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HEADER LIPID BINDING PROTEIN 07-JUL-20 6XOK
TITLE X-RAY STRUCTURE OF THE RHOMBOHEDRAL FORM OF THE LIPASE FROM
TITLE 2 THERMOMYCES LANUGINOSA AT 1.3 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_TAXID: 5541;
SOURCE 4 GENE: LIP;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS FLAVUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5059
KEYWDS DIACYLGLYCERIDE, INTERFACIAL ACTIVATION, OLIGOMER, SUBSTRATE COMPLEX,
KEYWDS 2 LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 14-OCT-20 6XOK 0
JRNL AUTH A.MCPHERSON,S.B.LARSON,A.KALASKY
JRNL TITL THE CRYSTAL STRUCTURES OF THERMOMYCES (HUMICOLA) LANUGINOSA
JRNL TITL 2 LIPASE IN COMPLEX WITH ENZYMATIC REACTANTS
JRNL REF CURRENT ENZYME INHIBITION V. 16 2020
JRNL DOI 10.2174/1573408016999200511090910
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 58353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.106
REMARK 3 R VALUE (WORKING SET) : 0.104
REMARK 3 FREE R VALUE : 0.134
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2865
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 80.5200 - 3.5400 1.00 3335 195 0.1417 0.1556
REMARK 3 2 3.5400 - 2.8100 1.00 3222 178 0.1136 0.1417
REMARK 3 3 2.8100 - 2.4600 1.00 3201 154 0.1127 0.1285
REMARK 3 4 2.4600 - 2.2300 1.00 3196 154 0.0948 0.1174
REMARK 3 5 2.2300 - 2.0700 1.00 3131 192 0.0878 0.1295
REMARK 3 6 2.0700 - 1.9500 1.00 3176 148 0.0874 0.1148
REMARK 3 7 1.9500 - 1.8500 1.00 3178 150 0.0881 0.1291
REMARK 3 8 1.8500 - 1.7700 1.00 3119 176 0.0863 0.1299
REMARK 3 9 1.7700 - 1.7000 1.00 3142 157 0.0885 0.1182
REMARK 3 10 1.7000 - 1.6400 1.00 3181 139 0.0811 0.1297
REMARK 3 11 1.6400 - 1.5900 1.00 3095 165 0.0799 0.1212
REMARK 3 12 1.5900 - 1.5500 1.00 3189 132 0.0756 0.1140
REMARK 3 13 1.5500 - 1.5100 0.99 3079 143 0.0761 0.1252
REMARK 3 14 1.5100 - 1.4700 0.96 3015 159 0.0715 0.1158
REMARK 3 15 1.4700 - 1.4400 0.92 2831 193 0.0756 0.1193
REMARK 3 16 1.4400 - 1.4100 0.86 2686 130 0.0800 0.1371
REMARK 3 17 1.4100 - 1.3800 0.74 2327 103 0.0867 0.1534
REMARK 3 18 1.3800 - 1.3500 0.57 1748 115 0.1006 0.1410
REMARK 3 19 1.3500 - 1.3300 0.38 1178 68 0.1169 0.1646
REMARK 3 20 1.3300 - 1.3000 0.14 459 14 0.1575 0.1926
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) : 0.079
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.345
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.44
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 2340
REMARK 3 ANGLE : 1.244 3189
REMARK 3 CHIRALITY : 0.099 342
REMARK 3 PLANARITY : 0.007 410
REMARK 3 DIHEDRAL : 20.100 882
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: STRUCTURE WAS THOROUGHLY REFINED USING
REMARK 3 REFMAC5 FROM CCP4 BUT THEN REFINED FURTHER USING REFINE FROM
REMARK 3 PHENIX. SOME IMPROVEMENTS, SUCH AS ADDITION OF AA 241-244 AT THE
REMARK 3 CLEAVAGE SITE WERE MADE IN REFINE. THE RESTRAINTS FOR THE
REMARK 3 DIGLYCERIDE SUBSTRATE WERE MADE IN THE GRADE SERVER. WATERS WERE
REMARK 3 ADDED BY HAND.
REMARK 4
REMARK 4 6XOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1000250512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 6.0 - 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X CDTE 1M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58358
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 31.00
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.04900
REMARK 200 FOR THE DATA SET : 42.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 14.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : 0.36000
REMARK 200 FOR SHELL : 2.600
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: 4EA6
REMARK 200
REMARK 200 REMARK: THIN NEEDLES OF INDETERMINATE CROSS SECTION
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY VAPOR DIFFUSION
REMARK 280 AT ROOM TEMPERATURE IN 24 WELL CRYSCHEM SITTING DROP PLATES
REMARK 280 (HAMPTON RESEARCH, ALISO VIEJO, CA) WITH 600 MICROLETERS
REMARK 280 RESERVOIRS OF 25% PEG 3350 IN 0.10 M MES BUFFER AT PH 6.5. THE
REMARK 280 PROTEIN DROPLETS WERE OF 8UL VOLUME AND CONSISTED OF EQUAL PARTS
REMARK 280 OF A 20 TO 30 MG/ML PROTEIN STOCK SOLUTION AND THE RESERVOIR
REMARK 280 SOLUTION. CRYSTALS USUALLY APPEARED AND GREW TO FULL SIZE WITHIN
REMARK 280 ONE TO TWO WEEKS. RHOMBOHEDRAL CRYSTALS WERE THIN NEEDLES OF
REMARK 280 INDETERMINATE CROSS-SECTION, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 38.18650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 22.04699
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 80.51700
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 38.18650
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 22.04699
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 80.51700
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 38.18650
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 22.04699
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 80.51700
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 38.18650
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 22.04699
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 80.51700
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 38.18650
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 22.04699
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 80.51700
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 38.18650
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 22.04699
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.51700
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 44.09397
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 161.03400
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 44.09397
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 161.03400
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 44.09397
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 161.03400
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 44.09397
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 161.03400
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 44.09397
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 161.03400
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 44.09397
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 161.03400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -214.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 P PO4 A 307 LIES ON A SPECIAL POSITION.
REMARK 375 O3 PO4 A 307 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 686 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 801 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 816 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 819 LIES ON A SPECIAL POSITION.
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 -21
REMARK 465 ARG A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 LEU A -17
REMARK 465 VAL A -16
REMARK 465 LEU A -15
REMARK 465 PHE A -14
REMARK 465 PHE A -13
REMARK 465 VAL A -12
REMARK 465 SER A -11
REMARK 465 ALA A -10
REMARK 465 TRP A -9
REMARK 465 THR A -8
REMARK 465 ALA A -7
REMARK 465 LEU A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 PRO A -3
REMARK 465 ILE A -2
REMARK 465 ARG A -1
REMARK 465 ARG A 0
REMARK 465 GLY A 245
REMARK 465 GLY A 246
REMARK 465 ASN A 247
REMARK 465 ASN A 248
REMARK 465 GLN A 249
REMARK 465 PRO A 250
REMARK 465 ASN A 251
REMARK 465 ILE A 252
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 THR A 244 CB OG1 CG2
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 HG SER A 146 O HOH A 402 1.26
REMARK 500 HG SER A 83 O HOH A 402 1.49
REMARK 500 HE ARG A 179 OE2 GLU A 183 1.59
REMARK 500 OD1 ASP A 102 O HOH A 401 1.86
REMARK 500 O HOH A 739 O HOH A 765 1.97
REMARK 500 OG SER A 146 O HOH A 402 2.05
REMARK 500 O HOH A 413 O HOH A 612 2.12
REMARK 500 O HOH A 470 O HOH A 733 2.12
REMARK 500 OD1 ASN A 233 O HOH A 403 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ILE A 241 O HOH A 698 5555 1.85
REMARK 500 O HOH A 475 O HOH A 613 5555 1.91
REMARK 500 O HOH A 462 O HOH A 462 5555 2.09
REMARK 500 O HOH A 761 O HOH A 818 3555 2.13
REMARK 500 O HOH A 767 O HOH A 817 3555 2.14
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 A 241 N - CA - C ANGL. DEV. = 19.2 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 CYS A 36 -154.59 -121.89
REMARK 500 CYS A 41 54.86 -149.87
REMARK 500 ARG A 84 -48.50 -136.65
REMARK 500 SER A 146 -130.08 61.43
REMARK 500 SER A 146 -128.74 59.26
REMARK 500 LEU A 227 -0.46 72.90
REMARK 500 ILE A 241 22.43 30.52
REMARK 500 ASP A 242 -65.79 -154.13
REMARK 500 PHE A 262 -41.25 74.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 243 THR A 244 -123.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 808 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A 809 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 810 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 812 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 813 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A 814 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 815 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A 816 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 817 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 819 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH A 821 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH A 822 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH A 823 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH A 824 DISTANCE = 8.89 ANGSTROMS
REMARK 525 HOH A 825 DISTANCE = 9.23 ANGSTROMS
REMARK 525 HOH A 826 DISTANCE = 12.20 ANGSTROMS
REMARK 525 HOH A 827 DISTANCE = 15.02 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 455
DBREF 6XOK A -21 269 UNP O59952 LIP_THELA 1 291
SEQADV 6XOK LEU A 86 UNP O59952 ILE 108 CONFLICT
SEQRES 1 A 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 A 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 A 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 A 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 A 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 A 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 A 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 A 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 A 291 SER ARG SER LEU GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 A 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 A 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 A 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 A 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 A 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 A 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 A 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 A 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 A 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 A 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 A 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 A 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 A 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 A 291 ILE GLY THR CYS LEU
HET NAG A 301 27
HET PG4 A 302 61
HET PO4 A 303 5
HET PO4 A 304 5
HET PO4 A 305 5
HET PO4 A 306 5
HET PO4 A 307 5
HET PO4 A 308 5
HET LTV A 309 51
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PO4 PHOSPHATE ION
HETNAM LTV 2-HYDROXY-3-(OCTADECANOYLOXY)PROPYL PENTACOSANOATE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 PO4 6(O4 P 3-)
FORMUL 10 LTV C46 H90 O5
FORMUL 11 HOH *427(H2 O)
HELIX 1 AA1 SER A 3 ALA A 20 1 18
HELIX 2 AA2 TYR A 21 ASN A 26 5 6
HELIX 3 AA3 CYS A 41 ALA A 47 1 7
HELIX 4 AA4 SER A 85 LEU A 93 1 9
HELIX 5 AA5 ASP A 111 HIS A 135 1 25
HELIX 6 AA6 SER A 146 ARG A 160 1 15
HELIX 7 AA7 ASN A 178 GLN A 188 1 11
HELIX 8 AA8 ILE A 202 LEU A 206 5 5
HELIX 9 AA9 PRO A 208 GLY A 212 5 5
HELIX 10 AB1 THR A 231 ASN A 233 5 3
HELIX 11 AB2 ASP A 254 TRP A 260 1 7
SHEET 1 AA1 8 ALA A 49 SER A 58 0
SHEET 2 AA1 8 VAL A 63 ASP A 70 -1 O LEU A 67 N TYR A 53
SHEET 3 AA1 8 LEU A 75 PHE A 80 -1 O VAL A 77 N ALA A 68
SHEET 4 AA1 8 ARG A 139 HIS A 145 1 O VAL A 141 N ILE A 76
SHEET 5 AA1 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA1 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 AA1 8 GLU A 219 ILE A 222 1 O ILE A 222 N THR A 197
SHEET 8 AA1 8 ILE A 235 ILE A 238 -1 O ILE A 238 N GLU A 219
SHEET 1 AA2 2 LEU A 97 GLU A 99 0
SHEET 2 AA2 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.09
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.04
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.05
LINK ND2 ASN A 33 C1 NAG A 301 1555 1555 1.42
CISPEP 1 LEU A 206 PRO A 207 0 -15.57
CISPEP 2 SER A 217 PRO A 218 0 -2.61
CRYST1 76.373 76.373 241.551 90.00 90.00 120.00 H 3 2 18
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 0.013094 0.007560 0.000000 0.00000
SCALE2 0.000000 0.015119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004140 0.00000
TER 4269 LEU A 269
MASTER 497 0 9 11 10 0 0 6 2550 1 176 23
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