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HEADER HYDROLASE 25-APR-13 4KE9
TITLE CRYSTAL STRUCTURE OF MONOGLYCERIDE LIPASE FROM BACILLUS SP. H257 IN
TITLE 2 COMPLEX WITH AN 1-STEARYOL GLYCEROL ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: 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, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
REVDAT 1 18-SEP-13 4KE9 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 48678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2492
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 43.6695 - 6.8276 0.94 3074 151 0.1974 0.2093
REMARK 3 2 6.8276 - 5.4225 1.00 3263 149 0.2112 0.2139
REMARK 3 3 5.4225 - 4.7380 1.00 3241 165 0.2013 0.2127
REMARK 3 4 4.7380 - 4.3052 1.00 3212 195 0.1833 0.2268
REMARK 3 5 4.3052 - 3.9969 1.00 3248 160 0.1950 0.2521
REMARK 3 6 3.9969 - 3.7614 1.00 3244 185 0.2008 0.1984
REMARK 3 7 3.7614 - 3.5731 1.00 3227 167 0.2173 0.2596
REMARK 3 8 3.5731 - 3.4176 1.00 3277 162 0.2245 0.2716
REMARK 3 9 3.4176 - 3.2861 1.00 3192 202 0.2319 0.2526
REMARK 3 10 3.2861 - 3.1727 1.00 3212 184 0.2427 0.2938
REMARK 3 11 3.1727 - 3.0736 1.00 3190 201 0.2357 0.2733
REMARK 3 12 3.0736 - 2.9857 1.00 3262 183 0.2416 0.3150
REMARK 3 13 2.9857 - 2.9071 1.00 3244 202 0.2382 0.3058
REMARK 3 14 2.9071 - 2.8362 1.00 3198 191 0.2330 0.2549
REMARK 3 15 2.8362 - 2.7718 1.00 3244 159 0.2261 0.2674
REMARK 3 16 2.7718 - 2.7128 1.00 3258 175 0.2220 0.2856
REMARK 3 17 2.7128 - 2.6585 1.00 3202 176 0.2221 0.2432
REMARK 3 18 2.6585 - 2.6084 1.00 3273 154 0.2224 0.2928
REMARK 3 19 2.6084 - 2.5618 1.00 3243 188 0.2246 0.2907
REMARK 3 20 2.5618 - 2.5184 1.00 3224 149 0.2251 0.2574
REMARK 3 21 2.5184 - 2.4777 0.99 3237 166 0.2289 0.2959
REMARK 3 22 2.4777 - 2.4396 0.95 3060 165 0.2379 0.2577
REMARK 3 23 2.4396 - 2.4038 0.90 2951 125 0.2371 0.2797
REMARK 3 24 2.4038 - 2.3699 0.85 2783 154 0.2349 0.3383
REMARK 3 25 2.3699 - 2.3379 0.79 2524 134 0.2339 0.2675
REMARK 3 26 2.3379 - 2.3075 0.75 2397 153 0.2314 0.3314
REMARK 3 27 2.3075 - 2.2787 0.70 2304 107 0.2422 0.3294
REMARK 3 28 2.2787 - 2.2512 0.67 2149 133 0.3003 0.3771
REMARK 3 29 2.2512 - 2.2250 0.62 1990 123 0.4385 0.4921
REMARK 3 30 2.2250 - 2.2000 0.60 1966 99 0.3340 0.3956
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.46400
REMARK 3 B22 (A**2) : 20.73080
REMARK 3 B33 (A**2) : -10.26690
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.00790
REMARK 3 B23 (A**2) : -0.00000
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 : 0.003 7907
REMARK 3 ANGLE : 0.840 10740
REMARK 3 CHIRALITY : 0.043 1191
REMARK 3 PLANARITY : 0.004 1378
REMARK 3 DIHEDRAL : 12.586 2836
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 4KE9 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 RCSB079228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : CHANNEL-CUT MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.661
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13900
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.55700
REMARK 200 R SYM FOR SHELL (I) : 0.55700
REMARK 200 FOR SHELL : 0.900
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 (%): 44.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC ACID PH 5.0 AND 22% PEG
REMARK 280 3350, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.14350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 SER A -7
REMARK 465 SER A -6
REMARK 465 GLY A -5
REMARK 465 LEU A -4
REMARK 465 VAL A -3
REMARK 465 PRO A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 HIS A 2
REMARK 465 GLY A 250
REMARK 465 MET B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 SER B -7
REMARK 465 SER B -6
REMARK 465 GLY B -5
REMARK 465 LEU B -4
REMARK 465 VAL B -3
REMARK 465 PRO B -2
REMARK 465 ARG B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 HIS B 2
REMARK 465 GLY B 250
REMARK 465 MET C -17
REMARK 465 GLY C -16
REMARK 465 SER C -15
REMARK 465 SER C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 SER C -7
REMARK 465 SER C -6
REMARK 465 GLY C -5
REMARK 465 LEU C -4
REMARK 465 VAL C -3
REMARK 465 PRO C -2
REMARK 465 ARG C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 HIS C 2
REMARK 465 GLU C 3
REMARK 465 GLY C 250
REMARK 465 MET D -17
REMARK 465 GLY D -16
REMARK 465 SER D -15
REMARK 465 SER D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 SER D -7
REMARK 465 SER D -6
REMARK 465 GLY D -5
REMARK 465 LEU D -4
REMARK 465 VAL D -3
REMARK 465 PRO D -2
REMARK 465 ARG D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 HIS D 2
REMARK 465 GLY D 250
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 -111.68 -118.62
REMARK 500 THR A 30 -5.63 65.31
REMARK 500 THR A 60 -84.91 -119.87
REMARK 500 ARG A 87 16.24 -152.73
REMARK 500 SER A 97 -114.15 60.22
REMARK 500 GLU A 195 63.22 -106.69
REMARK 500 TYR A 225 -145.68 -89.89
REMARK 500 ASN B 18 -121.78 -125.39
REMARK 500 THR B 30 -7.56 69.07
REMARK 500 THR B 60 -81.31 -118.07
REMARK 500 SER B 97 -116.65 60.03
REMARK 500 GLU B 195 60.81 -108.38
REMARK 500 TYR B 225 -144.54 -95.38
REMARK 500 ASN C 18 -114.11 -123.77
REMARK 500 THR C 60 -73.86 -130.08
REMARK 500 ARG C 87 12.03 -149.85
REMARK 500 SER C 97 -109.34 62.06
REMARK 500 GLU C 195 64.49 -103.66
REMARK 500 TYR C 225 -144.51 -92.43
REMARK 500 ASN D 18 -114.76 -126.97
REMARK 500 THR D 30 -1.12 63.19
REMARK 500 THR D 60 -73.47 -124.29
REMARK 500 SER D 97 -120.32 58.76
REMARK 500 TYR D 225 -141.39 -92.47
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 1R1 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1R1 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1R1 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1R1 D 301
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: 4KEA RELATED DB: PDB
DBREF 4KE9 A -17 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE9 B -17 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE9 C -17 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE9 D -17 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 4KE9 GLY A -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER A -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER A -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER A -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER A -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY A -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 LEU A -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 VAL A -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 PRO A -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 ARG A -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY A 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS A 2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY B -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER B -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER B -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER B -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER B -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY B -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 LEU B -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 VAL B -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 PRO B -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 ARG B -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY B 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS B 2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY C -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER C -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER C -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER C -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER C -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY C -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 LEU C -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 VAL C -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 PRO C -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 ARG C -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY C 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS C 2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY D -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER D -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER D -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER D -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 SER D -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY D -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 LEU D -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 VAL D -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 PRO D -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 ARG D -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 GLY D 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE9 HIS D 2 UNP P82597 EXPRESSION TAG
SEQRES 1 A 268 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 268 LEU VAL PRO ARG GLY SER HIS GLU GLN TYR PRO VAL LEU
SEQRES 3 A 268 SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY PRO VAL
SEQRES 4 A 268 GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR PRO HIS
SEQRES 5 A 268 SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS ALA GLY
SEQRES 6 A 268 TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS GLY THR
SEQRES 7 A 268 HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS ASP TRP
SEQRES 8 A 268 VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU LYS GLN
SEQRES 9 A 268 ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER MET GLY
SEQRES 10 A 268 GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS PRO ASP
SEQRES 11 A 268 ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL ASP ILE
SEQRES 12 A 268 PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY GLU LEU
SEQRES 13 A 268 PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU LYS ASN
SEQRES 14 A 268 PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR PRO THR
SEQRES 15 A 268 ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA GLN THR
SEQRES 16 A 268 LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA LEU ILE
SEQRES 17 A 268 PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO GLY ASN
SEQRES 18 A 268 ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR GLU LYS
SEQRES 19 A 268 GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL ALA THR
SEQRES 20 A 268 LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG SER LEU
SEQRES 21 A 268 GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 B 268 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 268 LEU VAL PRO ARG GLY SER HIS GLU GLN TYR PRO VAL LEU
SEQRES 3 B 268 SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY PRO VAL
SEQRES 4 B 268 GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR PRO HIS
SEQRES 5 B 268 SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS ALA GLY
SEQRES 6 B 268 TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS GLY THR
SEQRES 7 B 268 HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS ASP TRP
SEQRES 8 B 268 VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU LYS GLN
SEQRES 9 B 268 ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER MET GLY
SEQRES 10 B 268 GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS PRO ASP
SEQRES 11 B 268 ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL ASP ILE
SEQRES 12 B 268 PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY GLU LEU
SEQRES 13 B 268 PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU LYS ASN
SEQRES 14 B 268 PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR PRO THR
SEQRES 15 B 268 ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA GLN THR
SEQRES 16 B 268 LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA LEU ILE
SEQRES 17 B 268 PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO GLY ASN
SEQRES 18 B 268 ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR GLU LYS
SEQRES 19 B 268 GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL ALA THR
SEQRES 20 B 268 LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG SER LEU
SEQRES 21 B 268 GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 C 268 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 268 LEU VAL PRO ARG GLY SER HIS GLU GLN TYR PRO VAL LEU
SEQRES 3 C 268 SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY PRO VAL
SEQRES 4 C 268 GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR PRO HIS
SEQRES 5 C 268 SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS ALA GLY
SEQRES 6 C 268 TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS GLY THR
SEQRES 7 C 268 HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS ASP TRP
SEQRES 8 C 268 VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU LYS GLN
SEQRES 9 C 268 ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER MET GLY
SEQRES 10 C 268 GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS PRO ASP
SEQRES 11 C 268 ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL ASP ILE
SEQRES 12 C 268 PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY GLU LEU
SEQRES 13 C 268 PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU LYS ASN
SEQRES 14 C 268 PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR PRO THR
SEQRES 15 C 268 ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA GLN THR
SEQRES 16 C 268 LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA LEU ILE
SEQRES 17 C 268 PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO GLY ASN
SEQRES 18 C 268 ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR GLU LYS
SEQRES 19 C 268 GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL ALA THR
SEQRES 20 C 268 LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG SER LEU
SEQRES 21 C 268 GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 D 268 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 268 LEU VAL PRO ARG GLY SER HIS GLU GLN TYR PRO VAL LEU
SEQRES 3 D 268 SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY PRO VAL
SEQRES 4 D 268 GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR PRO HIS
SEQRES 5 D 268 SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS ALA GLY
SEQRES 6 D 268 TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS GLY THR
SEQRES 7 D 268 HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS ASP TRP
SEQRES 8 D 268 VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU LYS GLN
SEQRES 9 D 268 ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER MET GLY
SEQRES 10 D 268 GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS PRO ASP
SEQRES 11 D 268 ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL ASP ILE
SEQRES 12 D 268 PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY GLU LEU
SEQRES 13 D 268 PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU LYS ASN
SEQRES 14 D 268 PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR PRO THR
SEQRES 15 D 268 ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA GLN THR
SEQRES 16 D 268 LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA LEU ILE
SEQRES 17 D 268 PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO GLY ASN
SEQRES 18 D 268 ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR GLU LYS
SEQRES 19 D 268 GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL ALA THR
SEQRES 20 D 268 LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG SER LEU
SEQRES 21 D 268 GLU PHE PHE ALA LYS HIS ALA GLY
HET 1R1 A 301 25
HET 1R1 B 301 25
HET 1R1 C 301 25
HET 1R1 D 301 25
HETNAM 1R1 HEXADECYL HYDROGEN (R)-(3-AZIDOPROPYL)PHOSPHONATE
FORMUL 5 1R1 4(C19 H40 N3 O3 P)
FORMUL 9 HOH *303(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 GLU A 66 1 6
HELIX 4 4 THR A 69 GLN A 86 1 18
HELIX 5 5 SER A 97 GLU A 108 1 12
HELIX 6 6 ILE A 125 MET A 132 1 8
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 ASP A 233 ALA A 249 1 17
HELIX 11 11 THR B 32 SER B 35 5 4
HELIX 12 12 MET B 36 ALA B 46 1 11
HELIX 13 13 HIS B 61 GLU B 66 1 6
HELIX 14 14 THR B 69 GLN B 86 1 18
HELIX 15 15 SER B 97 HIS B 110 1 14
HELIX 16 16 ILE B 125 THR B 133 1 9
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 GLU C 66 1 6
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 ILE C 125 THR C 133 1 9
HELIX 28 28 THR C 164 LYS C 180 1 17
HELIX 29 29 LEU C 181 ILE C 184 5 4
HELIX 30 30 GLY C 202 ILE C 211 1 10
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 HIS D 110 1 14
HELIX 37 37 ILE D 125 THR D 133 1 9
HELIX 38 38 THR D 164 LYS D 180 1 17
HELIX 39 39 LEU D 181 ILE D 184 5 4
HELIX 40 40 GLY D 202 ILE D 211 1 10
HELIX 41 41 ASP D 233 ALA D 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 THR A 49
SHEET 4 A 5 THR A 90 LEU A 96 1 O THR A 94 N LEU A 24
SHEET 5 A 5 ILE A 113 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 2 ALA A 188 SER A 193 0
SHEET 2 C 2 LYS A 216 LEU A 221 1 O VAL A 219 N ILE A 190
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 VAL B 23 O THR B 49
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 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 VAL B 219 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 VAL C 23 O THR C 49
SHEET 4 G 5 THR C 90 LEU C 96 1 O THR C 94 N LEU C 24
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 2 ALA C 188 SER C 193 0
SHEET 2 I 2 LYS C 216 LEU C 221 1 O VAL C 219 N ILE C 190
SHEET 1 J 5 PHE D 14 ALA D 16 0
SHEET 2 J 5 THR D 49 LEU D 52 -1 O LEU D 52 N PHE D 14
SHEET 3 J 5 VAL D 21 VAL D 26 1 N VAL D 23 O THR D 49
SHEET 4 J 5 THR D 90 LEU D 96 1 O THR D 90 N GLY D 22
SHEET 5 J 5 GLY D 115 ILE D 119 1 O ILE D 119 N GLY D 95
SHEET 1 K 2 TYR D 141 ASP D 143 0
SHEET 2 K 2 LYS D 161 PRO D 163 -1 O THR D 162 N LEU D 142
SHEET 1 L 2 ALA D 188 SER D 193 0
SHEET 2 L 2 LYS D 216 LEU D 221 1 O GLU D 217 N ILE D 190
LINK OG SER A 97 P1 1R1 A 301 1555 1555 1.57
LINK OG SER D 97 P1 1R1 D 301 1555 1555 1.67
LINK OG SER B 97 P1 1R1 B 301 1555 1555 1.53
LINK OG SER C 97 P1 1R1 C 301 1555 1555 1.65
SITE 1 AC1 10 PHE A 29 SER A 97 MET A 98 ILE A 128
SITE 2 AC1 10 MET A 132 LEU A 142 LEU A 168 LEU A 170
SITE 3 AC1 10 HIS A 226 HOH A 451
SITE 1 AC2 12 GLY B 28 PHE B 29 SER B 97 MET B 98
SITE 2 AC2 12 ILE B 128 MET B 132 LEU B 138 LEU B 142
SITE 3 AC2 12 ILE B 145 LEU B 168 VAL B 198 HIS B 226
SITE 1 AC3 17 GLY C 28 PHE C 29 THR C 30 SER C 97
SITE 2 AC3 17 MET C 98 ALA C 127 ILE C 128 GLY C 131
SITE 3 AC3 17 MET C 132 LEU C 142 ILE C 145 GLY C 146
SITE 4 AC3 17 THR C 164 LEU C 167 LEU C 170 HIS C 226
SITE 5 AC3 17 VAL C 227
SITE 1 AC4 14 GLY D 28 PHE D 29 SER D 97 MET D 98
SITE 2 AC4 14 ILE D 128 PRO D 139 LEU D 142 ILE D 145
SITE 3 AC4 14 GLY D 146 SER D 147 ASP D 148 GLU D 156
SITE 4 AC4 14 LEU D 170 HIS D 226
CRYST1 76.857 80.287 85.712 90.00 100.02 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013011 0.000000 0.002299 0.00000
SCALE2 0.000000 0.012455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011848 0.00000
TER 1907 ALA A 249
TER 3814 ALA B 249
TER 5712 ALA C 249
TER 7619 ALA D 249
MASTER 394 0 4 41 36 0 15 6 8018 4 104 84
END |