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HEADER HYDROLASE 25-APR-13 4KEA
TITLE CRYSTAL STRUCTURE OF D196N MUTANT OF MONOGLYCERIDE LIPASE FROM
TITLE 2 BACILLUS SP. H257 IN SPACE GROUP P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 129908;
SOURCE 4 STRAIN: H-257;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A(+)
KEYWDS ALPHA/BETA HYDROLASE, MONOGLYCERIDE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
REVDAT 1 18-SEP-13 4KEA 0
JRNL AUTH S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
JRNL TITL CONFORMATIONAL PLASTICITY AND LIGAND BINDING OF BACTERIAL
JRNL TITL 2 MONOACYLGLYCEROL LIPASE
JRNL REF J.BIOL.CHEM. 2013
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 195079
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 9832
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 19.8829 - 5.2508 1.00 6666 382 0.1797 0.1912
REMARK 3 2 5.2508 - 4.1804 1.00 6379 348 0.1461 0.1585
REMARK 3 3 4.1804 - 3.6557 1.00 6303 359 0.1515 0.1678
REMARK 3 4 3.6557 - 3.3232 1.00 6259 340 0.1660 0.1876
REMARK 3 5 3.3232 - 3.0859 1.00 6255 341 0.1771 0.1961
REMARK 3 6 3.0859 - 2.9045 1.00 6224 321 0.1817 0.2002
REMARK 3 7 2.9045 - 2.7595 1.00 6184 340 0.1892 0.2125
REMARK 3 8 2.7595 - 2.6396 1.00 6202 312 0.1911 0.2031
REMARK 3 9 2.6396 - 2.5382 1.00 6218 327 0.1954 0.2073
REMARK 3 10 2.5382 - 2.4508 1.00 6072 343 0.1984 0.2281
REMARK 3 11 2.4508 - 2.3743 1.00 6240 332 0.2029 0.2242
REMARK 3 12 2.3743 - 2.3065 1.00 6056 334 0.2018 0.2247
REMARK 3 13 2.3065 - 2.2459 1.00 6275 319 0.2009 0.2404
REMARK 3 14 2.2459 - 2.1912 1.00 6060 331 0.2098 0.2289
REMARK 3 15 2.1912 - 2.1414 1.00 6187 337 0.2063 0.2387
REMARK 3 16 2.1414 - 2.0959 1.00 6165 294 0.2188 0.2608
REMARK 3 17 2.0959 - 2.0540 1.00 6033 349 0.2252 0.2459
REMARK 3 18 2.0540 - 2.0153 1.00 6210 322 0.2178 0.2487
REMARK 3 19 2.0153 - 1.9793 1.00 6108 330 0.2228 0.2219
REMARK 3 20 1.9793 - 1.9458 1.00 6128 280 0.2316 0.2602
REMARK 3 21 1.9458 - 1.9145 1.00 6168 332 0.2312 0.2486
REMARK 3 22 1.9145 - 1.8850 1.00 6110 301 0.2274 0.2632
REMARK 3 23 1.8850 - 1.8573 1.00 6069 320 0.2309 0.2397
REMARK 3 24 1.8573 - 1.8312 1.00 6174 330 0.2346 0.2536
REMARK 3 25 1.8312 - 1.8064 1.00 6142 293 0.2412 0.2781
REMARK 3 26 1.8064 - 1.7830 1.00 5965 318 0.2456 0.2674
REMARK 3 27 1.7830 - 1.7607 1.00 6166 334 0.2526 0.2802
REMARK 3 28 1.7607 - 1.7395 1.00 6169 328 0.2589 0.3249
REMARK 3 29 1.7395 - 1.7193 1.00 6076 301 0.2668 0.2865
REMARK 3 30 1.7193 - 1.7000 1.00 5984 334 0.2679 0.2999
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.18
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 12049
REMARK 3 ANGLE : 0.954 16465
REMARK 3 CHIRALITY : 0.180 1872
REMARK 3 PLANARITY : 0.005 2109
REMARK 3 DIHEDRAL : 13.111 4438
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 4KEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 195210
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : 0.40600
REMARK 200 FOR SHELL : 1.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 6.9, 54% V/V MPD, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
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 19.58250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 122.35200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.56550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 122.35200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.58250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.56550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 250
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 131
REMARK 465 MET B 132
REMARK 465 THR B 133
REMARK 465 GLY B 134
REMARK 465 GLY B 135
REMARK 465 GLY B 136
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 133
REMARK 465 GLY C 134
REMARK 465 GLY C 135
REMARK 465 GLY C 250
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLY D 131
REMARK 465 MET D 132
REMARK 465 THR D 133
REMARK 465 GLY D 134
REMARK 465 GLY D 250
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 GLY E 131
REMARK 465 MET E 132
REMARK 465 THR E 133
REMARK 465 GLY E 134
REMARK 465 GLY E 135
REMARK 465 GLY E 136
REMARK 465 GLU E 137
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ALA F 130
REMARK 465 GLY F 131
REMARK 465 MET F 132
REMARK 465 THR F 133
REMARK 465 GLY F 134
REMARK 465 GLY F 135
REMARK 465 GLY F 136
REMARK 465 GLU F 137
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 E 156 O4 MPD E 302 1.96
REMARK 500 OG SER E 147 OE1 GLU E 156 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 114 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
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 ASN A 18 -111.78 -129.73
REMARK 500 THR A 30 -3.05 70.87
REMARK 500 THR A 60 -78.54 -122.71
REMARK 500 SER A 97 -116.44 61.22
REMARK 500 VAL A 198 -60.24 -124.08
REMARK 500 TYR A 225 -149.48 -95.81
REMARK 500 ASN B 18 -108.32 -133.67
REMARK 500 THR B 30 -3.68 69.80
REMARK 500 THR B 60 -78.54 -127.39
REMARK 500 SER B 97 -116.51 62.40
REMARK 500 ASP B 194 -14.27 -41.63
REMARK 500 VAL B 198 -58.54 -122.36
REMARK 500 TYR B 225 -151.13 -97.34
REMARK 500 ASN C 18 -110.54 -131.24
REMARK 500 THR C 30 -1.12 68.20
REMARK 500 THR C 60 -80.99 -127.81
REMARK 500 SER C 97 -115.70 60.70
REMARK 500 ALA C 130 46.11 -91.19
REMARK 500 VAL C 198 -58.56 -123.26
REMARK 500 TYR C 225 -146.61 -96.74
REMARK 500 ASN D 18 -115.47 -130.22
REMARK 500 THR D 30 -2.59 68.35
REMARK 500 THR D 60 -79.61 -125.82
REMARK 500 SER D 97 -115.39 60.37
REMARK 500 ASP D 153 35.87 -99.32
REMARK 500 VAL D 198 -58.10 -123.72
REMARK 500 TYR D 225 -147.39 -99.05
REMARK 500 ASN E 18 -117.80 -129.41
REMARK 500 THR E 30 -0.95 69.17
REMARK 500 THR E 60 -82.14 -123.55
REMARK 500 SER E 97 -113.71 60.80
REMARK 500 ASP E 153 37.79 -82.28
REMARK 500 VAL E 198 -59.05 -121.67
REMARK 500 TYR E 225 -146.33 -98.55
REMARK 500 ASN F 18 -111.13 -131.50
REMARK 500 THR F 60 -78.57 -126.55
REMARK 500 SER F 97 -113.49 58.55
REMARK 500 ALA F 127 41.51 -68.19
REMARK 500 ILE F 128 -36.89 -137.78
REMARK 500 LEU F 173 -54.10 -23.38
REMARK 500 VAL F 198 -56.88 -125.05
REMARK 500 PRO F 201 -7.20 -57.03
REMARK 500 TYR F 225 -148.77 -92.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KE6 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE7 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE9 RELATED DB: PDB
DBREF 4KEA A 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KEA B 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KEA C 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KEA D 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KEA E 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KEA F 1 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 4KEA MET A -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY A -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER A -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER A -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER A -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER A -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY A -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU A -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL A -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO A -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG A -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY A -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER A -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS A 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN A 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KEA MET B -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY B -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER B -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER B -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER B -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER B -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY B -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU B -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL B -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO B -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG B -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY B -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER B -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS B 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN B 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KEA MET C -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY C -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER C -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER C -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER C -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER C -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY C -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU C -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL C -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO C -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG C -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY C -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER C -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS C 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN C 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KEA MET D -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY D -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER D -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER D -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER D -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER D -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY D -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU D -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL D -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO D -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG D -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY D -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER D -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS D 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN D 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KEA MET E -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY E -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER E -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER E -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER E -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER E -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY E -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU E -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL E -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO E -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG E -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY E -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER E -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS E 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN E 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KEA MET F -19 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY F -18 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER F -17 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER F -16 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -15 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -14 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -13 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -12 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -11 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F -10 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER F -9 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER F -8 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY F -7 UNP P82597 EXPRESSION TAG
SEQADV 4KEA LEU F -6 UNP P82597 EXPRESSION TAG
SEQADV 4KEA VAL F -5 UNP P82597 EXPRESSION TAG
SEQADV 4KEA PRO F -4 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ARG F -3 UNP P82597 EXPRESSION TAG
SEQADV 4KEA GLY F -2 UNP P82597 EXPRESSION TAG
SEQADV 4KEA SER F -1 UNP P82597 EXPRESSION TAG
SEQADV 4KEA HIS F 0 UNP P82597 EXPRESSION TAG
SEQADV 4KEA ASN F 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 A 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 A 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 A 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 A 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 A 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 A 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 A 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 A 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 A 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 A 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 A 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 A 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 A 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 A 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 A 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 A 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 A 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 A 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 A 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 B 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 B 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 B 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 B 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 B 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 B 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 B 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 B 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 B 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 B 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 B 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 B 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 B 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 B 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 B 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 B 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 B 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 B 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 B 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 B 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 C 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 C 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 C 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 C 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 C 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 C 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 C 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 C 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 C 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 C 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 C 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 C 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 C 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 C 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 C 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 C 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 C 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 C 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 C 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 C 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 D 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 D 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 D 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 D 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 D 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 D 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 D 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 D 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 D 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 D 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 D 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 D 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 D 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 D 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 D 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 D 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 D 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 D 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 D 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 D 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 E 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 E 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 E 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 E 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 E 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 E 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 E 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 E 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 E 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 E 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 E 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 E 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 E 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 E 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 E 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 E 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 E 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 E 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 E 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 E 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 F 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 F 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 F 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 F 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 F 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 F 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 F 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 F 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 F 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 F 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 F 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 F 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 F 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 F 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 F 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 F 270 LEU ILE PHE VAL SER ASP GLU ASN HIS VAL VAL PRO PRO
SEQRES 18 F 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 F 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 F 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 F 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
HET MPD A 301 8
HET MPD A 302 8
HET MPD A 303 8
HET MPD A 304 8
HET MPD A 305 8
HET MPD A 306 8
HET MPD B 301 8
HET MPD B 302 8
HET MPD B 303 8
HET MPD B 304 8
HET MPD C 301 8
HET MPD C 302 8
HET MPD C 303 8
HET MPD C 304 8
HET MPD D 301 8
HET MPD D 302 8
HET MPD D 303 8
HET MPD E 301 8
HET MPD E 302 8
HET MPD E 303 8
HET MPD E 304 8
HET MPD F 301 8
HET MPD F 302 8
HET MPD F 303 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 7 MPD 24(C6 H14 O2)
FORMUL 31 HOH *904(H2 O)
HELIX 1 1 THR A 32 SER A 35 5 4
HELIX 2 2 MET A 36 ALA A 46 1 11
HELIX 3 3 HIS A 61 THR A 68 1 8
HELIX 4 4 THR A 69 GLN A 86 1 18
HELIX 5 5 SER A 97 HIS A 110 1 14
HELIX 6 6 ILE A 125 GLY A 134 1 10
HELIX 7 7 THR A 164 LYS A 180 1 17
HELIX 8 8 LEU A 181 ILE A 184 5 4
HELIX 9 9 GLY A 202 ILE A 211 1 10
HELIX 10 10 VAL A 227 ASP A 231 5 5
HELIX 11 11 ASP A 233 ALA A 249 1 17
HELIX 12 12 THR B 32 SER B 35 5 4
HELIX 13 13 MET B 36 ALA B 46 1 11
HELIX 14 14 HIS B 61 ARG B 67 1 7
HELIX 15 15 THR B 69 GLN B 86 1 18
HELIX 16 16 SER B 97 HIS B 110 1 14
HELIX 17 17 ILE B 125 ALA B 130 1 6
HELIX 18 18 THR B 164 LYS B 180 1 17
HELIX 19 19 LEU B 181 ILE B 184 5 4
HELIX 20 20 GLY B 202 ILE B 211 1 10
HELIX 21 21 VAL B 227 ASP B 231 5 5
HELIX 22 22 ASP B 233 GLY B 250 1 18
HELIX 23 23 THR C 32 SER C 35 5 4
HELIX 24 24 MET C 36 ALA C 46 1 11
HELIX 25 25 HIS C 61 ARG C 67 1 7
HELIX 26 26 THR C 69 GLN C 86 1 18
HELIX 27 27 SER C 97 GLU C 108 1 12
HELIX 28 28 ILE C 125 ALA C 130 1 6
HELIX 29 29 THR C 164 LYS C 180 1 17
HELIX 30 30 LEU C 181 ILE C 184 5 4
HELIX 31 31 GLY C 202 ILE C 211 1 10
HELIX 32 32 VAL C 227 ASP C 231 5 5
HELIX 33 33 ASP C 233 ALA C 249 1 17
HELIX 34 34 THR D 32 SER D 35 5 4
HELIX 35 35 MET D 36 ALA D 46 1 11
HELIX 36 36 HIS D 61 ARG D 67 1 7
HELIX 37 37 THR D 69 GLN D 86 1 18
HELIX 38 38 SER D 97 HIS D 110 1 14
HELIX 39 39 ILE D 125 ALA D 130 1 6
HELIX 40 40 THR D 164 LYS D 180 1 17
HELIX 41 41 LEU D 181 ILE D 184 5 4
HELIX 42 42 GLY D 202 ILE D 211 1 10
HELIX 43 43 VAL D 227 ASP D 231 5 5
HELIX 44 44 ASP D 233 ALA D 249 1 17
HELIX 45 45 THR E 32 SER E 35 5 4
HELIX 46 46 MET E 36 ALA E 46 1 11
HELIX 47 47 HIS E 61 ARG E 67 1 7
HELIX 48 48 THR E 69 GLN E 86 1 18
HELIX 49 49 SER E 97 HIS E 110 1 14
HELIX 50 50 ILE E 125 ALA E 130 5 6
HELIX 51 51 THR E 164 LYS E 180 1 17
HELIX 52 52 LEU E 181 ILE E 184 5 4
HELIX 53 53 GLY E 202 ILE E 211 1 10
HELIX 54 54 VAL E 227 ASP E 231 5 5
HELIX 55 55 ASP E 233 ALA E 249 1 17
HELIX 56 56 THR F 32 SER F 35 5 4
HELIX 57 57 MET F 36 ALA F 46 1 11
HELIX 58 58 HIS F 61 ARG F 67 1 7
HELIX 59 59 THR F 69 GLN F 86 1 18
HELIX 60 60 SER F 97 GLU F 108 1 12
HELIX 61 61 THR F 164 LYS F 180 1 17
HELIX 62 62 LEU F 181 ILE F 184 5 4
HELIX 63 63 PRO F 201 ILE F 211 1 11
HELIX 64 64 VAL F 227 ASP F 231 5 5
HELIX 65 65 ASP F 233 ALA F 249 1 17
SHEET 1 A 5 PHE A 14 ALA A 16 0
SHEET 2 A 5 THR A 49 LEU A 52 -1 O LEU A 52 N PHE A 14
SHEET 3 A 5 VAL A 21 VAL A 26 1 N LEU A 25 O CYS A 51
SHEET 4 A 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 A 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 B 2 TYR A 141 ASP A 143 0
SHEET 2 B 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 C 4 ALA A 188 SER A 193 0
SHEET 2 C 4 GLU A 215 LEU A 221 1 O LEU A 221 N VAL A 192
SHEET 3 C 4 GLU C 215 LEU C 221 -1 O ILE C 218 N LYS A 216
SHEET 4 C 4 ALA C 188 SER C 193 1 N VAL C 192 O LEU C 221
SHEET 1 D 5 PHE B 14 ALA B 16 0
SHEET 2 D 5 THR B 49 LEU B 52 -1 O LEU B 52 N PHE B 14
SHEET 3 D 5 VAL B 21 VAL B 26 1 N LEU B 25 O CYS B 51
SHEET 4 D 5 THR B 90 LEU B 96 1 O THR B 90 N GLY B 22
SHEET 5 D 5 GLY B 115 ILE B 119 1 O ILE B 119 N GLY B 95
SHEET 1 E 2 TYR B 141 ASP B 143 0
SHEET 2 E 2 LYS B 161 PRO B 163 -1 O THR B 162 N LEU B 142
SHEET 1 F 2 ALA B 188 SER B 193 0
SHEET 2 F 2 LYS B 216 LEU B 221 1 O GLU B 217 N ILE B 190
SHEET 1 G 5 PHE C 14 ALA C 16 0
SHEET 2 G 5 THR C 49 LEU C 52 -1 O LEU C 52 N PHE C 14
SHEET 3 G 5 VAL C 21 VAL C 26 1 N LEU C 25 O CYS C 51
SHEET 4 G 5 THR C 90 LEU C 96 1 O THR C 90 N GLY C 22
SHEET 5 G 5 GLY C 115 ILE C 119 1 O ILE C 119 N GLY C 95
SHEET 1 H 2 TYR C 141 ASP C 143 0
SHEET 2 H 2 LYS C 161 PRO C 163 -1 O THR C 162 N LEU C 142
SHEET 1 I 5 PHE D 14 ALA D 16 0
SHEET 2 I 5 THR D 49 LEU D 52 -1 O LEU D 52 N PHE D 14
SHEET 3 I 5 VAL D 21 VAL D 26 1 N VAL D 23 O THR D 49
SHEET 4 I 5 THR D 90 LEU D 96 1 O THR D 94 N LEU D 24
SHEET 5 I 5 GLY D 115 ILE D 119 1 O ILE D 119 N GLY D 95
SHEET 1 J 2 TYR D 141 ASP D 143 0
SHEET 2 J 2 LYS D 161 PRO D 163 -1 O THR D 162 N LEU D 142
SHEET 1 K 2 ALA D 188 SER D 193 0
SHEET 2 K 2 LYS D 216 LEU D 221 1 O GLU D 217 N ILE D 190
SHEET 1 L 5 PHE E 14 ALA E 16 0
SHEET 2 L 5 THR E 49 LEU E 52 -1 O LEU E 52 N PHE E 14
SHEET 3 L 5 VAL E 21 VAL E 26 1 N VAL E 23 O THR E 49
SHEET 4 L 5 THR E 90 LEU E 96 1 O THR E 90 N GLY E 22
SHEET 5 L 5 GLY E 115 ILE E 119 1 O ILE E 119 N GLY E 95
SHEET 1 M 2 TYR E 141 ASP E 143 0
SHEET 2 M 2 LYS E 161 PRO E 163 -1 O THR E 162 N LEU E 142
SHEET 1 N 2 ALA E 188 SER E 193 0
SHEET 2 N 2 LYS E 216 LEU E 221 1 O LEU E 221 N VAL E 192
SHEET 1 O 5 PHE F 14 ALA F 16 0
SHEET 2 O 5 THR F 49 LEU F 52 -1 O LEU F 52 N PHE F 14
SHEET 3 O 5 VAL F 21 VAL F 26 1 N VAL F 21 O THR F 49
SHEET 4 O 5 THR F 90 LEU F 96 1 O PHE F 92 N LEU F 24
SHEET 5 O 5 GLY F 115 ILE F 119 1 O ILE F 119 N GLY F 95
SHEET 1 P 2 TYR F 141 ASP F 143 0
SHEET 2 P 2 LYS F 161 PRO F 163 -1 O THR F 162 N LEU F 142
SHEET 1 Q 2 ALA F 188 SER F 193 0
SHEET 2 Q 2 LYS F 216 LEU F 221 1 O LEU F 221 N VAL F 192
SITE 1 AC1 8 PHE A 29 THR A 30 LEU A 96 GLU A 156
SITE 2 AC1 8 ALA A 158 VAL A 227 HOH A 419 HOH A 431
SITE 1 AC2 4 SER A 97 VAL A 198 HOH A 570 MPD B 303
SITE 1 AC3 4 GLU A 239 ARG A 240 GLU A 243 LYS C 247
SITE 1 AC4 4 ASP A 231 TYR A 232 PRO A 235 HOH A 462
SITE 1 AC5 4 VAL A 21 GLY A 47 TYR A 48 ALA A 249
SITE 1 AC6 5 LEU A 8 LEU A 157 ALA A 158 TYR A 159
SITE 2 AC6 5 GLU A 160
SITE 1 AC7 9 GLY B 28 PHE B 29 THR B 30 LEU B 96
SITE 2 AC7 9 GLU B 156 VAL B 227 MPD B 302 HOH B 401
SITE 3 AC7 9 HOH B 411
SITE 1 AC8 4 PHE B 29 SER B 97 MPD B 301 HOH B 402
SITE 1 AC9 5 ALA A 127 MPD A 302 ASP B 143 MPD B 304
SITE 2 AC9 5 HOH B 437
SITE 1 BC1 4 ASP B 143 ILE B 145 MPD B 303 HOH B 583
SITE 1 BC2 4 PHE C 29 SER C 97 MPD C 302 HOH C 401
SITE 1 BC3 8 THR C 30 LEU C 96 SER C 97 GLU C 156
SITE 2 BC3 8 ALA C 158 MPD C 301 HOH C 401 HOH C 482
SITE 1 BC4 4 GLN C 86 ASP C 231 GLN C 234 PRO C 235
SITE 1 BC5 3 GLY C 47 TYR C 48 HOH C 519
SITE 1 BC6 6 PHE D 29 GLY D 31 GLU D 156 HIS D 226
SITE 2 BC6 6 MPD D 302 HOH D 493
SITE 1 BC7 6 SER D 97 ILE D 125 LEU D 170 VAL D 198
SITE 2 BC7 6 MPD D 301 HOH D 517
SITE 1 BC8 3 ASN D 151 ASP D 231 TYR D 232
SITE 1 BC9 8 PHE E 29 SER E 97 ILE E 125 LEU E 167
SITE 2 BC9 8 LEU E 170 VAL E 198 MPD E 302 HOH E 402
SITE 1 CC1 7 PHE E 29 THR E 30 LEU E 96 GLU E 156
SITE 2 CC1 7 VAL E 227 MPD E 301 HOH E 552
SITE 1 CC2 10 VAL E 21 ALA E 46 GLY E 47 TYR E 48
SITE 2 CC2 10 ALA E 249 HOH E 407 ALA F 46 TYR F 48
SITE 3 CC2 10 HOH F 402 HOH F 421
SITE 1 CC3 4 ASN E 151 ASP E 231 TYR E 232 GLN E 234
SITE 1 CC4 4 PHE F 29 SER F 97 VAL F 198 HOH F 462
SITE 1 CC5 6 PHE F 29 GLU F 156 ALA F 158 VAL F 227
SITE 2 CC5 6 HOH F 463 HOH F 504
SITE 1 CC6 5 ASN F 151 LEU F 230 ASP F 231 TYR F 232
SITE 2 CC6 5 GLN F 234
CRYST1 39.165 183.131 244.704 90.00 90.00 90.00 P 21 21 21 24
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 0.025533 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004087 0.00000
TER 1984 ALA A 249
TER 3906 GLY B 250
TER 5864 ALA C 249
TER 7783 ALA D 249
TER 9680 GLY E 250
TER 11566 GLY F 250
MASTER 622 0 24 65 54 0 38 612423 6 192 126
END |