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HEADER HYDROLASE 02-MAY-19 6OSZ
TITLE HIGH RESOLUTION STRUCTURE OF THE MONOCLINIC FORM OF THERMOMYCES
TITLE 2 LANUGINOSA LIPASE COMPLEXED WITH ITS CATALYTIC PRODUCTS
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: THERMOMYCES LANUGINOSUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5541
KEYWDS FATTY ACIDS, DIACYLGLYCEROL, ACYL INTERMEDIATE, LIPID BINDING
KEYWDS 2 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 01-MAY-24 6OSZ 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. 1.43 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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 306741
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 15362
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 76.6900 - 4.4400 1.00 9948 592 0.1611 0.1812
REMARK 3 2 4.4400 - 3.5300 1.00 9885 495 0.1318 0.1618
REMARK 3 3 3.5300 - 3.0800 1.00 9849 478 0.1438 0.1734
REMARK 3 4 3.0800 - 2.8000 1.00 9827 524 0.1432 0.1683
REMARK 3 5 2.8000 - 2.6000 1.00 9773 535 0.1406 0.1799
REMARK 3 6 2.6000 - 2.4500 1.00 9820 512 0.1324 0.1731
REMARK 3 7 2.4500 - 2.3200 1.00 9721 518 0.1238 0.1572
REMARK 3 8 2.3200 - 2.2200 1.00 9847 493 0.1161 0.1592
REMARK 3 9 2.2200 - 2.1400 1.00 9798 465 0.1160 0.1673
REMARK 3 10 2.1400 - 2.0600 1.00 9761 515 0.1249 0.1681
REMARK 3 11 2.0600 - 2.0000 1.00 9774 514 0.1299 0.1834
REMARK 3 12 2.0000 - 1.9400 1.00 9783 511 0.1469 0.1894
REMARK 3 13 1.9400 - 1.8900 1.00 9754 509 0.1340 0.1773
REMARK 3 14 1.8900 - 1.8400 1.00 9738 502 0.1231 0.1731
REMARK 3 15 1.8400 - 1.8000 1.00 9748 497 0.1258 0.1791
REMARK 3 16 1.8000 - 1.7600 1.00 9685 530 0.1315 0.1798
REMARK 3 17 1.7600 - 1.7300 1.00 9773 531 0.1437 0.1961
REMARK 3 18 1.7300 - 1.7000 1.00 9656 528 0.1513 0.2078
REMARK 3 19 1.7000 - 1.6700 1.00 9659 516 0.1670 0.2240
REMARK 3 20 1.6700 - 1.6400 1.00 9743 516 0.1845 0.2369
REMARK 3 21 1.6400 - 1.6100 0.99 9688 546 0.1929 0.2330
REMARK 3 22 1.6100 - 1.5900 0.99 9696 488 0.2167 0.2756
REMARK 3 23 1.5900 - 1.5600 0.99 9656 506 0.2185 0.2780
REMARK 3 24 1.5600 - 1.5400 0.99 9598 523 0.2289 0.2628
REMARK 3 25 1.5400 - 1.5200 0.99 9728 485 0.2489 0.2927
REMARK 3 26 1.5200 - 1.5000 0.99 9578 523 0.2630 0.3072
REMARK 3 27 1.5000 - 1.4800 0.98 9631 477 0.2789 0.3195
REMARK 3 28 1.4800 - 1.4600 0.98 9532 542 0.3136 0.3466
REMARK 3 29 1.4600 - 1.4500 0.98 9446 493 0.3250 0.3447
REMARK 3 30 1.4500 - 1.4300 0.95 9284 498 0.3617 0.3901
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) : 0.197
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.373
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 13401
REMARK 3 ANGLE : 0.924 18199
REMARK 3 CHIRALITY : 0.073 1946
REMARK 3 PLANARITY : 0.010 2395
REMARK 3 DIHEDRAL : 20.175 4950
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 6OSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1000241228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-19
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 6.0 - 7.5
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 307462
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 77.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 19.50
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : 0.15300
REMARK 200 FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 13.30
REMARK 200 R MERGE FOR SHELL (I) : 5.70000
REMARK 200 R SYM FOR SHELL (I) : 5.60000
REMARK 200 FOR SHELL : 0.400
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: 1TIB
REMARK 200
REMARK 200 REMARK: BLOCKS OF ABOUT EQUAL DIMENSIONS, ABOUT .30 MM EDGE
REMARK 200 LENGTHS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOR DIFFUSION AT ROOM
REMARK 280 TEMPERATURE IN 10 UL DROPS. DROPS COMPOSED OF EQUAL AMOUNTS OF
REMARK 280 STOCK PROTEIN SOLUTION, WHICH WAS APPROXIMATELY 30 MG/ML LIPASE
REMARK 280 IN THE FILTERED CULTURE MEDIA, AND THE RESERVOIR SOLUTION. THE
REMARK 280 LATTER WAS 20% PEG 3350 BUFFERED AT PH 6.5 WITH 0.10 M MES,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 44.96850
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: 7150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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: 7050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 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 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 GLU C 210 CA CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 210 C3 LTV A 303 1.37
REMARK 500 HH11 ARG A 125 O HOH A 403 1.54
REMARK 500 O HOH F 588 O HOH F 607 1.69
REMARK 500 OG SER C 83 O2 OCA C 301 1.70
REMARK 500 CD GLU A 210 C3 LTV A 303 1.80
REMARK 500 O HOH E 552 O HOH E 567 1.80
REMARK 500 O HOH F 686 O HOH F 692 1.83
REMARK 500 O HOH A 667 O HOH A 670 1.83
REMARK 500 OE2 GLU D 87 O HOH D 401 1.84
REMARK 500 O HOH C 580 O HOH C 592 1.86
REMARK 500 OD1 ASN D 94 O HOH D 402 1.89
REMARK 500 O HOH B 583 O HOH B 701 1.92
REMARK 500 O HOH A 590 O HOH A 647 1.92
REMARK 500 OD1 ASP D 130 O HOH D 403 1.93
REMARK 500 OE2 GLU A 210 C4 LTV A 303 1.96
REMARK 500 OE1 GLU B 129 O HOH B 401 1.96
REMARK 500 O GLY F 38 O HOH F 401 1.96
REMARK 500 OG SER E 146 O1 OCA E 301 1.98
REMARK 500 O HOH C 582 O HOH C 638 2.01
REMARK 500 OD1 ASN C 33 O HOH C 401 2.03
REMARK 500 O HOH F 404 O HOH F 521 2.05
REMARK 500 NH2 ARG D 125 O HOH D 404 2.05
REMARK 500 O4 PO4 B 302 O HOH B 402 2.07
REMARK 500 O HOH C 561 O HOH C 581 2.07
REMARK 500 O HOH E 404 O HOH E 490 2.08
REMARK 500 OD2 ASP F 102 O HOH F 402 2.09
REMARK 500 OE2 GLU B 210 O HOH B 403 2.10
REMARK 500 O HOH B 583 O HOH B 641 2.11
REMARK 500 O HOH C 585 O HOH C 613 2.12
REMARK 500 OD1 ASP A 57 O HOH A 401 2.13
REMARK 500 O HOH D 482 O HOH D 652 2.13
REMARK 500 O3 PO4 F 305 O HOH F 403 2.14
REMARK 500 OD1 ASN A 33 O HOH A 402 2.15
REMARK 500 O HOH B 553 O HOH B 697 2.15
REMARK 500 O HOH B 434 O HOH B 481 2.16
REMARK 500 CB SER C 83 C1 OCA C 301 2.16
REMARK 500 CB SER B 146 C1 OCA B 301 2.16
REMARK 500 O HOH C 424 O HOH C 546 2.17
REMARK 500 OD1 ASP F 57 O HOH F 404 2.17
REMARK 500 O HOH A 406 O HOH A 409 2.18
REMARK 500 OE1 GLU C 239 O HOH C 402 2.19
REMARK 500 O HOH A 417 O HOH A 578 2.19
REMARK 500 O HOH F 491 O HOH F 584 2.19
REMARK 500 NH2 ARG F 125 O HOH F 405 2.19
REMARK 500 CB SER F 146 C1 OCA F 301 2.19
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 HH22 ARG A 179 O HOH D 500 2647 1.46
REMARK 500 HZ3 LYS C 46 O HOH E 582 1455 1.55
REMARK 500 O HOH C 638 O HOH D 573 1554 1.69
REMARK 500 OE1 GLN E 4 O HOH D 629 1654 1.89
REMARK 500 NH2 ARG A 179 O HOH D 500 2647 2.04
REMARK 500 OE2 GLU B 43 O HOH F 589 1655 2.05
REMARK 500 O HOH B 694 O HOH F 710 1655 2.08
REMARK 500 OE2 GLU C 134 O HOH F 711 2646 2.15
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 41 57.12 -149.00
REMARK 500 ARG A 84 -43.83 -135.26
REMARK 500 SER A 146 -127.58 60.90
REMARK 500 THR A 189 -166.83 -100.56
REMARK 500 THR A 199 -116.98 34.33
REMARK 500 PHE A 262 -40.45 74.94
REMARK 500 ASN B 39 32.39 -97.53
REMARK 500 CYS B 41 57.78 -148.14
REMARK 500 ARG B 84 -44.95 -140.07
REMARK 500 SER B 146 -127.55 60.59
REMARK 500 THR B 199 -118.25 34.68
REMARK 500 PHE B 262 -42.68 73.15
REMARK 500 ASP C 27 33.98 -141.85
REMARK 500 ASN C 39 32.36 -98.54
REMARK 500 CYS C 41 56.17 -150.82
REMARK 500 ARG C 84 -45.76 -141.82
REMARK 500 SER C 146 -124.56 60.49
REMARK 500 THR C 199 -118.43 32.80
REMARK 500 PHE C 262 -39.89 72.40
REMARK 500 ASN E 39 36.80 -97.88
REMARK 500 CYS E 41 55.11 -146.10
REMARK 500 ARG E 84 -44.73 -138.40
REMARK 500 SER E 146 -127.83 59.96
REMARK 500 THR E 199 -119.70 33.49
REMARK 500 PHE E 262 -40.12 70.97
REMARK 500 ASP D 27 36.31 -141.86
REMARK 500 CYS D 41 57.38 -150.95
REMARK 500 ARG D 84 -43.17 -139.36
REMARK 500 SER D 146 -128.25 60.30
REMARK 500 THR D 199 -118.79 33.74
REMARK 500 PHE D 262 -43.65 69.88
REMARK 500 ASP F 27 79.81 -155.87
REMARK 500 CYS F 36 -157.44 -121.70
REMARK 500 CYS F 41 59.21 -149.29
REMARK 500 ARG F 84 -46.87 -141.02
REMARK 500 SER F 146 -127.72 59.64
REMARK 500 THR F 199 -117.01 30.38
REMARK 500 PHE F 262 -41.71 71.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG E 133 0.11 SIDE CHAIN
REMARK 500 ARG D 125 0.15 SIDE CHAIN
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 722 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 723 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 724 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A 725 DISTANCE = 9.67 ANGSTROMS
REMARK 525 HOH B 722 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 723 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH B 724 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH B 725 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH B 726 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH B 727 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH B 728 DISTANCE = 8.53 ANGSTROMS
REMARK 525 HOH B 729 DISTANCE = 9.21 ANGSTROMS
REMARK 525 HOH B 730 DISTANCE = 11.18 ANGSTROMS
REMARK 525 HOH C 659 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH C 660 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH C 661 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH C 662 DISTANCE = 9.94 ANGSTROMS
REMARK 525 HOH C 663 DISTANCE = 10.45 ANGSTROMS
REMARK 525 HOH C 664 DISTANCE = 10.74 ANGSTROMS
REMARK 525 HOH E 620 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH E 621 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH E 622 DISTANCE = 8.49 ANGSTROMS
REMARK 525 HOH E 623 DISTANCE = 9.97 ANGSTROMS
REMARK 525 HOH E 624 DISTANCE = 10.52 ANGSTROMS
REMARK 525 HOH D 657 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH D 658 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH D 659 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH D 660 DISTANCE = 10.25 ANGSTROMS
REMARK 525 HOH F 714 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH F 715 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH F 716 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH F 717 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH F 718 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH F 719 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH F 720 DISTANCE = 8.16 ANGSTROMS
REMARK 525 HOH F 721 DISTANCE = 8.68 ANGSTROMS
REMARK 525 HOH F 722 DISTANCE = 8.86 ANGSTROMS
REMARK 525 HOH F 723 DISTANCE = 10.29 ANGSTROMS
REMARK 525 HOH F 724 DISTANCE = 10.66 ANGSTROMS
REMARK 525 HOH F 725 DISTANCE = 16.95 ANGSTROMS
REMARK 525 HOH F 726 DISTANCE = 20.43 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 303
REMARK 610 NAG B 305
REMARK 610 LTV B 306
REMARK 610 LTV C 304
REMARK 610 NAG D 303
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 B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 45 O
REMARK 620 2 ALA B 47 O 79.3
REMARK 620 3 HOH B 500 O 152.3 81.5
REMARK 620 4 HOH B 522 O 85.0 69.6 69.6
REMARK 620 5 HOH B 542 O 72.1 137.7 134.3 135.6
REMARK 620 6 HOH B 589 O 135.3 123.2 72.2 136.9 66.2
REMARK 620 7 HOH B 593 O 82.1 72.6 110.9 141.7 73.0 71.5
REMARK 620 8 HOH B 618 O 97.7 142.6 85.6 73.0 73.1 85.0 144.4
REMARK 620 N 1 2 3 4 5 6 7
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 HOH B 404 O
REMARK 620 2 HOH B 513 O 50.9
REMARK 620 3 HOH B 587 O 56.0 67.4
REMARK 620 4 HOH B 601 O 155.8 118.9 100.4
REMARK 620 5 HOH B 650 O 48.4 99.1 65.2 131.0
REMARK 620 6 HOH B 715 O 96.0 109.5 45.6 65.1 74.1
REMARK 620 N 1 2 3 4 5
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 83.3
REMARK 620 3 HOH C 458 O 97.5 83.2
REMARK 620 4 HOH C 542 O 165.0 86.3 70.4
REMARK 620 5 HOH C 590 O 98.5 92.1 162.7 92.7
REMARK 620 6 HOH C 597 O 92.0 154.6 72.6 92.7 113.3
REMARK 620 N 1 2 3 4 5
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 84.1
REMARK 620 3 HOH E 405 O 101.2 92.5
REMARK 620 4 HOH E 481 O 90.4 76.9 163.5
REMARK 620 5 HOH E 495 O 166.9 89.4 90.4 77.0
REMARK 620 6 HOH E 564 O 92.2 154.6 112.9 77.9 88.8
REMARK 620 N 1 2 3 4 5
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 84.8
REMARK 620 3 HOH D 493 O 95.6 77.4
REMARK 620 4 HOH D 548 O 170.6 87.3 77.6
REMARK 620 5 HOH D 591 O 90.1 154.6 78.3 94.8
REMARK 620 6 HOH D 596 O 90.5 88.2 163.8 94.4 116.7
REMARK 620 N 1 2 3 4 5
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 83.9
REMARK 620 3 HOH F 412 O 83.0 73.7
REMARK 620 4 HOH F 495 O 95.1 77.5 151.1
REMARK 620 5 HOH F 550 O 163.0 85.7 106.9 69.5
REMARK 620 6 HOH F 612 O 88.2 156.0 127.8 80.7 96.0
REMARK 620 N 1 2 3 4 5
DBREF 6OSZ A -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6OSZ B -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6OSZ C -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6OSZ E -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6OSZ D -21 269 UNP O59952 LIP_THELA 1 291
DBREF 6OSZ 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 24
HET NAG A 302 27
HET LTV A 303 83
HET PO4 A 304 5
HET PO4 A 305 5
HET OCA B 301 24
HET PO4 B 302 5
HET CA B 303 1
HET CA B 304 1
HET NAG B 305 27
HET LTV B 306 107
HET PO4 B 307 5
HET OCA C 301 24
HET CA C 302 1
HET NAG C 303 27
HET LTV C 304 99
HET PO4 C 305 5
HET OCA E 301 24
HET CA E 302 1
HET NAG E 303 27
HET LTV E 304 141
HET PO4 E 305 5
HET PO4 E 306 5
HET OCA D 301 24
HET CA D 302 1
HET NAG D 303 27
HET LTV D 304 141
HET PO4 D 305 5
HET PO4 D 306 5
HET OCA F 301 24
HET CA F 302 1
HET NAG F 303 27
HET LTV F 304 101
HET PO4 F 305 5
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM LTV 2-HYDROXY-3-(OCTADECANOYLOXY)PROPYL PENTACOSANOATE
HETNAM PO4 PHOSPHATE ION
HETNAM CA CALCIUM 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 NAG 6(C8 H15 N O6)
FORMUL 9 LTV 6(C46 H90 O5)
FORMUL 10 PO4 10(O4 P 3-)
FORMUL 14 CA 6(CA 2+)
FORMUL 41 HOH *1729(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 LEU C 93 1 9
HELIX 27 AC9 ASP C 111 HIS C 135 1 25
HELIX 28 AD1 SER C 146 ARG C 160 1 15
HELIX 29 AD2 ASN C 178 GLN C 188 1 11
HELIX 30 AD3 ILE C 202 LEU C 206 5 5
HELIX 31 AD4 PRO C 208 GLY C 212 5 5
HELIX 32 AD5 THR C 231 ASN C 233 5 3
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 ASN E 26 5 6
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 LEU D 93 1 9
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 THR D 231 ASN D 233 5 3
HELIX 55 AG1 ILE D 255 TRP D 260 5 6
HELIX 56 AG2 SER F 3 ALA F 20 1 18
HELIX 57 AG3 TYR F 21 ASP F 27 5 7
HELIX 58 AG4 CYS F 41 ALA F 47 1 7
HELIX 59 AG5 SER F 85 LEU F 93 1 9
HELIX 60 AG6 ASP F 111 HIS F 135 1 25
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 THR A 143 N LEU A 78
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
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 LEU B 52
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 SER C 79 N PHE C 66
SHEET 4 AA5 8 ARG C 139 HIS C 145 1 O VAL C 141 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 ILE C 222 N THR C 197
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 TYR E 53
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 VAL E 141 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 ILE E 222 N THR E 197
SHEET 8 AA7 8 ILE E 235 ILE E 238 -1 O ILE E 238 N GLU E 219
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 VAL D 141 N ILE D 76
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 ILE D 238 N GLU D 219
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 LEU F 52
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 THR F 143 N LEU F 78
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 2.04
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 2.04
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 2.04
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 2.04
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 2.04
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 2.04
SSBOND 17 CYS F 36 CYS F 41 1555 1555 2.04
SSBOND 18 CYS F 104 CYS F 107 1555 1555 2.03
LINK ND2 ASN A 33 C1 NAG A 302 1555 1555 1.49
LINK OG SER A 146 C1 OCA A 301 1555 1555 1.37
LINK OG SER B 146 C1 OCA B 301 1555 1555 1.37
LINK ND2 ASN C 33 C1 NAG C 303 1555 1555 1.52
LINK OG SER C 83 C1 OCA C 301 1555 1555 1.38
LINK ND2 ASN E 33 C1 NAG E 303 1555 1555 1.43
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 1.37
LINK O GLU B 45 CA CA B 303 1555 1555 2.34
LINK O ALA B 47 CA CA B 303 1555 1555 2.53
LINK CA CA B 303 O HOH B 500 1555 1555 2.48
LINK CA CA B 303 O HOH B 522 1555 1555 2.48
LINK CA CA B 303 O HOH B 542 1555 1555 2.49
LINK CA CA B 303 O HOH B 589 1555 1555 2.48
LINK CA CA B 303 O HOH B 593 1555 1555 2.46
LINK CA CA B 303 O HOH B 618 1555 1555 2.46
LINK CA CA B 304 O HOH B 404 1555 1555 2.45
LINK CA CA B 304 O HOH B 513 1555 1555 2.92
LINK CA CA B 304 O HOH B 587 1555 1555 2.74
LINK CA CA B 304 O HOH B 601 1555 1555 2.13
LINK CA CA B 304 O HOH B 650 1555 1555 3.11
LINK CA CA B 304 O HOH B 715 1555 1555 3.11
LINK O GLU C 45 CA CA C 302 1555 1555 2.35
LINK O ALA C 47 CA CA C 302 1555 1555 2.43
LINK CA CA C 302 O HOH C 458 1555 1555 2.48
LINK CA CA C 302 O HOH C 542 1555 1555 2.38
LINK CA CA C 302 O HOH C 590 1555 1555 2.19
LINK CA CA C 302 O HOH C 597 1555 1555 2.32
LINK O GLU E 45 CA CA E 302 1555 1555 2.45
LINK O ALA E 47 CA CA E 302 1555 1555 2.48
LINK CA CA E 302 O HOH E 405 1555 1555 2.32
LINK CA CA E 302 O HOH E 481 1555 1555 2.49
LINK CA CA E 302 O HOH E 495 1555 1555 2.45
LINK CA CA E 302 O HOH E 564 1555 1555 2.50
LINK O GLU D 45 CA CA D 302 1555 1555 2.32
LINK O ALA D 47 CA CA D 302 1555 1555 2.43
LINK CA CA D 302 O HOH D 493 1555 1555 2.44
LINK CA CA D 302 O HOH D 548 1555 1555 2.50
LINK CA CA D 302 O HOH D 591 1555 1555 2.26
LINK CA CA D 302 O HOH D 596 1555 1555 2.31
LINK O GLU F 45 CA CA F 302 1555 1555 2.33
LINK O ALA F 47 CA CA F 302 1555 1555 2.56
LINK CA CA F 302 O HOH F 412 1555 1555 2.36
LINK CA CA F 302 O HOH F 495 1555 1555 2.40
LINK CA CA F 302 O HOH F 550 1555 1555 2.38
LINK CA CA F 302 O HOH F 612 1555 1555 2.39
CISPEP 1 LEU A 206 PRO A 207 0 -14.35
CISPEP 2 SER A 217 PRO A 218 0 -0.18
CISPEP 3 LEU B 206 PRO B 207 0 -14.13
CISPEP 4 SER B 217 PRO B 218 0 0.75
CISPEP 5 LEU C 206 PRO C 207 0 -13.26
CISPEP 6 SER C 217 PRO C 218 0 1.23
CISPEP 7 LEU E 206 PRO E 207 0 -14.94
CISPEP 8 SER E 217 PRO E 218 0 0.74
CISPEP 9 LEU D 206 PRO D 207 0 -14.64
CISPEP 10 SER D 217 PRO D 218 0 0.03
CISPEP 11 LEU F 206 PRO F 207 0 -13.54
CISPEP 12 SER F 217 PRO F 218 0 -0.19
CRYST1 76.929 89.937 123.422 90.00 94.49 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 0.012999 0.000000 0.001020 0.00000
SCALE2 0.000000 0.011119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008127 0.00000
TER 4127 LEU A 269
TER 8235 LEU B 269
TER 12373 LEU C 269
TER 16470 LEU E 269
TER 20557 LEU D 269
TER 24679 LEU F 269
MASTER 667 0 34 66 60 0 0 614613 6 1123 138
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