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HEADER HYDROLASE 12-DEC-19 6TP8
TITLE SUBSTRATE PROTEIN INTERACTIONS IN THE LIMBUS REGION OF THE CATALYTIC
TITLE 2 SITE OF CANDIDA ANTARCTICA LIPASE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS LIPASE, FATTY ACID/METABOLISM, LIPID CHEMISTRY, INTERFACIAL
KEYWDS 2 ENZYMOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CIANCI,L.SILVESTRINI
REVDAT 1 20-MAY-20 6TP8 0
JRNL AUTH L.SILVESTRINI,M.CIANCI
JRNL TITL PRINCIPLES OF LIPID-ENZYME INTERACTIONS IN THE LIMBUS REGION
JRNL TITL 2 OF THE CATALYTIC SITE OF CANDIDA ANTARCTICA LIPASE B.
JRNL REF INT.J.BIOL.MACROMOL. V. 158 358 2020
JRNL REFN ISSN 0141-8130
JRNL PMID 32380114
JRNL DOI 10.1016/J.IJBIOMAC.2020.04.061
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 138777
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 7001
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 67.6900 - 4.8200 0.99 4679 231 0.1445 0.1468
REMARK 3 2 4.8200 - 3.8200 1.00 4563 207 0.1171 0.1303
REMARK 3 3 3.8200 - 3.3400 1.00 4471 249 0.1293 0.1562
REMARK 3 4 3.3400 - 3.0300 1.00 4497 235 0.1490 0.1644
REMARK 3 5 3.0300 - 2.8200 1.00 4426 247 0.1529 0.1664
REMARK 3 6 2.8200 - 2.6500 1.00 4453 227 0.1528 0.1973
REMARK 3 7 2.6500 - 2.5200 1.00 4471 207 0.1526 0.1671
REMARK 3 8 2.5200 - 2.4100 1.00 4430 232 0.1483 0.1751
REMARK 3 9 2.4100 - 2.3200 1.00 4387 234 0.1507 0.2050
REMARK 3 10 2.3200 - 2.2400 1.00 4377 252 0.1547 0.1998
REMARK 3 11 2.2400 - 2.1700 0.99 4415 226 0.1551 0.1897
REMARK 3 12 2.1700 - 2.1000 0.99 4383 254 0.1627 0.1992
REMARK 3 13 2.1000 - 2.0500 0.99 4366 255 0.1677 0.2206
REMARK 3 14 2.0500 - 2.0000 0.99 4408 206 0.1689 0.2180
REMARK 3 15 2.0000 - 1.9500 0.99 4410 219 0.1686 0.1995
REMARK 3 16 1.9500 - 1.9100 0.99 4318 272 0.1780 0.2139
REMARK 3 17 1.9100 - 1.8700 0.99 4331 245 0.1879 0.2137
REMARK 3 18 1.8700 - 1.8400 0.99 4396 222 0.1929 0.2489
REMARK 3 19 1.8400 - 1.8000 0.99 4383 179 0.2068 0.2811
REMARK 3 20 1.8000 - 1.7700 0.99 4389 217 0.2279 0.2567
REMARK 3 21 1.7700 - 1.7500 0.99 4351 247 0.2521 0.3156
REMARK 3 22 1.7500 - 1.7200 0.99 4306 266 0.2496 0.3055
REMARK 3 23 1.7200 - 1.6900 0.99 4344 240 0.2374 0.2663
REMARK 3 24 1.6900 - 1.6700 0.99 4311 226 0.2376 0.2926
REMARK 3 25 1.6700 - 1.6500 0.99 4345 248 0.2466 0.2576
REMARK 3 26 1.6500 - 1.6300 0.99 4341 232 0.2590 0.2670
REMARK 3 27 1.6300 - 1.6100 0.99 4309 232 0.2711 0.3014
REMARK 3 28 1.6100 - 1.5900 0.98 4303 225 0.2749 0.3070
REMARK 3 29 1.5900 - 1.5700 0.98 4317 250 0.3020 0.2890
REMARK 3 30 1.5700 - 1.5500 0.97 4296 219 0.3178 0.3524
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.037
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.85
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 7388
REMARK 3 ANGLE : 0.904 10151
REMARK 3 CHIRALITY : 0.052 1191
REMARK 3 PLANARITY : 0.006 1324
REMARK 3 DIHEDRAL : 5.625 5935
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 6TP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105828.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.824
REMARK 200 MONOCHROMATOR : SI (III)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138806
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 67.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1TCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION TRIALS WERE PERFORMED
REMARK 280 AT 293 K USING THE HANGING-DROP METHOD USING A QIAGEN EASYXTAL
REMARK 280 15-WELL PLATE. A 15 MG.ML CALB SOLUTION IN 20MM NA(CH3COO) PH =
REMARK 280 4.8 WAS INCUBATED WITH A SOLUTION OF PARAOXON-ETHYL (SIGMA
REMARK 280 CATALOG N. N12816) 30MM IN WATER FOR ONE DAY. 1 UL OF CALB
REMARK 280 SOLUTION WAS DILUTED WITH 1 UL OF THE PRECIPITANT SOLUTION, MADE
REMARK 280 OF 200MM NA(CH3COO) PH = 4.8, 20% (W.V) PEG4000, AND 15% (V.V)
REMARK 280 GLYCERYL TRIBUTYRATE (SIGMA CATALOG N. T8626). THE DROP WAS
REMARK 280 EQUILIBRATED BY VAPOR DIFFUSION AGAINST 500 UL OF THE
REMARK 280 PRECIPITANT SOLUTION. PROTEIN CRYSTALS OF THE CALB COMPLEX
REMARK 280 APPEARED WITHIN TWO WEEKS AND GREW TO A SIZE OF 0.1 X 0.1 X 0.05
REMARK 280 MM3 IN FIVE WEEKS., PH 4.8, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.04200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.04200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.71300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.32700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.71300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.32700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.04200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.71300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.32700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.04200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.71300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.32700
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 69.04200
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 900 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 988 LIES ON A SPECIAL POSITION.
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 ND2 ASN C 74 O5 NAG C 403 2.16
REMARK 500 NH2 ARG C 249 O HOH C 501 2.17
REMARK 500 ND2 ASN A 74 O5 NAG A 402 2.18
REMARK 500 ND2 ASN B 74 O5 NAG B 402 2.19
REMARK 500 O HOH A 569 O HOH A 789 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 O HOH A 798 O HOH C 752 8445 2.13
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 SER A 29 85.86 -160.24
REMARK 500 ASN A 51 -91.24 -150.00
REMARK 500 ASP A 75 113.90 -30.74
REMARK 500 SER A 105 -124.17 52.91
REMARK 500 ASP A 134 67.05 -113.50
REMARK 500 THR A 186 48.68 -98.17
REMARK 500 ALA A 305 37.12 -142.60
REMARK 500 SER B 29 88.74 -155.35
REMARK 500 ASN B 51 -92.72 -153.25
REMARK 500 ASP B 75 113.23 -29.96
REMARK 500 SER B 105 -121.67 54.64
REMARK 500 ASP B 134 66.59 -111.46
REMARK 500 THR B 186 53.12 -95.21
REMARK 500 ASN B 206 -0.85 70.56
REMARK 500 ALA B 305 37.77 -143.37
REMARK 500 THR B 310 -169.70 -126.62
REMARK 500 SER C 29 89.68 -156.03
REMARK 500 ASN C 51 -92.63 -156.31
REMARK 500 ASP C 75 114.89 -30.83
REMARK 500 SER C 105 -122.59 51.73
REMARK 500 ASP C 134 67.37 -113.16
REMARK 500 THR C 186 46.96 -92.71
REMARK 500 ASN C 206 -2.86 71.69
REMARK 500 ALA C 305 38.13 -143.15
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 986 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 987 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 988 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 989 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 990 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 991 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 992 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 993 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 994 DISTANCE = 8.23 ANGSTROMS
REMARK 525 HOH B 959 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 960 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 961 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 962 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 963 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B 964 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH B 965 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH B 966 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH B 967 DISTANCE = 8.29 ANGSTROMS
REMARK 525 HOH B 968 DISTANCE = 8.43 ANGSTROMS
REMARK 525 HOH C 992 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 993 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 994 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C 995 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH C 996 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH C 997 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH C 998 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH C 999 DISTANCE = 6.91 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DEP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NTK A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NTK C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 402 through NAG A 403 bound to ASN A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 402 through NAG B 403 bound to ASN B 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 403 through NAG C 404 bound to ASN C 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DEP B 401 and SER B
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DEP C 402 and SER C
REMARK 800 105
DBREF 6TP8 A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6TP8 B 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6TP8 C 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 A 317 GLY ILE VAL THR PRO
SEQRES 1 B 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 B 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 B 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 B 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 B 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 B 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 B 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 B 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 B 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 B 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 B 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 B 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 B 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 B 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 B 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 B 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 B 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 B 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 B 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 B 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 B 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 B 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 B 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 B 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 B 317 GLY ILE VAL THR PRO
SEQRES 1 C 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 C 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 C 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 C 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 C 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 C 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 C 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 C 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 C 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 C 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 C 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 C 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 C 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 C 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 C 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 C 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 C 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 C 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 C 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 C 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 C 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 C 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 C 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 C 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 C 317 GLY ILE VAL THR PRO
HET DEP A 401 8
HET NAG A 402 14
HET NAG A 403 14
HET NTK A 404 21
HET DEP B 401 8
HET NAG B 402 14
HET NAG B 403 14
HET NTK C 401 21
HET DEP C 402 8
HET NAG C 403 14
HET NAG C 404 14
HETNAM DEP DIETHYL PHOSPHONATE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NTK 2,3-DI(BUTANOYLOXY)PROPYL BUTANOATE
FORMUL 4 DEP 3(C4 H11 O3 P)
FORMUL 5 NAG 6(C8 H15 N O6)
FORMUL 6 NTK 2(C15 H26 O6)
FORMUL 12 HOH *1461(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 SER A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 THR A 138 LEU A 140 5 3
HELIX 8 AA8 ALA A 141 LEU A 147 1 7
HELIX 9 AA9 ALA A 151 GLN A 157 1 7
HELIX 10 AB1 SER A 161 ALA A 170 1 10
HELIX 11 AB2 ALA A 212 GLY A 217 1 6
HELIX 12 AB3 ALA A 225 SER A 230 1 6
HELIX 13 AB4 SER A 230 SER A 243 1 14
HELIX 14 AB5 ARG A 249 TYR A 253 5 5
HELIX 15 AB6 GLY A 254 CYS A 258 5 5
HELIX 16 AB7 THR A 267 ALA A 276 1 10
HELIX 17 AB8 LEU A 277 GLY A 288 1 12
HELIX 18 AB9 ALA A 301 ALA A 305 5 5
HELIX 19 AC1 PRO B 12 GLY B 19 1 8
HELIX 20 AC2 THR B 43 ASP B 49 1 7
HELIX 21 AC3 ASN B 51 LEU B 59 1 9
HELIX 22 AC4 ASP B 75 SER B 94 1 20
HELIX 23 AC5 SER B 105 PHE B 118 1 14
HELIX 24 AC6 PRO B 119 ARG B 122 5 4
HELIX 25 AC7 THR B 138 LEU B 140 5 3
HELIX 26 AC8 ALA B 141 LEU B 147 1 7
HELIX 27 AC9 ALA B 151 GLN B 157 1 7
HELIX 28 AD1 SER B 161 ALA B 170 1 10
HELIX 29 AD2 ALA B 212 GLY B 217 1 6
HELIX 30 AD3 ALA B 225 SER B 230 1 6
HELIX 31 AD4 SER B 230 SER B 243 1 14
HELIX 32 AD5 ARG B 249 TYR B 253 5 5
HELIX 33 AD6 GLY B 254 CYS B 258 5 5
HELIX 34 AD7 THR B 267 ALA B 276 1 10
HELIX 35 AD8 LEU B 277 GLY B 288 1 12
HELIX 36 AD9 ALA B 301 VAL B 306 5 6
HELIX 37 AE1 PRO C 12 GLY C 19 1 8
HELIX 38 AE2 THR C 43 ASP C 49 1 7
HELIX 39 AE3 ASN C 51 LEU C 59 1 9
HELIX 40 AE4 ASP C 75 SER C 94 1 20
HELIX 41 AE5 SER C 105 PHE C 118 1 14
HELIX 42 AE6 PRO C 119 ARG C 122 5 4
HELIX 43 AE7 THR C 138 LEU C 140 5 3
HELIX 44 AE8 ALA C 141 LEU C 147 1 7
HELIX 45 AE9 ALA C 151 GLN C 157 1 7
HELIX 46 AF1 SER C 161 ALA C 170 1 10
HELIX 47 AF2 ALA C 212 GLY C 217 1 6
HELIX 48 AF3 ALA C 225 SER C 230 1 6
HELIX 49 AF4 SER C 230 SER C 243 1 14
HELIX 50 AF5 ARG C 249 TYR C 253 5 5
HELIX 51 AF6 GLY C 254 CYS C 258 5 5
HELIX 52 AF7 THR C 267 ALA C 276 1 10
HELIX 53 AF8 LEU C 277 GLY C 288 1 12
HELIX 54 AF9 ALA C 301 ALA C 305 5 5
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N ILE A 34 O CYS A 64
SHEET 4 AA1 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N ILE B 34 O CYS B 64
SHEET 4 AA3 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SHEET 1 AA5 7 LEU C 20 CYS C 22 0
SHEET 2 AA5 7 THR C 62 ILE C 66 -1 O TRP C 65 N THR C 21
SHEET 3 AA5 7 PRO C 33 VAL C 37 1 N LEU C 36 O CYS C 64
SHEET 4 AA5 7 LEU C 99 TRP C 104 1 O LEU C 102 N LEU C 35
SHEET 5 AA5 7 VAL C 125 PHE C 131 1 O MET C 129 N VAL C 101
SHEET 6 AA5 7 THR C 179 TYR C 183 1 O THR C 180 N ALA C 130
SHEET 7 AA5 7 LYS C 208 GLN C 211 1 O VAL C 210 N ASN C 181
SHEET 1 AA6 2 ARG C 309 THR C 310 0
SHEET 2 AA6 2 GLY C 313 ILE C 314 -1 O GLY C 313 N THR C 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.04
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.03
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.03
SSBOND 7 CYS C 22 CYS C 64 1555 1555 2.03
SSBOND 8 CYS C 216 CYS C 258 1555 1555 2.03
SSBOND 9 CYS C 293 CYS C 311 1555 1555 2.04
LINK ND2 ASN A 74 C1 NAG A 402 1555 1555 1.43
LINK OG SER A 105 P DEP A 401 1555 1555 1.56
LINK ND2 ASN B 74 C1 NAG B 402 1555 1555 1.44
LINK OG SER B 105 P DEP B 401 1555 1555 1.56
LINK ND2 ASN C 74 C1 NAG C 403 1555 1555 1.44
LINK OG SER C 105 P DEP C 402 1555 1555 1.56
LINK O4 NAG A 402 C1 NAG A 403 1555 1555 1.44
LINK O4 NAG B 402 C1 NAG B 403 1555 1555 1.44
LINK O4 NAG C 403 C1 NAG C 404 1555 1555 1.45
CISPEP 1 PRO A 69 PRO A 70 0 -10.50
CISPEP 2 GLN A 191 PRO A 192 0 3.07
CISPEP 3 PRO B 69 PRO B 70 0 -12.74
CISPEP 4 GLN B 191 PRO B 192 0 3.56
CISPEP 5 PRO C 69 PRO C 70 0 -10.28
CISPEP 6 GLN C 191 PRO C 192 0 2.66
SITE 1 AC1 8 THR A 40 SER A 105 GLN A 106 THR A 138
SITE 2 AC1 8 GLN A 157 ILE A 189 HIS A 224 NTK A 404
SITE 1 AC2 15 GLU A 188 ILE A 189 LEU A 278 ALA A 282
SITE 2 AC2 15 ILE A 285 DEP A 401 HOH A 619 HOH A 718
SITE 3 AC2 15 HOH A 721 HOH A 780 ILE B 189 LEU B 278
SITE 4 AC2 15 ALA B 282 ILE B 285 HOH B 786
SITE 1 AC3 9 GLU C 188 ILE C 189 LEU C 278 ALA C 279
SITE 2 AC3 9 ALA C 282 ILE C 285 HOH C 508 HOH C 520
SITE 3 AC3 9 HOH C 838
SITE 1 AC4 9 PRO A 70 ASN A 74 HOH A 505 HOH A 520
SITE 2 AC4 9 HOH A 557 HOH A 615 HOH A 620 HOH A 724
SITE 3 AC4 9 HOH A 775
SITE 1 AC5 5 ASN B 74 HOH B 506 HOH B 518 HOH B 732
SITE 2 AC5 5 HOH B 751
SITE 1 AC6 7 ASN C 74 HOH C 509 HOH C 548 HOH C 638
SITE 2 AC6 7 HOH C 686 HOH C 748 HOH C 773
SITE 1 AC7 14 THR B 40 TRP B 104 GLN B 106 GLY B 107
SITE 2 AC7 14 GLY B 108 PHE B 131 ALA B 132 PRO B 133
SITE 3 AC7 14 ASP B 134 THR B 138 GLN B 157 ILE B 189
SITE 4 AC7 14 HIS B 224 HOH B 678
SITE 1 AC8 14 THR C 40 TRP C 104 GLN C 106 GLY C 107
SITE 2 AC8 14 GLY C 108 PHE C 131 ALA C 132 PRO C 133
SITE 3 AC8 14 ASP C 134 THR C 138 GLN C 157 ILE C 189
SITE 4 AC8 14 HIS C 224 HOH C 662
CRYST1 89.426 156.654 138.084 90.00 90.00 90.00 C 2 2 21 24
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 0.011182 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007242 0.00000
TER 2344 PRO A 317
TER 4691 PRO B 317
TER 7044 PRO C 317
MASTER 422 0 11 54 27 0 24 6 8583 3 174 75
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