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HEADER HYDROLASE 13-MAR-19 6O9F
TITLE THE STRUCTURE OF THERMOMYCES LANUGINOSA LIPASE IN COMPLEX WITH 1,3
TITLE 2 DIACYLGLYCEROL IN A MONOCLINIC CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, E, D, F;
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: THERMOACTINOMYCES VULGARIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 2026
KEYWDS LIPIDS, TRIGLYCERIDES, CATALYTIC TRIAD, MONOLAYER, ACYL INTERMEDIATE,
KEYWDS 2 TRIMER, NCS, LIPID BINDING PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 01-MAY-24 6O9F 0
JRNL AUTH A.MCPHERSON,B.S.LARSON,A.KALASKY
JRNL TITL THE CRYSTAL STRUCTURES OF THERMOMYCES (HUMICOLA) LANUGINOSA
JRNL TITL 2 LIPASE IN COMPLEX WITH ENZYMATIC REACTANTS
JRNL REF CURR ENZYM INHIB V. 16 199 2020
JRNL REFN ESSN 1875-6662
JRNL DOI HTTP://DX.DOI.ORG/10.2174/1573408016999200511090910
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19RC7_4070
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 61661
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 3025
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 51.2700 - 6.9500 1.00 2751 151 0.1587 0.1662
REMARK 3 2 6.9400 - 5.5100 1.00 2717 131 0.1505 0.1795
REMARK 3 3 5.5100 - 4.8200 1.00 2703 126 0.1287 0.1616
REMARK 3 4 4.8200 - 4.3800 1.00 2711 145 0.1137 0.1712
REMARK 3 5 4.3800 - 4.0600 1.00 2682 133 0.1269 0.1563
REMARK 3 6 4.0600 - 3.8300 1.00 2685 128 0.1366 0.1990
REMARK 3 7 3.8200 - 3.6300 1.00 2685 125 0.1397 0.1751
REMARK 3 8 3.6300 - 3.4800 1.00 2704 124 0.1512 0.1801
REMARK 3 9 3.4800 - 3.3400 1.00 2658 144 0.1736 0.2202
REMARK 3 10 3.3400 - 3.2300 1.00 2675 137 0.1741 0.2360
REMARK 3 11 3.2300 - 3.1300 1.00 2653 141 0.1820 0.2333
REMARK 3 12 3.1300 - 3.0400 1.00 2677 134 0.1885 0.2230
REMARK 3 13 3.0400 - 2.9600 1.00 2650 153 0.1963 0.2429
REMARK 3 14 2.9600 - 2.8800 1.00 2672 143 0.2027 0.2550
REMARK 3 15 2.8800 - 2.8200 1.00 2652 137 0.2203 0.2504
REMARK 3 16 2.8200 - 2.7600 1.00 2647 147 0.2321 0.2537
REMARK 3 17 2.7600 - 2.7000 1.00 2648 142 0.2404 0.2892
REMARK 3 18 2.7000 - 2.6500 0.99 2659 147 0.2506 0.2876
REMARK 3 19 2.6500 - 2.6000 0.99 2627 135 0.2586 0.3019
REMARK 3 20 2.6000 - 2.5600 0.99 2683 121 0.2709 0.3353
REMARK 3 21 2.5600 - 2.5200 0.98 2564 150 0.2893 0.2794
REMARK 3 22 2.5200 - 2.4800 0.94 2533 131 0.3072 0.3471
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) : 0.321
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.021
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.59
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 : 0.003 13396
REMARK 3 ANGLE : 0.521 18197
REMARK 3 CHIRALITY : 0.042 1945
REMARK 3 PLANARITY : 0.004 2398
REMARK 3 DIHEDRAL : 14.449 4951
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 6O9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 6.0 - 7.5
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 : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5419
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81074
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.29200
REMARK 200 R SYM (I) : 0.24500
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 1.02000
REMARK 200 R SYM FOR SHELL (I) : 0.85000
REMARK 200 FOR SHELL : 1.300
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: THICK EQUIDIMENSIONAL BLOCKS 0.25 TO 0.50 MM EDGE LENGTHS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOURCE WAS A FILTERED FUNGAL
REMARK 280 CULTURE MEDIUM AT ABOUT 50 MG/ML. THIS WAS COMBINED IN 8 UL
REMARK 280 DROPS WITH EQUAL AMOUNTS OF 25% PEG 3350 BUFFERED AT PH 6.5 WITH
REMARK 280 0.10 M MES AND CRYSTALLIZED AT ROOM TEMPERATURE BY SITTING DROPS
REMARK 280 IN CRYSCHEM PLATES, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 45.68300
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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 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 MET B -21
REMARK 465 ARG B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 LEU B -17
REMARK 465 VAL B -16
REMARK 465 LEU B -15
REMARK 465 PHE B -14
REMARK 465 PHE B -13
REMARK 465 VAL B -12
REMARK 465 SER B -11
REMARK 465 ALA B -10
REMARK 465 TRP B -9
REMARK 465 THR B -8
REMARK 465 ALA B -7
REMARK 465 LEU B -6
REMARK 465 ALA B -5
REMARK 465 SER B -4
REMARK 465 PRO B -3
REMARK 465 ILE B -2
REMARK 465 ARG B -1
REMARK 465 ARG B 0
REMARK 465 MET C -21
REMARK 465 ARG C -20
REMARK 465 SER C -19
REMARK 465 SER C -18
REMARK 465 LEU C -17
REMARK 465 VAL C -16
REMARK 465 LEU C -15
REMARK 465 PHE C -14
REMARK 465 PHE C -13
REMARK 465 VAL C -12
REMARK 465 SER C -11
REMARK 465 ALA C -10
REMARK 465 TRP C -9
REMARK 465 THR C -8
REMARK 465 ALA C -7
REMARK 465 LEU C -6
REMARK 465 ALA C -5
REMARK 465 SER C -4
REMARK 465 PRO C -3
REMARK 465 ILE C -2
REMARK 465 ARG C -1
REMARK 465 ARG C 0
REMARK 465 MET E -21
REMARK 465 ARG E -20
REMARK 465 SER E -19
REMARK 465 SER E -18
REMARK 465 LEU E -17
REMARK 465 VAL E -16
REMARK 465 LEU E -15
REMARK 465 PHE E -14
REMARK 465 PHE E -13
REMARK 465 VAL E -12
REMARK 465 SER E -11
REMARK 465 ALA E -10
REMARK 465 TRP E -9
REMARK 465 THR E -8
REMARK 465 ALA E -7
REMARK 465 LEU E -6
REMARK 465 ALA E -5
REMARK 465 SER E -4
REMARK 465 PRO E -3
REMARK 465 ILE E -2
REMARK 465 ARG E -1
REMARK 465 ARG E 0
REMARK 465 MET D -21
REMARK 465 ARG D -20
REMARK 465 SER D -19
REMARK 465 SER D -18
REMARK 465 LEU D -17
REMARK 465 VAL D -16
REMARK 465 LEU D -15
REMARK 465 PHE D -14
REMARK 465 PHE D -13
REMARK 465 VAL D -12
REMARK 465 SER D -11
REMARK 465 ALA D -10
REMARK 465 TRP D -9
REMARK 465 THR D -8
REMARK 465 ALA D -7
REMARK 465 LEU D -6
REMARK 465 ALA D -5
REMARK 465 SER D -4
REMARK 465 PRO D -3
REMARK 465 ILE D -2
REMARK 465 ARG D -1
REMARK 465 ARG D 0
REMARK 465 MET F -21
REMARK 465 ARG F -20
REMARK 465 SER F -19
REMARK 465 SER F -18
REMARK 465 LEU F -17
REMARK 465 VAL F -16
REMARK 465 LEU F -15
REMARK 465 PHE F -14
REMARK 465 PHE F -13
REMARK 465 VAL F -12
REMARK 465 SER F -11
REMARK 465 ALA F -10
REMARK 465 TRP F -9
REMARK 465 THR F -8
REMARK 465 ALA F -7
REMARK 465 LEU F -6
REMARK 465 ALA F -5
REMARK 465 SER F -4
REMARK 465 PRO F -3
REMARK 465 ILE F -2
REMARK 465 ARG F -1
REMARK 465 ARG F 0
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA A 173 CB
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 NE2 HIS E 258 O1 OCA E 301 1.30
REMARK 500 O SER E 83 C6 OCA E 301 1.37
REMARK 500 C5 OCA B 301 C33 LTV B 306 1.49
REMARK 500 C5 OCA D 301 C31 LTV D 304 1.49
REMARK 500 OG SER F 146 O1 OCA F 301 1.75
REMARK 500 O HOH A 401 O HOH A 415 1.85
REMARK 500 OD1 ASP A 57 O HOH A 401 1.97
REMARK 500 CD2 HIS E 258 O1 OCA E 301 2.01
REMARK 500 C5 OCA B 301 C32 LTV B 306 2.01
REMARK 500 O4 PO4 D 305 O HOH D 401 2.01
REMARK 500 OD1 ASP B 57 O HOH B 401 2.04
REMARK 500 OE1 GLU D 87 O HOH D 401 2.04
REMARK 500 O THR B 244 O HOH B 402 2.06
REMARK 500 O HOH E 404 O HOH E 420 2.07
REMARK 500 CB SER F 146 C1 OCA F 301 2.07
REMARK 500 O HOH A 409 O HOH A 415 2.08
REMARK 500 O HOH A 401 O HOH A 404 2.09
REMARK 500 O ALA B 30 O HOH B 403 2.09
REMARK 500 O HOH E 446 O HOH E 450 2.09
REMARK 500 OXT LEU C 269 O HOH C 401 2.10
REMARK 500 OG SER D 146 O1 OCA D 301 2.11
REMARK 500 OG SER A 146 C2 OCA A 301 2.11
REMARK 500 OXT LEU F 269 O HOH F 401 2.11
REMARK 500 OG1 THR A 37 O HOH A 402 2.12
REMARK 500 OD1 ASP C 48 O HOH C 402 2.13
REMARK 500 OD1 ASP F 57 O HOH F 402 2.13
REMARK 500 OD1 ASP B 57 O HOH B 404 2.15
REMARK 500 OG SER B 146 O2 OCA B 301 2.16
REMARK 500 O3 PO4 A 305 O HOH A 403 2.17
REMARK 500 OE2 GLU D 45 O HOH D 402 2.18
REMARK 500 C4 OCA B 301 C33 LTV B 306 2.18
REMARK 500 O HOH B 401 O HOH B 404 2.19
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 ARG A 84 -40.29 -138.53
REMARK 500 SER A 146 -124.00 61.49
REMARK 500 THR A 199 -119.39 35.56
REMARK 500 PHE A 262 -37.25 75.39
REMARK 500 ASN B 39 34.02 -93.70
REMARK 500 ARG B 84 -48.19 -145.86
REMARK 500 SER B 146 -130.63 62.62
REMARK 500 THR B 199 -119.07 37.11
REMARK 500 ASN B 251 -164.96 -76.31
REMARK 500 PHE B 262 -40.72 72.73
REMARK 500 ASP C 27 33.53 -141.55
REMARK 500 ASN C 39 34.98 -95.33
REMARK 500 ASP C 62 63.17 63.47
REMARK 500 ARG C 84 -43.71 -140.12
REMARK 500 SER C 146 -121.64 56.00
REMARK 500 THR C 199 -115.61 30.85
REMARK 500 PHE C 262 -42.55 75.26
REMARK 500 ASN E 39 38.00 -98.48
REMARK 500 ARG E 84 -47.85 -145.76
REMARK 500 SER E 146 -125.19 62.31
REMARK 500 THR E 199 -122.47 34.91
REMARK 500 PHE E 262 -35.63 73.93
REMARK 500 ASP D 27 38.15 -145.94
REMARK 500 ASN D 39 41.59 -100.66
REMARK 500 ARG D 84 -44.42 -148.34
REMARK 500 SER D 146 -130.94 59.81
REMARK 500 THR D 199 -118.24 34.66
REMARK 500 ASN D 251 -168.14 -112.04
REMARK 500 PHE D 262 -43.36 70.32
REMARK 500 ASP F 27 66.46 -153.59
REMARK 500 ARG F 84 -45.32 -142.38
REMARK 500 SER F 146 -125.53 61.45
REMARK 500 THR F 199 -119.42 36.38
REMARK 500 PRO F 250 45.54 -83.57
REMARK 500 PHE F 262 -28.37 74.41
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 F 482 DISTANCE = 8.71 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 LTV A 304
REMARK 610 LTV B 306
REMARK 610 OCA C 301
REMARK 610 NAG C 304
REMARK 610 LTV C 305
REMARK 610 NAG E 303
REMARK 610 LTV E 304
REMARK 610 NAG D 303
REMARK 610 OCA F 301
REMARK 610 NAG F 303
REMARK 610 LTV F 304
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 45 O
REMARK 620 2 ALA A 47 O 69.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 45 O
REMARK 620 2 ALA B 47 O 74.0
REMARK 620 3 HOH B 414 O 90.0 64.9
REMARK 620 4 HOH B 421 O 75.6 71.2 136.1
REMARK 620 5 HOH B 446 O 147.0 83.9 102.6 74.3
REMARK 620 6 HOH B 452 O 89.0 134.4 159.0 63.6 89.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 62 OD2
REMARK 620 2 HOH B 401 O 53.9
REMARK 620 3 HOH B 404 O 104.9 54.0
REMARK 620 4 HOH B 406 O 61.2 58.1 65.9
REMARK 620 5 HOH B 468 O 120.9 157.4 133.6 142.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 45 O
REMARK 620 2 ALA C 47 O 75.8
REMARK 620 3 HOH C 408 O 96.1 64.1
REMARK 620 4 HOH C 433 O 150.4 82.6 92.4
REMARK 620 5 HOH C 450 O 90.3 69.4 129.7 63.0
REMARK 620 6 HOH C 471 O 93.2 144.3 151.6 92.6 76.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 404 O
REMARK 620 2 HOH C 459 O 50.4
REMARK 620 3 HOH C 475 O 113.5 68.7
REMARK 620 4 HOH C 478 O 121.8 127.6 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 45 O
REMARK 620 2 ALA E 47 O 66.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 45 O
REMARK 620 2 ALA D 47 O 70.7
REMARK 620 3 HOH D 423 O 76.3 71.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 45 O
REMARK 620 2 ALA F 47 O 74.5
REMARK 620 3 HOH F 415 O 86.0 84.1
REMARK 620 N 1 2
DBREF 6O9F A -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6O9F B -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6O9F C -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6O9F E -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6O9F D -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6O9F F -21 269 UNP O59952 LIP_THELA 1 291
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 ILE 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
SEQRES 1 B 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 B 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 B 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 B 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 B 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 B 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 B 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 B 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 B 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 B 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 B 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 B 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 B 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 B 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 B 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 B 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 B 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 B 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 B 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 B 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 B 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 B 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 B 291 ILE GLY THR CYS LEU
SEQRES 1 C 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 C 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 C 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 C 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 C 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 C 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 C 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 C 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 C 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 C 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 C 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 C 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 C 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 C 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 C 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 C 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 C 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 C 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 C 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 C 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 C 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 C 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 C 291 ILE GLY THR CYS LEU
SEQRES 1 E 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 E 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 E 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 E 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 E 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 E 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 E 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 E 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 E 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 E 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 E 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 E 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 E 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 E 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 E 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 E 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 E 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 E 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 E 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 E 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 E 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 E 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 E 291 ILE GLY THR CYS LEU
SEQRES 1 D 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 D 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 D 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 D 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 D 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 D 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 D 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 D 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 D 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 D 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 D 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 D 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 D 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 D 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 D 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 D 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 D 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 D 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 D 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 D 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 D 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 D 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 D 291 ILE GLY THR CYS LEU
SEQRES 1 F 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 F 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 F 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 F 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 F 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 F 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 F 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 F 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 F 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 F 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 F 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 F 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 F 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 F 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 F 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 F 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 F 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 F 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 F 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 F 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 F 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 F 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 F 291 ILE GLY THR CYS LEU
HET OCA A 301 9
HET CA A 302 1
HET NAG A 303 27
HET LTV A 304 36
HET PO4 A 305 5
HET OCA B 301 9
HET PO4 B 302 5
HET CA B 303 1
HET CA B 304 1
HET NAG B 305 27
HET LTV B 306 43
HET PO4 B 307 5
HET OCA C 301 9
HET CA C 302 1
HET CA C 303 1
HET NAG C 304 27
HET LTV C 305 41
HET OCA E 301 9
HET CA E 302 1
HET NAG E 303 27
HET LTV E 304 48
HET PO4 E 305 5
HET OCA D 301 9
HET CA D 302 1
HET NAG D 303 27
HET LTV D 304 51
HET PO4 D 305 5
HET OCA F 301 7
HET CA F 302 1
HET NAG F 303 27
HET LTV F 304 43
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
HETNAM CA CALCIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM LTV 2-HYDROXY-3-(OCTADECANOYLOXY)PROPYL PENTACOSANOATE
HETNAM PO4 PHOSPHATE ION
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 7 OCA 6(C8 H16 O2)
FORMUL 8 CA 8(CA 2+)
FORMUL 9 NAG 6(C8 H15 N O6)
FORMUL 10 LTV 6(C46 H90 O5)
FORMUL 11 PO4 5(O4 P 3-)
FORMUL 38 HOH *428(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 ILE A 255 TRP A 260 5 6
HELIX 12 AB3 SER B 3 ALA B 20 1 18
HELIX 13 AB4 TYR B 21 ASN B 26 5 6
HELIX 14 AB5 CYS B 41 ALA B 47 1 7
HELIX 15 AB6 SER B 85 LEU B 93 1 9
HELIX 16 AB7 ASP B 111 HIS B 135 1 25
HELIX 17 AB8 SER B 146 ARG B 160 1 15
HELIX 18 AB9 ASN B 178 GLN B 188 1 11
HELIX 19 AC1 ILE B 202 LEU B 206 5 5
HELIX 20 AC2 PRO B 208 GLY B 212 5 5
HELIX 21 AC3 THR B 231 ASN B 233 5 3
HELIX 22 AC4 ILE B 255 TRP B 260 5 6
HELIX 23 AC5 SER C 3 ALA C 20 1 18
HELIX 24 AC6 TYR C 21 ASN C 26 5 6
HELIX 25 AC7 CYS C 41 ALA C 47 1 7
HELIX 26 AC8 SER C 85 ASN C 94 1 10
HELIX 27 AC9 ASP C 111 SER C 119 1 9
HELIX 28 AD1 VAL C 120 HIS C 135 1 16
HELIX 29 AD2 SER C 146 ARG C 160 1 15
HELIX 30 AD3 ASN C 178 GLN C 188 1 11
HELIX 31 AD4 ILE C 202 LEU C 206 5 5
HELIX 32 AD5 PRO C 208 GLY C 212 5 5
HELIX 33 AD6 ILE C 255 TRP C 260 5 6
HELIX 34 AD7 SER E 3 ALA E 20 1 18
HELIX 35 AD8 TYR E 21 ASP E 27 5 7
HELIX 36 AD9 CYS E 41 ALA E 47 1 7
HELIX 37 AE1 SER E 85 LEU E 93 1 9
HELIX 38 AE2 ASP E 111 HIS E 135 1 25
HELIX 39 AE3 SER E 146 ARG E 160 1 15
HELIX 40 AE4 ASN E 178 GLN E 188 1 11
HELIX 41 AE5 ILE E 202 LEU E 206 5 5
HELIX 42 AE6 PRO E 208 GLY E 212 5 5
HELIX 43 AE7 THR E 231 ASN E 233 5 3
HELIX 44 AE8 ILE E 255 TRP E 260 5 6
HELIX 45 AE9 SER D 3 ALA D 20 1 18
HELIX 46 AF1 TYR D 21 ASN D 26 5 6
HELIX 47 AF2 CYS D 41 ALA D 47 1 7
HELIX 48 AF3 SER D 85 ASN D 94 1 10
HELIX 49 AF4 ASP D 111 HIS D 135 1 25
HELIX 50 AF5 SER D 146 ARG D 160 1 15
HELIX 51 AF6 ASN D 178 GLN D 188 1 11
HELIX 52 AF7 ILE D 202 LEU D 206 5 5
HELIX 53 AF8 PRO D 208 GLY D 212 5 5
HELIX 54 AF9 ILE D 255 TRP D 260 5 6
HELIX 55 AG1 SER F 3 ALA F 20 1 18
HELIX 56 AG2 TYR F 21 ASP F 27 5 7
HELIX 57 AG3 CYS F 41 ALA F 47 1 7
HELIX 58 AG4 SER F 85 LEU F 93 1 9
HELIX 59 AG5 ASP F 111 SER F 119 1 9
HELIX 60 AG6 VAL F 120 HIS F 135 1 16
HELIX 61 AG7 SER F 146 ARG F 160 1 15
HELIX 62 AG8 ASN F 178 GLN F 188 1 11
HELIX 63 AG9 ILE F 202 LEU F 206 5 5
HELIX 64 AH1 PRO F 208 GLY F 212 5 5
HELIX 65 AH2 THR F 231 ASN F 233 5 3
HELIX 66 AH3 ILE F 255 TRP F 260 5 6
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 TYR A 220 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
SHEET 1 AA3 8 ALA B 49 SER B 58 0
SHEET 2 AA3 8 VAL B 63 ASP B 70 -1 O LEU B 67 N TYR B 53
SHEET 3 AA3 8 LEU B 75 PHE B 80 -1 O VAL B 77 N ALA B 68
SHEET 4 AA3 8 ARG B 139 HIS B 145 1 O VAL B 141 N ILE B 76
SHEET 5 AA3 8 ILE B 166 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 AA3 8 LEU B 193 HIS B 198 1 O TYR B 194 N VAL B 168
SHEET 7 AA3 8 GLU B 219 ILE B 222 1 O ILE B 222 N THR B 197
SHEET 8 AA3 8 ILE B 235 ILE B 238 -1 O ILE B 238 N GLU B 219
SHEET 1 AA4 2 LEU B 97 GLU B 99 0
SHEET 2 AA4 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SHEET 1 AA5 8 ALA C 49 SER C 58 0
SHEET 2 AA5 8 VAL C 63 ASP C 70 -1 O LEU C 67 N TYR C 53
SHEET 3 AA5 8 LEU C 75 PHE C 80 -1 O VAL C 77 N ALA C 68
SHEET 4 AA5 8 ARG C 139 HIS C 145 1 O ARG C 139 N ILE C 76
SHEET 5 AA5 8 ILE C 166 TYR C 171 1 O ASP C 167 N PHE C 142
SHEET 6 AA5 8 LEU C 193 HIS C 198 1 O TYR C 194 N VAL C 168
SHEET 7 AA5 8 GLU C 219 ILE C 222 1 O TYR C 220 N ARG C 195
SHEET 8 AA5 8 ILE C 235 ILE C 238 -1 O ILE C 238 N GLU C 219
SHEET 1 AA6 2 LEU C 97 GLU C 99 0
SHEET 2 AA6 2 ARG C 108 HIS C 110 -1 O GLY C 109 N LYS C 98
SHEET 1 AA7 8 ALA E 49 SER E 58 0
SHEET 2 AA7 8 VAL E 63 ASP E 70 -1 O LEU E 67 N LEU E 52
SHEET 3 AA7 8 LEU E 75 PHE E 80 -1 O VAL E 77 N ALA E 68
SHEET 4 AA7 8 ARG E 139 HIS E 145 1 O ARG E 139 N ILE E 76
SHEET 5 AA7 8 ILE E 166 TYR E 171 1 O ASP E 167 N PHE E 142
SHEET 6 AA7 8 LEU E 193 HIS E 198 1 O TYR E 194 N VAL E 168
SHEET 7 AA7 8 GLU E 219 ILE E 222 1 O TYR E 220 N ARG E 195
SHEET 8 AA7 8 ILE E 235 ILE E 238 -1 O VAL E 236 N TRP E 221
SHEET 1 AA8 2 LEU E 97 GLU E 99 0
SHEET 2 AA8 2 ARG E 108 HIS E 110 -1 O GLY E 109 N LYS E 98
SHEET 1 AA9 8 ALA D 49 SER D 58 0
SHEET 2 AA9 8 VAL D 63 ASP D 70 -1 O LEU D 67 N LEU D 52
SHEET 3 AA9 8 LEU D 75 PHE D 80 -1 O VAL D 77 N ALA D 68
SHEET 4 AA9 8 ARG D 139 HIS D 145 1 O THR D 143 N LEU D 78
SHEET 5 AA9 8 ILE D 166 TYR D 171 1 O ASP D 167 N PHE D 142
SHEET 6 AA9 8 LEU D 193 HIS D 198 1 O TYR D 194 N VAL D 168
SHEET 7 AA9 8 GLU D 219 ILE D 222 1 O ILE D 222 N THR D 197
SHEET 8 AA9 8 ILE D 235 ILE D 238 -1 O VAL D 236 N TRP D 221
SHEET 1 AB1 2 LEU D 97 GLU D 99 0
SHEET 2 AB1 2 ARG D 108 HIS D 110 -1 O GLY D 109 N LYS D 98
SHEET 1 AB2 8 ALA F 49 SER F 58 0
SHEET 2 AB2 8 VAL F 63 ASP F 70 -1 O LEU F 67 N TYR F 53
SHEET 3 AB2 8 LEU F 75 PHE F 80 -1 O VAL F 77 N ALA F 68
SHEET 4 AB2 8 ARG F 139 HIS F 145 1 O VAL F 141 N ILE F 76
SHEET 5 AB2 8 ILE F 166 TYR F 171 1 O ASP F 167 N PHE F 142
SHEET 6 AB2 8 LEU F 193 HIS F 198 1 O TYR F 194 N VAL F 168
SHEET 7 AB2 8 GLU F 219 ILE F 222 1 O ILE F 222 N THR F 197
SHEET 8 AB2 8 ILE F 235 ILE F 238 -1 O ILE F 238 N GLU F 219
SHEET 1 AB3 2 LEU F 97 GLU F 99 0
SHEET 2 AB3 2 ARG F 108 HIS F 110 -1 O GLY F 109 N LYS F 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.03
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.03
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.03
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.03
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.03
SSBOND 7 CYS C 22 CYS C 268 1555 1555 2.03
SSBOND 8 CYS C 36 CYS C 41 1555 1555 2.03
SSBOND 9 CYS C 104 CYS C 107 1555 1555 2.03
SSBOND 10 CYS E 22 CYS E 268 1555 1555 2.03
SSBOND 11 CYS E 36 CYS E 41 1555 1555 2.03
SSBOND 12 CYS E 104 CYS E 107 1555 1555 2.03
SSBOND 13 CYS D 22 CYS D 268 1555 1555 2.03
SSBOND 14 CYS D 36 CYS D 41 1555 1555 2.03
SSBOND 15 CYS D 104 CYS D 107 1555 1555 2.03
SSBOND 16 CYS F 22 CYS F 268 1555 1555 2.03
SSBOND 17 CYS F 36 CYS F 41 1555 1555 2.03
SSBOND 18 CYS F 104 CYS F 107 1555 1555 2.03
LINK ND2 ASN A 33 C1 NAG A 303 1555 1555 1.43
LINK OG SER A 146 C1 OCA A 301 1555 1555 1.38
LINK ND2 ASN B 33 C1 NAG B 305 1555 1555 1.43
LINK OG SER B 146 C1 OCA B 301 1555 1555 1.38
LINK OG SER E 146 C1 OCA E 301 1555 1555 1.38
LINK OG SER D 146 C1 OCA D 301 1555 1555 1.38
LINK OG SER F 146 C1 OCA F 301 1555 1555 1.38
LINK O GLU A 45 CA CA A 302 1555 1555 2.60
LINK O ALA A 47 CA CA A 302 1555 1555 2.64
LINK O GLU B 45 CA CA B 303 1555 1555 2.49
LINK O ALA B 47 CA CA B 303 1555 1555 2.48
LINK OD2 ASP B 62 CA CA B 304 1555 1555 3.12
LINK CA CA B 303 O HOH B 414 1555 1555 2.17
LINK CA CA B 303 O HOH B 421 1555 1555 2.66
LINK CA CA B 303 O HOH B 446 1555 1555 2.44
LINK CA CA B 303 O HOH B 452 1555 1555 2.67
LINK CA CA B 304 O HOH B 401 1555 1555 2.27
LINK CA CA B 304 O HOH B 404 1555 1555 2.53
LINK CA CA B 304 O HOH B 406 1555 1555 2.36
LINK CA CA B 304 O HOH B 468 1555 1555 2.28
LINK O GLU C 45 CA CA C 302 1555 1555 2.62
LINK O ALA C 47 CA CA C 302 1555 1555 2.64
LINK CA CA C 302 O HOH C 408 1555 1555 3.10
LINK CA CA C 302 O HOH C 433 1555 1555 2.63
LINK CA CA C 302 O HOH C 450 1555 1555 2.47
LINK CA CA C 302 O HOH C 471 1555 1555 2.41
LINK CA CA C 303 O HOH C 404 1555 1555 2.80
LINK CA CA C 303 O HOH C 459 1555 1555 3.12
LINK CA CA C 303 O HOH C 475 1555 1555 2.76
LINK CA CA C 303 O HOH C 478 1555 1555 2.77
LINK O GLU E 45 CA CA E 302 1555 1555 2.81
LINK O ALA E 47 CA CA E 302 1555 1555 2.97
LINK O GLU D 45 CA CA D 302 1555 1555 2.82
LINK O ALA D 47 CA CA D 302 1555 1555 2.60
LINK CA CA D 302 O HOH D 423 1555 1555 2.81
LINK O GLU F 45 CA CA F 302 1555 1555 2.47
LINK O ALA F 47 CA CA F 302 1555 1555 2.57
LINK CA CA F 302 O HOH F 415 1555 1555 2.47
CISPEP 1 LEU A 206 PRO A 207 0 -7.14
CISPEP 2 SER A 217 PRO A 218 0 0.15
CISPEP 3 LEU B 206 PRO B 207 0 -8.64
CISPEP 4 SER B 217 PRO B 218 0 2.78
CISPEP 5 LEU C 206 PRO C 207 0 -10.24
CISPEP 6 SER C 217 PRO C 218 0 -1.03
CISPEP 7 LEU E 206 PRO E 207 0 -10.70
CISPEP 8 SER E 217 PRO E 218 0 0.62
CISPEP 9 LEU D 206 PRO D 207 0 -11.32
CISPEP 10 SER D 217 PRO D 218 0 -0.41
CISPEP 11 LEU F 206 PRO F 207 0 -8.45
CISPEP 12 SER F 217 PRO F 218 0 -0.07
CRYST1 78.185 91.366 124.316 90.00 94.71 90.00 P 1 21 1 12
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 0.012790 0.000000 0.001053 0.00000
SCALE2 0.000000 0.010945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008071 0.00000
TER 4099 LEU A 269
TER 8207 LEU B 269
TER 12348 LEU C 269
TER 16441 LEU E 269
TER 20557 LEU D 269
TER 24689 LEU F 269
MASTER 565 0 31 66 60 0 0 613284 6 586 138
END |