0.3220
REMARK 3 16 2.4100 - 2.3600 0.96 1295 144 0.2566 0.3123
REMARK 3 17 2.3600 - 2.3100 0.95 1329 144 0.2644 0.3085
REMARK 3 18 2.3100 - 2.2600 0.95 1258 142 0.2728 0.3609
REMARK 3 19 2.2600 - 2.2200 0.91 1253 142 0.2906 0.3009
REMARK 3 20 2.2200 - 2.1900 0.94 1295 146 0.2986 0.3599
REMARK 3 21 2.1900 - 2.1500 0.93 1273 141 0.3007 0.3552
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.725
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.97
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 : 0.007 2170
REMARK 3 ANGLE : 0.858 2964
REMARK 3 CHIRALITY : 0.053 343
REMARK 3 PLANARITY : 0.009 392
REMARK 3 DIHEDRAL : 5.233 311
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 7OZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1292116699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0723
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16663
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 39.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2700
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.75200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.430
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: 6EIC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % 2-PROPANOL, 24 % PEG 3350, 100 MM
REMARK 280 TRIS-HCL PH 8.5, 10 MG/ML PROTEIN, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.43000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.43000
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: 280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 -27
REMARK 465 SER A -26
REMARK 465 TYR A -25
REMARK 465 TYR A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 ASP A -17
REMARK 465 TYR A -16
REMARK 465 ASP A -15
REMARK 465 ILE A -14
REMARK 465 PRO A -13
REMARK 465 THR A -12
REMARK 465 THR A -11
REMARK 465 GLU A -10
REMARK 465 ASN A -9
REMARK 465 LEU A -8
REMARK 465 TYR A -7
REMARK 465 PHE A -6
REMARK 465 GLN A -5
REMARK 465 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
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 ASP A 26 45.54 -88.65
REMARK 500 GLU A 41 -150.26 -103.50
REMARK 500 VAL A 76 34.79 31.69
REMARK 500 SER A 110 -118.61 63.52
REMARK 500 ALA A 134 58.40 33.92
REMARK 500 ALA A 138 49.00 -147.06
REMARK 500 TYR A 255 -157.57 -87.35
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7OZM A 1 279 UNP O07427 MGLL_MYCTU 1 279
SEQADV 7OZM MET A -27 UNP O07427 INITIATING METHIONINE
SEQADV 7OZM SER A -26 UNP O07427 EXPRESSION TAG
SEQADV 7OZM TYR A -25 UNP O07427 EXPRESSION TAG
SEQADV 7OZM TYR A -24 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -23 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -22 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -21 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -20 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -19 UNP O07427 EXPRESSION TAG
SEQADV 7OZM HIS A -18 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ASP A -17 UNP O07427 EXPRESSION TAG
SEQADV 7OZM TYR A -16 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ASP A -15 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ILE A -14 UNP O07427 EXPRESSION TAG
SEQADV 7OZM PRO A -13 UNP O07427 EXPRESSION TAG
SEQADV 7OZM THR A -12 UNP O07427 EXPRESSION TAG
SEQADV 7OZM THR A -11 UNP O07427 EXPRESSION TAG
SEQADV 7OZM GLU A -10 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ASN A -9 UNP O07427 EXPRESSION TAG
SEQADV 7OZM LEU A -8 UNP O07427 EXPRESSION TAG
SEQADV 7OZM TYR A -7 UNP O07427 EXPRESSION TAG
SEQADV 7OZM PHE A -6 UNP O07427 EXPRESSION TAG
SEQADV 7OZM GLN A -5 UNP O07427 EXPRESSION TAG
SEQADV 7OZM GLY A -4 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ALA A -3 UNP O07427 EXPRESSION TAG
SEQADV 7OZM MET A -2 UNP O07427 EXPRESSION TAG
SEQADV 7OZM GLY A -1 UNP O07427 EXPRESSION TAG
SEQADV 7OZM SER A 0 UNP O07427 EXPRESSION TAG
SEQADV 7OZM ALA A 74 UNP O07427 LYS 74 ENGINEERED MUTATION
SEQRES 1 A 307 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 307 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 307 GLY SER MET THR THR THR ARG THR GLU ARG ASN PHE ALA
SEQRES 4 A 307 GLY ILE GLY ASP VAL ARG ILE VAL TYR ASP VAL TRP THR
SEQRES 5 A 307 PRO ASP THR ALA PRO GLN ALA VAL VAL VAL LEU ALA HIS
SEQRES 6 A 307 GLY LEU GLY GLU HIS ALA ARG ARG TYR ASP HIS VAL ALA
SEQRES 7 A 307 GLN ARG LEU GLY ALA ALA GLY LEU VAL THR TYR ALA LEU
SEQRES 8 A 307 ASP HIS ARG GLY HIS GLY ARG SER GLY GLY ALA ARG VAL
SEQRES 9 A 307 LEU VAL ARG ASP ILE SER GLU TYR THR ALA ASP PHE ASP
SEQRES 10 A 307 THR LEU VAL GLY ILE ALA THR ARG GLU TYR PRO GLY CYS
SEQRES 11 A 307 LYS ARG ILE VAL LEU GLY HIS SER MET GLY GLY GLY ILE
SEQRES 12 A 307 VAL PHE ALA TYR GLY VAL GLU ARG PRO ASP ASN TYR ASP
SEQRES 13 A 307 LEU MET VAL LEU SER ALA PRO ALA VAL ALA ALA GLN ASP
SEQRES 14 A 307 LEU VAL SER PRO VAL VAL ALA VAL ALA ALA LYS LEU LEU
SEQRES 15 A 307 GLY VAL VAL VAL PRO GLY LEU PRO VAL GLN GLU LEU ASP
SEQRES 16 A 307 PHE THR ALA ILE SER ARG ASP PRO GLU VAL VAL GLN ALA
SEQRES 17 A 307 TYR ASN THR ASP PRO LEU VAL HIS HIS GLY ARG VAL PRO
SEQRES 18 A 307 ALA GLY ILE GLY ARG ALA LEU LEU GLN VAL GLY GLU THR
SEQRES 19 A 307 MET PRO ARG ARG ALA PRO ALA LEU THR ALA PRO LEU LEU
SEQRES 20 A 307 VAL LEU HIS GLY THR ASP ASP ARG LEU ILE PRO ILE GLU
SEQRES 21 A 307 GLY SER ARG ARG LEU VAL GLU CYS VAL GLY SER ALA ASP
SEQRES 22 A 307 VAL GLN LEU LYS GLU TYR PRO GLY LEU TYR HIS GLU VAL
SEQRES 23 A 307 PHE ASN GLU PRO GLU ARG ASN GLN VAL LEU ASP ASP VAL
SEQRES 24 A 307 VAL ALA TRP LEU THR GLU ARG LEU
HET IPA A 301 4
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 IPA C3 H8 O
FORMUL 3 HOH *133(H2 O)
HELIX 1 AA1 ILE A 13 ASP A 15 5 3
HELIX 2 AA2 HIS A 42 ARG A 45 5 4
HELIX 3 AA3 TYR A 46 ALA A 56 1 11
HELIX 4 AA4 ASP A 80 TYR A 99 1 20
HELIX 5 AA5 SER A 110 ARG A 123 1 14
HELIX 6 AA6 ALA A 138 LEU A 142 5 5
HELIX 7 AA7 SER A 144 GLY A 155 1 12
HELIX 8 AA8 ASP A 167 ILE A 171 5 5
HELIX 9 AA9 ASP A 174 THR A 183 1 10
HELIX 10 AB1 ALA A 194 ALA A 211 1 18
HELIX 11 AB2 PRO A 212 LEU A 214 5 3
HELIX 12 AB3 PRO A 230 VAL A 241 1 12
HELIX 13 AB4 GLU A 257 PRO A 262 5 6
HELIX 14 AB5 GLU A 263 LEU A 279 1 17
SHEET 1 AA1 8 THR A 3 ALA A 11 0
SHEET 2 AA1 8 ARG A 17 PRO A 25 -1 O TYR A 20 N ARG A 8
SHEET 3 AA1 8 LEU A 58 LEU A 63 -1 O THR A 60 N TRP A 23
SHEET 4 AA1 8 ALA A 31 ALA A 36 1 N VAL A 33 O TYR A 61
SHEET 5 AA1 8 LYS A 103 HIS A 109 1 O ILE A 105 N VAL A 34
SHEET 6 AA1 8 LEU A 129 SER A 133 1 O SER A 133 N GLY A 108
SHEET 7 AA1 8 LEU A 218 GLY A 223 1 O LEU A 219 N LEU A 132
SHEET 8 AA1 8 VAL A 246 TYR A 251 1 O LYS A 249 N VAL A 220
SHEET 1 AA2 2 PRO A 162 GLN A 164 0
SHEET 2 AA2 2 VAL A 192 PRO A 193 -1 O VAL A 192 N GLN A 164
CRYST1 40.500 82.240 90.860 90.00 90.00 90.00 P 2 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 0.024691 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011006 0.00000
TER 2123 LEU A 279
MASTER 273 0 1 14 10 0 0 6 2259 1 4 24
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