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HEADER LIPID BINDING PROTEIN 15-JUL-26 37DS
TITLE CRYSTAL STRUCTURE OF THERMOMYCES LANUGINOSA LIPASE WITH BOUND 1,3
TITLE 2 DIACYLGLYCROL AND FATTY ACID ACYL INTERMEDIATES: MONOCLINIC CRYSTALS
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: ASPERGILLACEAE SP.;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1914746
KEYWDS CATALYTIC INTERMEDIATES, TRIMER, SUBSTRATES, PRODUCTS, LID OPENING,
KEYWDS 2 INTERFACIAL ACTIVATION, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 05-AUG-26 37DS 0
SPRSDE 05-AUG-26 37DS 6XRV
JRNL AUTH A.MCPHERSON
JRNL TITL CRYSTAL STRUCTURE OF THERMOMYCES LANUGINOSA LIPASE WITH
JRNL TITL 2 BOUND 1,3 DIACYLGLYCROL AND FATTY ACID ACYL INTERMEDIATES:
JRNL TITL 3 MONOCLINIC CRYSTALS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.1_5286
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 : 306740
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.181
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 9947 592 0.1346 0.1723
REMARK 3 2 4.4400 - 3.5300 1.00 9885 495 0.1025 0.1633
REMARK 3 3 3.5300 - 3.0800 1.00 9849 478 0.1128 0.1580
REMARK 3 4 3.0800 - 2.8000 1.00 9827 524 0.1168 0.1628
REMARK 3 5 2.8000 - 2.6000 1.00 9773 535 0.1152 0.1661
REMARK 3 6 2.6000 - 2.4500 1.00 9820 512 0.1128 0.1593
REMARK 3 7 2.4500 - 2.3200 1.00 9721 518 0.1073 0.1550
REMARK 3 8 2.3200 - 2.2200 1.00 9847 493 0.1050 0.1588
REMARK 3 9 2.2200 - 2.1400 1.00 9798 465 0.1090 0.1658
REMARK 3 10 2.1400 - 2.0600 1.00 9761 515 0.1186 0.1703
REMARK 3 11 2.0600 - 2.0000 1.00 9774 514 0.1262 0.1822
REMARK 3 12 2.0000 - 1.9400 1.00 9783 511 0.1458 0.1993
REMARK 3 13 1.9400 - 1.8900 1.00 9754 509 0.1319 0.1846
REMARK 3 14 1.8900 - 1.8400 1.00 9738 502 0.1180 0.1723
REMARK 3 15 1.8400 - 1.8000 1.00 9748 497 0.1175 0.1836
REMARK 3 16 1.8000 - 1.7600 1.00 9685 530 0.1244 0.1748
REMARK 3 17 1.7600 - 1.7300 1.00 9773 531 0.1416 0.2057
REMARK 3 18 1.7300 - 1.7000 1.00 9656 528 0.1464 0.2078
REMARK 3 19 1.7000 - 1.6700 1.00 9659 516 0.1605 0.2260
REMARK 3 20 1.6700 - 1.6400 1.00 9743 516 0.1749 0.2343
REMARK 3 21 1.6400 - 1.6100 0.99 9688 546 0.1919 0.2412
REMARK 3 22 1.6100 - 1.5900 0.99 9696 488 0.2126 0.2779
REMARK 3 23 1.5900 - 1.5600 0.99 9656 506 0.2110 0.2720
REMARK 3 24 1.5600 - 1.5400 0.99 9598 523 0.2204 0.2671
REMARK 3 25 1.5400 - 1.5200 0.99 9728 485 0.2421 0.2991
REMARK 3 26 1.5200 - 1.5000 0.99 9578 523 0.2567 0.3100
REMARK 3 27 1.5000 - 1.4800 0.98 9631 477 0.2727 0.3216
REMARK 3 28 1.4800 - 1.4600 0.98 9532 542 0.3031 0.3403
REMARK 3 29 1.4600 - 1.4500 0.98 9446 493 0.3175 0.3438
REMARK 3 30 1.4500 - 1.4300 0.95 9284 498 0.3544 0.3886
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.198
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.28
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 13784
REMARK 3 ANGLE : 1.012 18576
REMARK 3 CHIRALITY : 0.078 1958
REMARK 3 PLANARITY : 0.009 2411
REMARK 3 DIHEDRAL : 16.832 5271
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 37DS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-26.
REMARK 100 THE DEPOSITION ID IS D_1000309924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-24
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 4.5 - 6.0
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
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 : 19.20
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : 0.14600
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) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 13.30
REMARK 200 R MERGE FOR SHELL (I) : 5.69000
REMARK 200 R SYM FOR SHELL (I) : 4.85000
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: NULL
REMARK 200
REMARK 200 REMARK: MONOCLINIC PRISMS
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: CRYSTALLIZED BY SITTING DROP VAPOR
REMARK 280 DIFFUSION WITH 0.6 ML RESERVOIRS AND DROP VOLUMES 6 UL. DROPS
REMARK 280 CONSISTED OF EQUAL VOLUMES OF THE RESERVOIR AND THE PROTEIN
REMARK 280 STOCK SOLUTION. THE RESERVOIRS WERE 20% W/V PEG 3350 WITH 0.1 M
REMARK 280 HEPES BUFFER. THE PROTEIN WAS IN THE GROWTH BROTH OF THE
REMARK 280 ASPERGILLUM EXPRESSION SYSTEM AND WAS NOT FURTHER PURIFIED. THE
REMARK 280 STOCK PROTEIN CONCENTRATION WAS 30 MG/ML, PH 5.5, VAPOR
REMARK 280 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, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -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 ARG B 179 CZ NH1 NH2
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 ASP F 102 OD2
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 H ARG E 209 O4 PO4 E 314 1.52
REMARK 500 HH11 ARG D 209 O HOH D 414 1.57
REMARK 500 HO1 PEG B 304 O HOH B 404 1.60
REMARK 500 OXT ACT A 302 O HOH A 401 1.75
REMARK 500 O HOH F 622 O HOH F 649 1.76
REMARK 500 O HOH E 592 O HOH E 617 1.80
REMARK 500 O HOH C 625 O HOH C 643 1.83
REMARK 500 O HOH A 586 O HOH A 652 1.85
REMARK 500 O HOH F 611 O HOH F 631 1.86
REMARK 500 OE1 GLU B 129 O HOH B 401 1.86
REMARK 500 O HOH B 635 O HOH B 665 1.88
REMARK 500 O HOH A 652 O HOH A 664 1.88
REMARK 500 O HOH E 553 O HOH E 564 1.88
REMARK 500 OD1 ASN D 94 O HOH D 401 1.93
REMARK 500 O HOH A 617 O HOH A 665 1.93
REMARK 500 O HOH A 727 O HOH A 729 1.93
REMARK 500 O HOH A 454 O HOH A 662 1.94
REMARK 500 O HOH F 634 O HOH F 660 1.94
REMARK 500 O HOH E 669 O HOH E 676 1.94
REMARK 500 O HOH C 635 O HOH C 703 1.95
REMARK 500 O HOH D 627 O HOH D 643 1.95
REMARK 500 NE ARG B 179 O HOH B 402 1.95
REMARK 500 O HOH F 686 O HOH F 782 1.95
REMARK 500 O HOH D 704 O HOH D 707 1.96
REMARK 500 O HOH A 431 O HOH A 438 1.97
REMARK 500 O HOH B 609 O HOH B 734 1.97
REMARK 500 O HOH A 718 O HOH A 753 1.99
REMARK 500 O HOH D 469 O HOH D 655 1.99
REMARK 500 O HOH B 640 O HOH B 716 2.00
REMARK 500 O HOH B 749 O HOH B 752 2.00
REMARK 500 O HOH A 710 O HOH A 744 2.00
REMARK 500 O HOH A 672 O HOH A 718 2.01
REMARK 500 O HOH E 448 O HOH E 676 2.01
REMARK 500 O HOH D 411 O HOH D 547 2.02
REMARK 500 O HOH A 672 O HOH A 750 2.03
REMARK 500 O HOH F 616 O HOH F 727 2.03
REMARK 500 O HOH F 650 O HOH F 732 2.03
REMARK 500 O HOH E 607 O HOH E 656 2.04
REMARK 500 O HOH F 683 O HOH F 731 2.04
REMARK 500 OE2 GLU C 134 O4 PEG C 319 2.04
REMARK 500 O HOH E 653 O HOH E 689 2.04
REMARK 500 O HOH C 553 O HOH C 645 2.04
REMARK 500 O HOH B 755 O HOH B 792 2.05
REMARK 500 O HOH E 426 O HOH E 666 2.05
REMARK 500 O HOH E 624 O HOH E 689 2.05
REMARK 500 O HOH A 651 O HOH A 685 2.06
REMARK 500 O HOH B 445 O HOH B 632 2.06
REMARK 500 O HOH A 760 O HOH A 806 2.06
REMARK 500 CD GLU A 210 C3 LTV A 316 2.06
REMARK 500 O HOH A 719 O HOH A 726 2.07
REMARK 500
REMARK 500 THIS ENTRY HAS 110 CLOSE CONTACTS
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 464 2647 1.46
REMARK 500 O HOH C 604 O HOH E 651 2746 1.93
REMARK 500 O HOH C 464 O HOH D 660 1554 1.95
REMARK 500 O HOH B 786 O HOH F 798 1655 1.98
REMARK 500 O HOH B 792 O HOH E 734 2756 1.99
REMARK 500 O HOH B 503 O HOH F 580 1655 2.05
REMARK 500 O HOH B 773 O HOH F 641 1655 2.06
REMARK 500 O HOH E 523 O HOH F 642 1655 2.11
REMARK 500 NH2 ARG A 179 O HOH D 464 2647 2.12
REMARK 500 O HOH B 711 O HOH F 678 1655 2.14
REMARK 500 O HOH E 541 O HOH F 668 1655 2.15
REMARK 500 OE2 GLU B 43 O HOH F 647 1655 2.17
REMARK 500 O HOH B 681 O HOH F 701 1655 2.18
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 55.74 -149.73
REMARK 500 ARG A 84 -42.45 -135.10
REMARK 500 SER A 146 -129.39 63.49
REMARK 500 THR A 189 -167.41 -102.02
REMARK 500 THR A 199 -117.37 35.41
REMARK 500 PHE A 262 -40.08 74.06
REMARK 500 ASN B 39 32.61 -99.34
REMARK 500 CYS B 41 57.06 -149.86
REMARK 500 ARG B 84 -46.81 -139.42
REMARK 500 SER B 146 -127.56 59.21
REMARK 500 THR B 199 -118.16 34.60
REMARK 500 PHE B 262 -42.01 72.59
REMARK 500 ASP C 27 33.32 -142.35
REMARK 500 CYS C 41 55.01 -151.45
REMARK 500 ARG C 84 -47.37 -143.33
REMARK 500 ARG C 84 -47.37 -141.68
REMARK 500 SER C 146 -126.75 61.46
REMARK 500 THR C 199 -118.93 33.13
REMARK 500 PHE C 262 -36.22 69.20
REMARK 500 ASN E 39 26.53 41.09
REMARK 500 CYS E 41 54.70 -145.12
REMARK 500 ARG E 84 -42.79 -139.57
REMARK 500 SER E 146 -128.31 59.24
REMARK 500 THR E 199 -117.30 31.70
REMARK 500 PHE E 262 -43.93 72.38
REMARK 500 ASP D 27 37.06 -142.44
REMARK 500 CYS D 41 56.88 -150.07
REMARK 500 ARG D 84 -43.40 -140.25
REMARK 500 SER D 146 -129.24 61.72
REMARK 500 THR D 199 -117.94 32.97
REMARK 500 PHE D 262 -43.72 70.83
REMARK 500 ASP F 27 78.62 -157.04
REMARK 500 CYS F 36 -158.48 -121.91
REMARK 500 CYS F 41 59.88 -149.40
REMARK 500 ARG F 84 -47.42 -140.57
REMARK 500 SER F 146 -128.14 61.15
REMARK 500 THR F 199 -118.18 31.59
REMARK 500 PHE F 262 -41.75 71.73
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 819 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 821 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 822 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 823 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH A 824 DISTANCE = 9.60 ANGSTROMS
REMARK 525 HOH B 837 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 838 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 839 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 840 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 841 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH B 842 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH B 843 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH B 844 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH B 845 DISTANCE = 11.24 ANGSTROMS
REMARK 525 HOH C 768 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH C 769 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 770 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH C 771 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH C 772 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH C 773 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH C 774 DISTANCE = 10.05 ANGSTROMS
REMARK 525 HOH C 775 DISTANCE = 10.65 ANGSTROMS
REMARK 525 HOH E 736 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH E 737 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH E 738 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH E 739 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH E 740 DISTANCE = 10.79 ANGSTROMS
REMARK 525 HOH D 759 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH D 760 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH D 761 DISTANCE = 9.70 ANGSTROMS
REMARK 525 HOH D 762 DISTANCE = 10.15 ANGSTROMS
REMARK 525 HOH F 799 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH F 800 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH F 801 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH F 802 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH F 803 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH F 804 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH F 805 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH F 806 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH F 807 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH F 808 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH F 809 DISTANCE = 10.42 ANGSTROMS
REMARK 525 HOH F 810 DISTANCE = 14.56 ANGSTROMS
REMARK 525 HOH F 811 DISTANCE = 17.08 ANGSTROMS
REMARK 525 HOH F 812 DISTANCE = 17.44 ANGSTROMS
REMARK 525 HOH F 813 DISTANCE = 20.69 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 PG4 A 304
REMARK 610 LTV A 316
REMARK 610 OCA B 301
REMARK 610 NAG B 311
REMARK 610 OCA C 301
REMARK 610 PG4 C 311
REMARK 610 LTV C 315
REMARK 610 OCA E 301
REMARK 610 LTV E 311
REMARK 610 LTV E 312
REMARK 610 OCA D 301
REMARK 610 LTV D 311
REMARK 610 OCA F 302
REMARK 610 LTV F 307
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 OCA F 302
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 312 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 62 OD1 73.8
REMARK 620 3 ASP A 62 OD2 122.2 52.1
REMARK 620 4 PEG A 310 O2 86.5 118.1 100.7
REMARK 620 5 HOH A 573 O 88.3 75.3 95.4 163.4
REMARK 620 6 HOH A 635 O 83.5 149.3 154.3 80.0 83.8
REMARK 620 7 HOH A 665 O 151.7 125.1 84.2 99.2 78.4 70.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 314 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 101 O
REMARK 620 2 SER A 105 OG 121.4
REMARK 620 3 HOH B 514 O 114.3 100.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 313 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 465 O
REMARK 620 2 HOH A 483 O 77.4
REMARK 620 3 HOH A 772 O 153.3 76.1
REMARK 620 4 SER F 54 O 71.7 20.9 82.2
REMARK 620 5 HOH F 488 O 82.6 72.6 93.2 92.0
REMARK 620 6 HOH F 547 O 93.4 88.2 82.0 69.0 160.8
REMARK 620 7 HOH F 616 O 60.4 134.3 142.3 119.0 115.1 78.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 309 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 45 O
REMARK 620 2 ALA B 47 O 78.5
REMARK 620 3 HOH B 515 O 151.9 81.9
REMARK 620 4 HOH B 559 O 84.8 69.7 69.6
REMARK 620 5 HOH B 582 O 72.8 137.6 134.1 135.6
REMARK 620 6 HOH B 626 O 83.6 74.9 110.4 144.3 71.5
REMARK 620 7 HOH B 650 O 96.5 142.2 86.8 72.5 72.7 142.4
REMARK 620 8 HOH B 691 O 134.9 123.6 73.0 137.7 65.3 68.4 86.5
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 310 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 57 OD1
REMARK 620 2 ASP B 62 OD1 84.8
REMARK 620 3 ASP B 62 OD2 132.0 50.6
REMARK 620 4 HOH B 534 O 91.5 75.3 92.9
REMARK 620 5 HOH B 556 O 76.0 149.8 151.9 82.1
REMARK 620 6 HOH B 640 O 79.1 80.5 76.9 154.7 117.5
REMARK 620 7 HOH B 665 O 146.1 120.6 80.6 75.8 71.3 124.0
REMARK 620 8 HOH B 716 O 102.0 125.8 93.1 155.5 81.4 49.6 81.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 312 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 45 O
REMARK 620 2 ALA C 47 O 81.5
REMARK 620 3 PEG C 318 O2 79.3 81.7
REMARK 620 4 HOH C 465 O 97.7 83.0 164.6
REMARK 620 5 HOH C 578 O 163.6 85.4 108.7 70.8
REMARK 620 6 HOH C 646 O 95.5 156.0 121.3 73.8 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 313 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 57 OD1
REMARK 620 2 ASP C 62 OD1 82.1
REMARK 620 3 ASP C 62 OD2 129.6 51.3
REMARK 620 4 HOH C 493 O 64.3 73.0 82.5
REMARK 620 5 HOH C 557 O 93.4 76.0 92.6 143.8
REMARK 620 6 HOH C 614 O 98.0 123.6 94.1 57.6 158.5
REMARK 620 7 HOH C 627 O 83.2 154.8 147.1 118.1 84.6 78.8
REMARK 620 8 HOH C 643 O 144.9 125.9 84.8 138.1 76.4 83.8 62.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 45 O
REMARK 620 2 ALA E 47 O 82.3
REMARK 620 3 HOH E 478 O 89.1 77.9
REMARK 620 4 HOH E 513 O 168.6 90.6 80.7
REMARK 620 5 HOH E 575 O 93.0 151.7 74.1 89.1
REMARK 620 6 HOH E 627 O 99.5 113.0 166.9 91.5 95.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 309 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 62 OD1 78.6
REMARK 620 3 ASP E 62 OD2 128.4 52.5
REMARK 620 4 HOH E 502 O 87.1 72.3 92.1
REMARK 620 5 HOH E 614 O 84.6 151.2 146.6 83.7
REMARK 620 6 HOH E 617 O 145.1 126.3 84.7 79.8 61.9
REMARK 620 7 HOH E 630 O 110.4 127.8 91.0 154.6 80.0 75.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 45 O
REMARK 620 2 ALA D 47 O 84.9
REMARK 620 3 HOH D 489 O 94.9 77.0
REMARK 620 4 HOH D 563 O 170.7 87.9 77.7
REMARK 620 5 HOH D 639 O 92.7 156.8 80.2 91.6
REMARK 620 6 HOH D 646 O 93.6 91.8 165.3 92.5 111.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 309 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 57 OD1
REMARK 620 2 ASP D 62 OD1 78.0
REMARK 620 3 ASP D 62 OD2 125.4 51.5
REMARK 620 4 PO4 D 312 O4 154.9 121.8 79.1
REMARK 620 5 HOH D 427 O 80.5 150.5 154.1 75.3
REMARK 620 6 HOH D 479 O 69.7 76.5 78.7 126.7 114.2
REMARK 620 7 HOH D 530 O 92.1 75.8 93.8 79.6 85.2 149.5
REMARK 620 8 HOH D 578 O 105.8 121.9 87.8 77.8 83.3 53.5 156.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 45 O
REMARK 620 2 ALA F 47 O 84.2
REMARK 620 3 HOH F 412 O 90.5 78.5
REMARK 620 4 HOH F 499 O 95.1 79.0 156.1
REMARK 620 5 HOH F 600 O 165.1 86.3 98.8 71.7
REMARK 620 6 HOH F 667 O 87.0 156.8 123.1 80.5 97.4
REMARK 620 N 1 2 3 4 5
DBREF 37DS A -21 269 UNP O59952 LIP_THELA 1 291
DBREF 37DS B -21 269 UNP O59952 LIP_THELA 1 291
DBREF 37DS C -21 269 UNP O59952 LIP_THELA 1 291
DBREF 37DS E -21 269 UNP O59952 LIP_THELA 1 291
DBREF 37DS D -21 269 UNP O59952 LIP_THELA 1 291
DBREF 37DS 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 ACT A 302 7
HET PEG A 303 17
HET PG4 A 304 25
HET PEG A 305 17
HET PEG A 306 17
HET PEG A 307 17
HET PEG A 308 17
HET PEG A 309 17
HET PEG A 310 17
HET GOL A 311 14
HET CA A 312 1
HET CA A 313 1
HET CA A 314 1
HET NAG A 315 27
HET LTV A 316 94
HET PO4 A 317 5
HET PO4 A 318 5
HET OCA B 301 17
HET PO4 B 302 5
HET PEG B 303 17
HET PEG B 304 17
HET PEG B 305 17
HET PEG B 306 17
HET PG4 B 307 31
HET PEG B 308 17
HET CA B 309 1
HET CA B 310 1
HET NAG B 311 27
HET PEG B 312 17
HET PO4 B 313 5
HET PO4 B 314 5
HET PEG B 315 17
HET OCA C 301 11
HET ACT C 302 7
HET PEG C 303 17
HET PEG C 304 17
HET PEG C 305 17
HET PEG C 306 17
HET ACT C 307 7
HET PG5 C 308 30
HET PG4 C 309 31
HET PG4 C 310 31
HET PG4 C 311 23
HET CA C 312 1
HET CA C 313 1
HET NAG C 314 27
HET LTV C 315 107
HET PO4 C 316 5
HET PEG C 317 17
HET PEG C 318 17
HET PEG C 319 17
HET PEG C 320 17
HET OCA E 301 17
HET PEG E 302 17
HET PEG E 303 17
HET PEG E 304 17
HET PEG E 305 17
HET PEG E 306 17
HET PG4 E 307 31
HET CA E 308 1
HET CA E 309 1
HET NAG E 310 27
HET LTV E 311 137
HET LTV E 312 116
HET PO4 E 313 5
HET PO4 E 314 5
HET PEG E 315 17
HET PEG E 316 17
HET OCA D 301 11
HET PEG D 302 17
HET PEG D 303 17
HET PEG D 304 17
HET PEG D 305 17
HET PEG D 306 17
HET PEG D 307 17
HET CA D 308 1
HET CA D 309 1
HET NAG D 310 27
HET LTV D 311 116
HET PO4 D 312 5
HET PO4 D 313 5
HET PEG D 314 17
HET PEG D 315 17
HET PEG D 316 17
HET PEG F 301 17
HET OCA F 302 20
HET PEG F 303 17
HET GOL F 304 14
HET CA F 305 1
HET NAG F 306 27
HET LTV F 307 106
HET PO4 F 308 5
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
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
HETNAM PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
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 ACT 3(C2 H3 O2 1-)
FORMUL 9 PEG 40(C4 H10 O3)
FORMUL 10 PG4 6(C8 H18 O5)
FORMUL 17 GOL 2(C3 H8 O3)
FORMUL 18 CA 12(CA 2+)
FORMUL 21 NAG 6(C8 H15 N O6)
FORMUL 22 LTV 6(C46 H90 O5)
FORMUL 23 PO4 11(O4 P 3-)
FORMUL 47 PG5 C8 H18 O4
FORMUL 00 HOH *2359(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 ASN F 26 5 6
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 2.06
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.04
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.07
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.06
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.08
SSBOND 7 CYS C 22 CYS C 268 1555 1555 2.08
SSBOND 8 CYS C 36 CYS C 41 1555 1555 2.07
SSBOND 9 CYS C 104 CYS C 107 1555 1555 2.04
SSBOND 10 CYS E 22 CYS E 268 1555 1555 2.06
SSBOND 11 CYS E 36 CYS E 41 1555 1555 2.03
SSBOND 12 CYS E 104 CYS E 107 1555 1555 2.07
SSBOND 13 CYS D 22 CYS D 268 1555 1555 2.11
SSBOND 14 CYS D 36 CYS D 41 1555 1555 2.03
SSBOND 15 CYS D 104 CYS D 107 1555 1555 2.06
SSBOND 16 CYS F 22 CYS F 268 1555 1555 2.07
SSBOND 17 CYS F 36 CYS F 41 1555 1555 2.05
SSBOND 18 CYS F 104 CYS F 107 1555 1555 2.05
LINK ND2 ASN A 33 C1 NAG A 315 1555 1555 1.50
LINK OG SER A 146 C1 OCA A 301 1555 1555 1.38
LINK OE2 GLU A 210 C3 LTV A 316 1555 1555 1.38
LINK OG SER B 146 C1 OCA B 301 1555 1555 1.38
LINK ND2 ASN C 33 C1 NAG C 314 1555 1555 1.43
LINK OG SER C 146 C1 OCA C 301 1555 1555 1.38
LINK ND2 ASN E 33 C1 NAG E 310 1555 1555 1.49
LINK OG SER E 146 C1 OCA E 301 1555 1555 1.38
LINK ND2 ASN D 33 C1 NAG D 310 1555 1555 1.44
LINK OG SER D 146 C1 OCA D 301 1555 1555 1.38
LINK ND2 ASN F 33 C1 NAG F 306 1555 1555 1.45
LINK OG SER F 146 C1 OCA F 302 1555 1555 1.38
LINK OD1 ASP A 57 CA CA A 312 1555 1555 2.15
LINK OD1 ASP A 62 CA CA A 312 1555 1555 2.53
LINK OD2 ASP A 62 CA CA A 312 1555 1555 2.50
LINK O ASN A 101 CA CA A 314 1555 1555 2.80
LINK OG SER A 105 CA CA A 314 1555 1555 2.79
LINK O2 PEG A 310 CA CA A 312 1555 1555 2.70
LINK CA CA A 312 O HOH A 573 1555 1555 2.22
LINK CA CA A 312 O HOH A 635 1555 1555 2.40
LINK CA CA A 312 O HOH A 665 1555 1555 2.58
LINK CA CA A 313 O HOH A 465 1555 1555 2.47
LINK CA CA A 313 O HOH A 483 1555 1555 2.61
LINK CA CA A 313 O HOH A 772 1555 1555 2.57
LINK CA CA A 313 O SER F 54 2657 1555 2.28
LINK CA CA A 313 O HOH F 488 1555 2647 2.60
LINK CA CA A 313 O HOH F 547 1555 2647 2.37
LINK CA CA A 313 O HOH F 616 1555 2647 2.49
LINK CA CA A 314 O HOH B 514 1555 1555 2.81
LINK O GLU B 45 CA CA B 309 1555 1555 2.36
LINK O ALA B 47 CA CA B 309 1555 1555 2.53
LINK OD1 ASP B 57 CA CA B 310 1555 1555 2.24
LINK OD1 ASP B 62 CA CA B 310 1555 1555 2.54
LINK OD2 ASP B 62 CA CA B 310 1555 1555 2.54
LINK CA CA B 309 O HOH B 515 1555 1555 2.45
LINK CA CA B 309 O HOH B 559 1555 1555 2.45
LINK CA CA B 309 O HOH B 582 1555 1555 2.47
LINK CA CA B 309 O HOH B 626 1555 1555 2.37
LINK CA CA B 309 O HOH B 650 1555 1555 2.43
LINK CA CA B 309 O HOH B 691 1555 1555 2.46
LINK CA CA B 310 O HOH B 534 1555 1555 2.32
LINK CA CA B 310 O HOH B 556 1555 1555 2.36
LINK CA CA B 310 O HOH B 640 1555 1555 2.48
LINK CA CA B 310 O HOH B 665 1555 1555 2.49
LINK CA CA B 310 O HOH B 716 1555 1555 2.27
LINK O GLU C 45 CA CA C 312 1555 1555 2.31
LINK O ALA C 47 CA CA C 312 1555 1555 2.47
LINK OD1 ASP C 57 CA CA C 313 1555 1555 2.20
LINK OD1 ASP C 62 CA CA C 313 1555 1555 2.53
LINK OD2 ASP C 62 CA CA C 313 1555 1555 2.46
LINK CA CA C 312 O2 PEG C 318 1555 1555 2.45
LINK CA CA C 312 O HOH C 465 1555 1555 2.48
LINK CA CA C 312 O HOH C 578 1555 1555 2.46
LINK CA CA C 312 O HOH C 646 1555 1555 2.21
LINK CA CA C 313 O HOH C 493 1555 1555 3.07
LINK CA CA C 313 O HOH C 557 1555 1555 2.21
LINK CA CA C 313 O HOH C 614 1555 1555 2.14
LINK CA CA C 313 O HOH C 627 1555 1555 2.35
LINK CA CA C 313 O HOH C 643 1555 1555 2.52
LINK O GLU E 45 CA CA E 308 1555 1555 2.52
LINK O ALA E 47 CA CA E 308 1555 1555 2.47
LINK OD1 ASP E 57 CA CA E 309 1555 1555 2.32
LINK OD1 ASP E 62 CA CA E 309 1555 1555 2.56
LINK OD2 ASP E 62 CA CA E 309 1555 1555 2.42
LINK CA CA E 308 O HOH E 478 1555 1555 2.47
LINK CA CA E 308 O HOH E 513 1555 1555 2.50
LINK CA CA E 308 O HOH E 575 1555 1555 2.41
LINK CA CA E 308 O HOH E 627 1555 1555 2.16
LINK CA CA E 309 O HOH E 502 1555 1555 2.22
LINK CA CA E 309 O HOH E 614 1555 1555 2.36
LINK CA CA E 309 O HOH E 617 1555 1555 2.40
LINK CA CA E 309 O HOH E 630 1555 1555 2.27
LINK O GLU D 45 CA CA D 308 1555 1555 2.31
LINK O ALA D 47 CA CA D 308 1555 1555 2.41
LINK OD1 ASP D 57 CA CA D 309 1555 1555 2.20
LINK OD1 ASP D 62 CA CA D 309 1555 1555 2.52
LINK OD2 ASP D 62 CA CA D 309 1555 1555 2.46
LINK CA CA D 308 O HOH D 489 1555 1555 2.44
LINK CA CA D 308 O HOH D 563 1555 1555 2.55
LINK CA CA D 308 O HOH D 639 1555 1555 2.25
LINK CA CA D 308 O HOH D 646 1555 1555 2.16
LINK CA CA D 309 O4 PO4 D 312 1555 1555 2.37
LINK CA CA D 309 O HOH D 427 1555 1555 2.32
LINK CA CA D 309 O HOH D 479 1555 1555 2.54
LINK CA CA D 309 O HOH D 530 1555 1555 2.35
LINK CA CA D 309 O HOH D 578 1555 1555 2.30
LINK O GLU F 45 CA CA F 305 1555 1555 2.34
LINK O ALA F 47 CA CA F 305 1555 1555 2.55
LINK CA CA F 305 O HOH F 412 1555 1555 2.43
LINK CA CA F 305 O HOH F 499 1555 1555 2.34
LINK CA CA F 305 O HOH F 600 1555 1555 2.31
LINK CA CA F 305 O HOH F 667 1555 1555 2.39
CISPEP 1 LEU A 206 PRO A 207 0 -14.22
CISPEP 2 SER A 217 PRO A 218 0 -0.58
CISPEP 3 LEU B 206 PRO B 207 0 -16.37
CISPEP 4 SER B 217 PRO B 218 0 0.78
CISPEP 5 LEU C 206 PRO C 207 0 -11.79
CISPEP 6 SER C 217 PRO C 218 0 0.30
CISPEP 7 LEU E 206 PRO E 207 0 -14.86
CISPEP 8 SER E 217 PRO E 218 0 1.52
CISPEP 9 LEU D 206 PRO D 207 0 -15.45
CISPEP 10 SER D 217 PRO D 218 0 0.45
CISPEP 11 LEU F 206 PRO F 207 0 -13.86
CISPEP 12 SER F 217 PRO F 218 0 0.84
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 8261 LEU B 269
TER 12443 LEU C 269
TER 16577 LEU E 269
TER 20678 LEU D 269
TER 24781 LEU F 269
MASTER 781 0 93 66 60 0 0 615615 6 2067 138
END |