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HEADER HYDROLASE 25-APR-13 4KE6
TITLE CRYSTAL STRUCTURE D196N MUTANT OF MONOGLYCERIDE LIPASE FROM BACILLUS
TITLE 2 SP. H257 IN COMPLEX WITH 1-RAC-LAUROYL GLYCEROL
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 FOLD, MONOGLYCERIDE LIPASE, MONOGLYCERIDES,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
REVDAT 1 18-SEP-13 4KE6 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 42399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2152
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 61.3722 - 6.9025 0.87 2764 140 0.1785 0.1969
REMARK 3 2 6.9025 - 5.4798 0.92 2733 129 0.2045 0.2488
REMARK 3 3 5.4798 - 4.7874 0.94 2733 154 0.1758 0.1948
REMARK 3 4 4.7874 - 4.3499 0.96 2727 155 0.1622 0.2029
REMARK 3 5 4.3499 - 4.0381 0.95 2821 128 0.1726 0.2117
REMARK 3 6 4.0381 - 3.8001 0.96 2753 153 0.1877 0.2365
REMARK 3 7 3.8001 - 3.6098 0.97 2749 134 0.2046 0.2649
REMARK 3 8 3.6098 - 3.4527 0.97 2779 155 0.2041 0.2436
REMARK 3 9 3.4527 - 3.3198 0.97 2740 135 0.2102 0.2555
REMARK 3 10 3.3198 - 3.2052 0.97 2753 138 0.2231 0.2852
REMARK 3 11 3.2052 - 3.1050 0.98 2770 155 0.2393 0.3086
REMARK 3 12 3.1050 - 3.0163 0.96 2640 172 0.2566 0.3274
REMARK 3 13 3.0163 - 2.9369 0.84 2460 115 0.2637 0.3407
REMARK 3 14 2.9369 - 2.8652 0.87 2422 144 0.2779 0.3608
REMARK 3 15 2.8652 - 2.8000 0.88 2403 145 0.2780 0.3683
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.06
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 : 0.008 11367
REMARK 3 ANGLE : 1.360 15472
REMARK 3 CHIRALITY : 0.066 1741
REMARK 3 PLANARITY : 0.009 1991
REMARK 3 DIHEDRAL : 13.933 4144
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 4KE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42482
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 73.621
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : 0.40100
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 (%): 51.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ~0.9 MM OF BMGL(D196N) WAS MIXED WITH
REMARK 280 180 MM 1-(RAC)-LAUROYL GLYCEROL DISSOLVED IN 99% ETOH TO ACHIEVE
REMARK 280 A FINAL PROTEIN-LIGAND RATIO OF 1:5. THE PROTEIN-LIGAND MIXTURE
REMARK 280 WAS INCUBATED AT 4 C FOR 1 HOUR. INITIAL CRYSTALS WERE OBTAINED
REMARK 280 USING THE MORPHEUS SCREEN IN CONDITION A4. THESE CRYSTALS WERE
REMARK 280 USED FOR PREPARING A SEED STOCK. THE OPTIMISED CRYSTALS WERE
REMARK 280 OBTAINED IN A DROP CONTAINING 0.9 MM BMGL(D196N); 56 % V/V MPD,
REMARK 280 0.1 M HEPES PH 6.9 AND 1:1000 DILUTION OF SEED STOCK IN A RATIO
REMARK 280 OF 2:2:1 RESPECTIVELY. 1-LG POWDER WAS ADDED TO THESE
REMARK 280 CRYSTALLIZATION DROPS AND THE CRYSTALS WERE SOAKED FOR 8H., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, 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 19.59250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.13200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.43900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 124.13200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.59250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.43900
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 THR A 133
REMARK 465 GLY A 134
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 ALA B 130
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 GLY B 250
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 ILE C 128
REMARK 465 ALA C 129
REMARK 465 ALA C 130
REMARK 465 GLY C 131
REMARK 465 MET C 132
REMARK 465 THR C 133
REMARK 465 GLY C 134
REMARK 465 GLY C 135
REMARK 465 GLY C 136
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 ILE D 128
REMARK 465 ALA D 129
REMARK 465 ALA D 130
REMARK 465 GLY D 131
REMARK 465 MET D 132
REMARK 465 THR D 133
REMARK 465 GLY D 134
REMARK 465 GLY D 135
REMARK 465 GLY D 136
REMARK 465 GLU D 137
REMARK 465 LEU D 138
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 SER E 2
REMARK 465 GLU E 3
REMARK 465 ILE E 128
REMARK 465 ALA E 129
REMARK 465 ALA E 130
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 LEU E 138
REMARK 465 PRO E 139
REMARK 465 ARG E 140
REMARK 465 TYR E 141
REMARK 465 LEU E 142
REMARK 465 ASP E 143
REMARK 465 SER E 144
REMARK 465 ILE E 145
REMARK 465 GLY E 146
REMARK 465 SER E 147
REMARK 465 GLY E 250
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 GLU F 3
REMARK 465 ILE F 128
REMARK 465 ALA F 129
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 465 LEU F 138
REMARK 465 PRO F 139
REMARK 465 ARG F 140
REMARK 465 TYR F 141
REMARK 465 LEU F 142
REMARK 465 ASP F 143
REMARK 465 SER F 144
REMARK 465 ILE F 145
REMARK 465 GLY F 146
REMARK 465 GLY F 250
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 45 CB CG CD CE
REMARK 480 GLN A 89 CD OE1 NE2
REMARK 480 MET A 132 CB CG SD CE
REMARK 480 LYS A 155 CB CG CD CE
REMARK 480 LYS B 45 CD CE NZ
REMARK 480 LYS B 56 CD CE NZ
REMARK 480 LEU B 138 CD1 CD2
REMARK 480 LYS B 155 CG CD CE NZ
REMARK 480 ARG B 183 CD NE CZ NH1 NH2
REMARK 480 GLU B 215 CA CB CG CD OE1 OE2
REMARK 480 GLN C 89 CG CD OE1 NE2
REMARK 480 LYS C 155 CB CG CD CE NZ
REMARK 480 ARG C 183 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG C 222 CZ NH1 NH2
REMARK 480 GLN D 89 CB CG CD OE1 NE2
REMARK 480 CYS D 114 N CA C O CB SG
REMARK 480 LYS D 155 CB CG CD CE NZ
REMARK 480 ARG D 183 CD NE CZ NH1 NH2
REMARK 480 GLN E 4 CB CG CD OE1 NE2
REMARK 480 VAL E 7 CG1 CG2
REMARK 480 LYS E 45 CG CD CE NZ
REMARK 480 LYS E 56 CD CE NZ
REMARK 480 TYR E 62 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR E 62 OH
REMARK 480 GLU E 63 CG CD OE1 OE2
REMARK 480 ARG E 67 CG CD NE CZ NH1 NH2
REMARK 480 LYS E 155 CD CE NZ
REMARK 480 LYS E 161 CB CG CD CE NZ
REMARK 480 ARG E 172 CA CB CG CD NE CZ NH1
REMARK 480 ARG E 172 NH2
REMARK 480 LYS F 45 CG CD CE NZ
REMARK 480 GLN F 89 CB CG CD OE1 NE2
REMARK 480 GLU F 215 CA CB CG CD OE1 OE2
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 OE1 GLU B 137 OG1 THR D 69 1.77
REMARK 500 ND2 ASN C 196 O VAL C 199 1.95
REMARK 500 O ALA A 129 N GLY A 131 2.01
REMARK 500 OG SER D 144 OG1 THR D 162 2.11
REMARK 500 ND2 ASN A 196 O VAL A 199 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 ILE B 125 CG1 - CB - CG2 ANGL. DEV. = -17.5 DEGREES
REMARK 500 PRO C 111 C - N - CD ANGL. DEV. = -19.8 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 GLU A 3 133.62 -29.83
REMARK 500 ASN A 18 -112.10 -131.46
REMARK 500 THR A 30 -2.82 70.58
REMARK 500 THR A 60 -78.05 -122.72
REMARK 500 SER A 97 -115.99 60.76
REMARK 500 ALA A 130 20.33 11.46
REMARK 500 VAL A 198 -60.30 -123.83
REMARK 500 TYR A 225 -149.50 -95.60
REMARK 500 ASN B 18 -108.15 -133.53
REMARK 500 THR B 30 -3.94 69.33
REMARK 500 THR B 60 -79.16 -127.84
REMARK 500 SER B 97 -115.87 61.99
REMARK 500 ALA B 127 -49.12 -165.39
REMARK 500 ILE B 128 94.95 -52.78
REMARK 500 VAL B 198 -58.05 -122.39
REMARK 500 TYR B 225 -151.65 -97.66
REMARK 500 ASN C 18 -111.49 -131.80
REMARK 500 THR C 30 -1.42 68.43
REMARK 500 THR C 60 -80.56 -128.08
REMARK 500 SER C 97 -115.71 60.84
REMARK 500 VAL C 198 -59.70 -123.52
REMARK 500 GLU C 215 67.65 -160.43
REMARK 500 GLU C 217 140.38 -171.40
REMARK 500 TYR C 225 -147.32 -96.17
REMARK 500 ASN D 18 -78.54 -130.85
REMARK 500 THR D 30 -2.43 68.91
REMARK 500 THR D 60 -80.11 -126.58
REMARK 500 SER D 97 -114.65 60.02
REMARK 500 ASP D 153 35.29 -97.15
REMARK 500 VAL D 198 -58.88 -123.79
REMARK 500 TYR D 225 -147.63 -99.36
REMARK 500 LEU E 8 -170.22 -66.86
REMARK 500 ASN E 18 -113.77 -130.25
REMARK 500 THR E 30 -0.59 68.99
REMARK 500 THR E 60 -82.46 -123.20
REMARK 500 SER E 97 -112.99 60.78
REMARK 500 ASP E 153 34.73 -81.93
REMARK 500 LEU E 157 104.52 -54.77
REMARK 500 VAL E 198 -59.48 -121.72
REMARK 500 TYR E 225 -146.09 -98.64
REMARK 500 ASN F 18 -109.38 -132.05
REMARK 500 THR F 60 -77.72 -126.66
REMARK 500 SER F 97 -112.92 58.73
REMARK 500 LEU F 173 -54.56 -25.68
REMARK 500 VAL F 198 -56.91 -124.20
REMARK 500 PRO F 201 -7.74 -58.43
REMARK 500 TYR F 225 -149.44 -92.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS B 110 10.02
REMARK 500 ASN E 18 12.45
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 1QW A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KE7 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE9 RELATED DB: PDB
REMARK 900 RELATED ID: 4KEA RELATED DB: PDB
DBREF 4KE6 A 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE6 B 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE6 C 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE6 D 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE6 E 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE6 F 1 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 4KE6 MET A -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY A -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER A -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER A -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER A -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER A -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY A -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU A -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL A -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO A -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG A -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY A -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER A -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS A 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ASN A 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KE6 MET B -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY B -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER B -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER B -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER B -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER B -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY B -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU B -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL B -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO B -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG B -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY B -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER B -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS B 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ASN B 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KE6 MET C -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY C -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER C -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER C -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER C -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER C -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY C -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU C -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL C -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO C -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG C -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY C -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER C -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS C 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ASN C 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KE6 MET D -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY D -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER D -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER D -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER D -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER D -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY D -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU D -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL D -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO D -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG D -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY D -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER D -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS D 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ASN D 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KE6 MET E -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY E -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER E -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER E -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER E -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER E -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY E -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU E -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL E -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO E -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG E -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY E -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER E -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS E 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ASN E 196 UNP P82597 ASP 196 ENGINEERED MUTATION
SEQADV 4KE6 MET F -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY F -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER F -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER F -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER F -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER F -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY F -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 LEU F -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 VAL F -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 PRO F -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 ARG F -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 GLY F -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 SER F -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 HIS F 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE6 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 1QW A 301 19
HET MPD C 301 8
HET MPD E 301 8
HET MPD F 301 8
HET MPD F 302 8
HETNAM 1QW (2R)-2,3-DIHYDROXYPROPYL DODECANOATE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN 1QW 1-LAUROYL-RAC-GLYCEROL
FORMUL 7 1QW C15 H30 O4
FORMUL 8 MPD 4(C6 H14 O2)
FORMUL 12 HOH *31(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 ALA A 130 1 6
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 THR B 164 LYS B 180 1 17
HELIX 18 18 LEU B 181 ILE B 184 5 4
HELIX 19 19 PRO B 201 ILE B 211 1 11
HELIX 20 20 VAL B 227 ASP B 231 5 5
HELIX 21 21 ASP B 233 ALA B 249 1 17
HELIX 22 22 THR C 32 SER C 35 5 4
HELIX 23 23 MET C 36 ALA C 46 1 11
HELIX 24 24 HIS C 61 ARG C 67 1 7
HELIX 25 25 THR C 69 GLN C 86 1 18
HELIX 26 26 SER C 97 HIS C 110 1 14
HELIX 27 27 THR C 164 LYS C 180 1 17
HELIX 28 28 LEU C 181 ILE C 184 5 4
HELIX 29 29 PRO C 201 ILE C 211 1 11
HELIX 30 30 VAL C 227 ASP C 231 5 5
HELIX 31 31 ASP C 233 ALA C 249 1 17
HELIX 32 32 THR D 32 SER D 35 5 4
HELIX 33 33 MET D 36 ALA D 46 1 11
HELIX 34 34 HIS D 61 ARG D 67 1 7
HELIX 35 35 THR D 69 GLN D 86 1 18
HELIX 36 36 SER D 97 GLU D 108 1 12
HELIX 37 37 THR D 164 LYS D 180 1 17
HELIX 38 38 LEU D 181 ILE D 184 5 4
HELIX 39 39 GLY D 202 ILE D 211 1 10
HELIX 40 40 ASP D 233 ALA D 249 1 17
HELIX 41 41 THR E 32 SER E 35 5 4
HELIX 42 42 MET E 36 ALA E 46 1 11
HELIX 43 43 HIS E 61 ARG E 67 1 7
HELIX 44 44 THR E 69 GLN E 86 1 18
HELIX 45 45 SER E 97 HIS E 110 1 14
HELIX 46 46 PRO E 163 LYS E 180 1 18
HELIX 47 47 LEU E 181 ILE E 184 5 4
HELIX 48 48 GLY E 202 ILE E 211 1 10
HELIX 49 49 VAL E 227 ASP E 231 5 5
HELIX 50 50 ASP E 233 ALA E 249 1 17
HELIX 51 51 THR F 32 SER F 35 5 4
HELIX 52 52 MET F 36 GLY F 47 1 12
HELIX 53 53 HIS F 61 ARG F 67 1 7
HELIX 54 54 THR F 69 GLN F 86 1 18
HELIX 55 55 SER F 97 GLU F 108 1 12
HELIX 56 56 PRO F 163 LYS F 180 1 18
HELIX 57 57 LEU F 181 ILE F 184 5 4
HELIX 58 58 PRO F 201 ILE F 211 1 11
HELIX 59 59 VAL F 227 ASP F 231 5 5
HELIX 60 60 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 VAL A 23 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 ILE A 113 ILE A 119 1 O CYS A 114 N ILE A 91
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 GLU A 217 N ILE A 190
SHEET 3 C 4 GLU B 215 LEU B 221 -1 O ILE B 218 N LYS A 216
SHEET 4 C 4 ALA B 188 SER B 193 1 N ILE B 190 O GLU B 217
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 PHE B 92 N LEU B 24
SHEET 5 D 5 GLY B 115 ILE B 119 1 O VAL B 117 N VAL B 93
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 5 PHE C 14 ALA C 16 0
SHEET 2 F 5 THR C 49 LEU C 52 -1 O LEU C 52 N PHE C 14
SHEET 3 F 5 VAL C 21 VAL C 26 1 N LEU C 25 O CYS C 51
SHEET 4 F 5 THR C 90 LEU C 96 1 O THR C 90 N GLY C 22
SHEET 5 F 5 GLY C 115 ILE C 119 1 O ILE C 119 N GLY C 95
SHEET 1 G 2 TYR C 141 ASP C 143 0
SHEET 2 G 2 LYS C 161 PRO C 163 -1 O THR C 162 N LEU C 142
SHEET 1 H 4 ILE C 190 SER C 193 0
SHEET 2 H 4 GLU C 215 LEU C 221 1 O GLU C 217 N ILE C 190
SHEET 3 H 4 GLU F 215 LEU F 221 -1 O LYS F 216 N ILE C 218
SHEET 4 H 4 ALA F 188 SER F 193 1 N ILE F 190 O GLU F 217
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 LEU D 25 O CYS D 51
SHEET 4 I 5 THR D 90 LEU D 96 1 O THR D 94 N LEU D 24
SHEET 5 I 5 ILE D 113 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 4 ALA D 188 SER D 193 0
SHEET 2 K 4 GLU D 215 LEU D 221 1 O LEU D 221 N VAL D 192
SHEET 3 K 4 GLU E 215 LEU E 221 -1 O ILE E 218 N LYS D 216
SHEET 4 K 4 ALA E 188 SER E 193 1 N VAL E 192 O LEU E 221
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 21 O THR E 49
SHEET 4 L 5 THR E 90 LEU E 96 1 O PHE E 92 N LEU E 24
SHEET 5 L 5 GLY E 115 ILE E 119 1 O VAL E 117 N VAL E 93
SHEET 1 M 5 PHE F 14 ALA F 16 0
SHEET 2 M 5 THR F 49 LEU F 52 -1 O LEU F 52 N PHE F 14
SHEET 3 M 5 VAL F 21 VAL F 26 1 N VAL F 21 O THR F 49
SHEET 4 M 5 THR F 90 LEU F 96 1 O THR F 94 N LEU F 24
SHEET 5 M 5 GLY F 115 ILE F 119 1 O ILE F 119 N GLY F 95
CISPEP 1 GLY D 146 SER D 147 0 3.27
SITE 1 AC1 8 GLY A 28 PHE A 29 SER A 97 MET A 98
SITE 2 AC1 8 ILE A 128 SER A 147 GLU A 156 ASP C 143
SITE 1 AC2 3 SER C 97 ILE C 145 LEU C 167
SITE 1 AC3 6 VAL E 21 GLY E 47 TYR E 48 VAL F 21
SITE 2 AC3 6 ALA F 46 TYR F 48
SITE 1 AC4 2 LYS F 161 MPD F 302
SITE 1 AC5 2 THR F 164 MPD F 301
CRYST1 39.185 182.878 248.264 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 0.025520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005468 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004028 0.00000
TER 1910 ALA A 249
TER 3793 ALA B 249
TER 5657 ALA C 249
TER 7510 ALA D 249
TER 9272 ALA E 249
TER 11046 ALA F 249
MASTER 648 0 5 60 50 0 7 611104 6 51 126
END |