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HEADER TRANSFERASE 11-DEC-14 4X97
TITLE CRYSTAL STRUCTURE OF LYSOSOMAL PHOSPHOLIPASE A2 IN COMPLEX WITH METHYL
TITLE 2 ARACHIDONYL FLUOROPHOSPHONATE (MAFP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROUP XV PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 34-412;
COMPND 5 SYNONYM: 1-O-ACYLCERAMIDE SYNTHASE,ACS,LCAT-LIKE LYSOPHOSPHOLIPASE,
COMPND 6 LLPL,LYSOPHOSPHOLIPASE 3,LYSOSOMAL PHOSPHOLIPASE A2,LPLA2;
COMPND 7 EC: 2.3.1.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: LPLA2 IS COVALENTLY LINKED TO MAFP VIA S165
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLA2G15, LYPLA3, UNQ341/PRO540;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022
KEYWDS HYDROLASE, PHOSPHOLIPASE, MAFP, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 11-MAR-15 4X97 0
JRNL AUTH A.GLUKHOVA,V.HINKOVSKA-GALCHEVA,R.KELLY,A.ABE,J.A.SHAYMAN,
JRNL AUTH 2 J.J.G.TESMER
JRNL TITL STRUCTURE AND FUNCTION OF LYSOSOMAL PHOSPHOLIPASE A2 AND
JRNL TITL 2 LECITHIN:CHOLESTEROL ACYLTRANSFERASE
JRNL REF NAT COMMUN 2015
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/NCOMMS7250
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 49603
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2558
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1905
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12098
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 372
REMARK 3 SOLVENT ATOMS : 232
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.30000
REMARK 3 B22 (A**2) : -1.00000
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : 1.46000
REMARK 3 B13 (A**2) : -0.29000
REMARK 3 B23 (A**2) : -0.70000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.305
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.048
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12917 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12020 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17610 ; 1.788 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27623 ; 1.262 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1524 ; 6.160 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 581 ;35.427 ;23.494
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2018 ;14.054 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 82 ;15.994 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1901 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14344 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3008 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6051 ; 2.018 ; 2.238
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6050 ; 2.014 ; 2.237
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7566 ; 3.282 ; 3.352
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 379 B 3 379 24368 0.060 0.050
REMARK 3 2 A 4 378 C 4 378 24181 0.060 0.050
REMARK 3 3 A 4 378 D 4 378 24133 0.070 0.050
REMARK 3 4 B 4 378 C 4 378 24320 0.060 0.050
REMARK 3 5 B 4 378 D 4 378 24424 0.050 0.050
REMARK 3 6 C 4 379 D 4 379 24222 0.060 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 405
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4835 -18.0773 -16.5478
REMARK 3 T TENSOR
REMARK 3 T11: 0.1050 T22: 0.0888
REMARK 3 T33: 0.0725 T12: 0.0283
REMARK 3 T13: -0.0708 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.5954 L22: 1.8002
REMARK 3 L33: 1.0249 L12: -0.3895
REMARK 3 L13: -0.1901 L23: 0.5200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: -0.0019 S13: -0.0745
REMARK 3 S21: 0.0409 S22: -0.0741 S23: -0.0084
REMARK 3 S31: 0.1808 S32: -0.0187 S33: -0.0251
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8736 21.5879 -20.8039
REMARK 3 T TENSOR
REMARK 3 T11: 0.0471 T22: 0.0951
REMARK 3 T33: 0.0080 T12: 0.0459
REMARK 3 T13: -0.0154 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 1.0194 L22: 1.0593
REMARK 3 L33: 0.9541 L12: -0.3258
REMARK 3 L13: 0.4644 L23: -0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: 0.0321 S13: -0.0015
REMARK 3 S21: -0.1371 S22: -0.0913 S23: 0.0240
REMARK 3 S31: -0.0664 S32: 0.0277 S33: 0.0166
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 405
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0705 17.0069 18.5370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: 0.0878
REMARK 3 T33: 0.0247 T12: 0.0406
REMARK 3 T13: -0.0609 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.5529 L22: 1.3034
REMARK 3 L33: 1.8902 L12: -0.2188
REMARK 3 L13: -0.0207 L23: 0.7891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0853 S12: -0.0256 S13: 0.0381
REMARK 3 S21: 0.3478 S22: 0.0639 S23: -0.0864
REMARK 3 S31: 0.1792 S32: 0.0300 S33: 0.0214
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 405
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4482 -24.1074 23.5394
REMARK 3 T TENSOR
REMARK 3 T11: 0.1578 T22: 0.1326
REMARK 3 T33: 0.0683 T12: 0.0226
REMARK 3 T13: -0.0049 T23: 0.0511
REMARK 3 L TENSOR
REMARK 3 L11: 0.9455 L22: 2.3347
REMARK 3 L33: 3.4184 L12: -1.0609
REMARK 3 L13: 0.9555 L23: -1.9260
REMARK 3 S TENSOR
REMARK 3 S11: -0.0985 S12: -0.1003 S13: -0.1550
REMARK 3 S21: 0.3788 S22: 0.3992 S23: 0.2629
REMARK 3 S31: -0.1391 S32: -0.4497 S33: -0.3007
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4X97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52162
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 4.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.20
REMARK 200 R MERGE FOR SHELL (I) : 0.57300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 4X90
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 3.5% PEG 8000,
REMARK 280 28% MPD, 300 MM (NH4)2HPO4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 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 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 GLY A 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 GLY B 0
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 GLY C 0
REMARK 465 ALA C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY D 0
REMARK 465 ALA D 1
REMARK 465 GLY D 2
REMARK 465 ARG D 3
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 256 C2 NAG C 403 1.95
REMARK 500 ND2 ASN D 256 O5 NAG D 403 2.02
REMARK 500 SG CYS D 297 O HOH D 523 2.03
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 OG SER A 33 OG SER B 33 1655 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 110 CG GLU C 110 CD 0.091
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 23 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LEU B 91 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 145 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASN C 213 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP D 307 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 52 -59.38 74.71
REMARK 500 TYR A 104 -79.47 -124.09
REMARK 500 GLU A 121 -91.19 -115.85
REMARK 500 ALA A 126 63.44 -119.28
REMARK 500 SER A 165 -127.32 52.10
REMARK 500 THR A 329 -55.25 -128.85
REMARK 500 VAL B 52 -59.31 74.42
REMARK 500 TYR B 104 -79.47 -125.22
REMARK 500 GLU B 121 -91.23 -115.43
REMARK 500 ALA B 126 63.43 -119.54
REMARK 500 SER B 165 -127.19 53.98
REMARK 500 THR B 329 -58.09 -129.16
REMARK 500 ASP C 23 66.97 -150.19
REMARK 500 VAL C 52 -59.15 74.74
REMARK 500 TYR C 104 -80.72 -125.61
REMARK 500 GLU C 121 -92.65 -115.88
REMARK 500 SER C 165 -127.99 55.80
REMARK 500 ILE C 215 62.53 -167.10
REMARK 500 THR C 329 -55.55 -129.64
REMARK 500 ASP D 23 67.97 -150.67
REMARK 500 VAL D 52 -59.81 74.95
REMARK 500 TYR D 104 -80.30 -124.78
REMARK 500 GLU D 121 -91.79 -116.48
REMARK 500 ALA D 126 64.19 -119.97
REMARK 500 SER D 165 -127.86 53.57
REMARK 500 THR D 329 -57.32 -128.64
REMARK 500
REMARK 500 REMARK: NULL
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 MAY A 405
REMARK 610 MAY B 405
REMARK 610 MAY C 405
REMARK 610 MAY D 405
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MAY A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound
REMARK 800 to ASN A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound
REMARK 800 to ASN A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 403 bound
REMARK 800 to ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 404 bound
REMARK 800 to ASN A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound
REMARK 800 to ASN B 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound
REMARK 800 to ASN B 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 403 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 404 bound
REMARK 800 to ASN B 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 401 bound
REMARK 800 to ASN C 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 402 bound
REMARK 800 to ASN C 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 403 bound
REMARK 800 to ASN C 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 404 bound
REMARK 800 to ASN C 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 401 bound
REMARK 800 to ASN D 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 402 bound
REMARK 800 to ASN D 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 403 bound
REMARK 800 to ASN D 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 404 bound
REMARK 800 to ASN D 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MAY B 405 and SER B
REMARK 800 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MAY C 405 and SER C
REMARK 800 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MAY D 405 and SER D
REMARK 800 165
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X90 RELATED DB: PDB
REMARK 900 RELATED ID: 4X91 RELATED DB: PDB
REMARK 900 RELATED ID: 4X93 RELATED DB: PDB
REMARK 900 RELATED ID: 4X94 RELATED DB: PDB
REMARK 900 RELATED ID: 4X95 RELATED DB: PDB
REMARK 900 RELATED ID: 4X96 RELATED DB: PDB
REMARK 900 RELATED ID: 4X92 RELATED DB: PDB
DBREF 4X97 A 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X97 B 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X97 C 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X97 D 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
SEQADV 4X97 GLY A 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X97 GLY B 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X97 GLY C 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X97 GLY D 0 UNP Q8NCC3 CLONING ARTIFACT
SEQRES 1 A 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 A 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 A 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 A 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 A 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 A 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 A 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 A 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 A 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 A 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 A 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 A 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 A 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 A 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 A 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 A 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 A 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 A 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 A 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 A 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 A 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 A 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 A 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 A 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 A 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 A 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 A 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 A 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 A 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 A 380 LEU GLY PRO
SEQRES 1 B 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 B 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 B 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 B 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 B 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 B 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 B 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 B 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 B 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 B 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 B 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 B 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 B 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 B 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 B 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 B 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 B 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 B 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 B 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 B 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 B 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 B 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 B 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 B 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 B 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 B 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 B 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 B 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 B 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 B 380 LEU GLY PRO
SEQRES 1 C 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 C 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 C 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 C 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 C 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 C 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 C 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 C 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 C 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 C 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 C 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 C 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 C 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 C 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 C 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 C 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 C 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 C 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 C 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 C 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 C 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 C 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 C 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 C 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 C 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 C 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 C 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 C 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 C 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 C 380 LEU GLY PRO
SEQRES 1 D 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 D 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 D 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 D 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 D 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 D 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 D 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 D 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 D 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 D 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 D 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 D 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 D 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 D 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 D 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 D 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 D 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 D 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 D 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 D 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 D 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 D 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 D 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 D 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 D 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 D 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 D 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 D 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 D 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 D 380 LEU GLY PRO
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET NAG A 404 14
HET MAY A 405 20
HET EPE A 406 15
HET PO4 A 407 5
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 14
HET NAG B 404 14
HET MAY B 405 18
HET EPE B 406 15
HET CL B 407 1
HET PO4 B 408 5
HET NAG C 401 14
HET NAG C 402 14
HET NAG C 403 14
HET NAG C 404 14
HET MAY C 405 19
HET EPE C 406 15
HET PO4 C 407 5
HET NAG D 401 14
HET NAG D 402 14
HET NAG D 403 14
HET NAG D 404 14
HET MAY D 405 10
HET EPE D 406 15
HET PO4 D 407 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAY METHYL ARACHIDONYL FLUOROPHOSPHONATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETSYN MAY MAFP
HETSYN EPE HEPES
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 9 MAY 4(C21 H36 F O2 P)
FORMUL 10 EPE 4(C8 H18 N2 O4 S)
FORMUL 11 PO4 4(O4 P 3-)
FORMUL 18 CL CL 1-
FORMUL 34 HOH *232(H2 O)
HELIX 1 AA1 ASN A 45 LEU A 50 5 6
HELIX 2 AA2 VAL A 52 ARG A 62 1 11
HELIX 3 AA3 THR A 88 PHE A 93 1 6
HELIX 4 AA4 SER A 99 SER A 103 5 5
HELIX 5 AA5 PHE A 105 TRP A 115 1 11
HELIX 6 AA6 ALA A 133 GLU A 136 5 4
HELIX 7 AA7 ASN A 137 GLY A 156 1 20
HELIX 8 AA8 MET A 166 ARG A 177 1 12
HELIX 9 AA9 PRO A 179 TYR A 186 1 8
HELIX 10 AB1 ALA A 201 GLY A 210 1 10
HELIX 11 AB2 GLY A 219 ALA A 230 1 12
HELIX 12 AB3 ALA A 230 LEU A 236 1 7
HELIX 13 AB4 ASP A 261 ILE A 269 1 9
HELIX 14 AB5 PHE A 271 GLU A 282 1 12
HELIX 15 AB6 ASN A 331 LEU A 336 1 6
HELIX 16 AB7 LEU A 336 TRP A 341 1 6
HELIX 17 AB8 GLN A 342 ARG A 344 5 3
HELIX 18 AB9 ILE A 360 ALA A 364 5 5
HELIX 19 AC1 ASN A 365 GLY A 378 1 14
HELIX 20 AC2 ASN B 45 LEU B 49 5 5
HELIX 21 AC3 VAL B 52 ARG B 62 1 11
HELIX 22 AC4 THR B 88 PHE B 93 1 6
HELIX 23 AC5 SER B 99 SER B 103 5 5
HELIX 24 AC6 PHE B 105 TRP B 115 1 11
HELIX 25 AC7 ALA B 133 GLU B 136 5 4
HELIX 26 AC8 ASN B 137 GLY B 156 1 20
HELIX 27 AC9 MET B 166 ARG B 177 1 12
HELIX 28 AD1 PRO B 179 TYR B 186 1 8
HELIX 29 AD2 ALA B 201 GLY B 210 1 10
HELIX 30 AD3 GLY B 219 ALA B 230 1 12
HELIX 31 AD4 ALA B 230 LEU B 236 1 7
HELIX 32 AD5 ASP B 261 GLY B 270 1 10
HELIX 33 AD6 GLU B 272 GLU B 282 1 11
HELIX 34 AD7 ASN B 331 LEU B 336 1 6
HELIX 35 AD8 GLN B 337 ARG B 344 5 8
HELIX 36 AD9 ILE B 360 ALA B 364 5 5
HELIX 37 AE1 ASN B 365 GLY B 378 1 14
HELIX 38 AE2 ASN C 45 LEU C 50 5 6
HELIX 39 AE3 VAL C 52 ARG C 62 1 11
HELIX 40 AE4 THR C 88 PHE C 93 1 6
HELIX 41 AE5 SER C 99 SER C 103 5 5
HELIX 42 AE6 PHE C 105 TRP C 115 1 11
HELIX 43 AE7 ALA C 133 GLU C 136 5 4
HELIX 44 AE8 ASN C 137 GLY C 156 1 20
HELIX 45 AE9 MET C 166 ARG C 177 1 12
HELIX 46 AF1 PRO C 179 TYR C 186 1 8
HELIX 47 AF2 ALA C 201 GLY C 210 1 10
HELIX 48 AF3 GLY C 219 ALA C 230 1 12
HELIX 49 AF4 ALA C 230 LEU C 236 1 7
HELIX 50 AF5 ASP C 261 ILE C 269 1 9
HELIX 51 AF6 GLU C 272 GLU C 282 1 11
HELIX 52 AF7 ASN C 331 LEU C 336 1 6
HELIX 53 AF8 GLN C 337 ARG C 344 5 8
HELIX 54 AF9 ILE C 360 ALA C 364 5 5
HELIX 55 AG1 ASN C 365 GLY C 378 1 14
HELIX 56 AG2 ASN D 45 LEU D 50 5 6
HELIX 57 AG3 VAL D 52 ARG D 62 1 11
HELIX 58 AG4 THR D 88 PHE D 93 1 6
HELIX 59 AG5 SER D 99 SER D 103 5 5
HELIX 60 AG6 PHE D 105 TRP D 115 1 11
HELIX 61 AG7 ALA D 133 GLU D 136 5 4
HELIX 62 AG8 ASN D 137 GLY D 156 1 20
HELIX 63 AG9 MET D 166 ARG D 177 1 12
HELIX 64 AH1 PRO D 179 TYR D 186 1 8
HELIX 65 AH2 ALA D 201 GLY D 210 1 10
HELIX 66 AH3 GLY D 219 ALA D 230 1 12
HELIX 67 AH4 ALA D 230 LEU D 236 1 7
HELIX 68 AH5 ASP D 261 GLY D 270 1 10
HELIX 69 AH6 GLU D 272 GLU D 282 1 11
HELIX 70 AH7 ASN D 331 LEU D 336 1 6
HELIX 71 AH8 GLN D 337 ARG D 344 5 8
HELIX 72 AH9 ILE D 360 ALA D 364 5 5
HELIX 73 AI1 ASN D 365 GLY D 378 1 14
SHEET 1 AA1 6 VAL A 123 GLY A 125 0
SHEET 2 AA1 6 VAL A 7 VAL A 10 1 N LEU A 9 O ARG A 124
SHEET 3 AA1 6 VAL A 159 HIS A 164 1 O VAL A 162 N VAL A 8
SHEET 4 AA1 6 ILE A 187 LEU A 193 1 O VAL A 191 N LEU A 161
SHEET 5 AA1 6 LEU A 295 THR A 301 1 O HIS A 296 N SER A 192
SHEET 6 AA1 6 VAL A 349 PRO A 355 1 O LEU A 350 N CYS A 297
SHEET 1 AA2 3 PHE A 40 TRP A 43 0
SHEET 2 AA2 3 LEU A 18 LEU A 22 -1 N ALA A 20 O PHE A 40
SHEET 3 AA2 3 VAL A 78 ARG A 81 -1 O ARG A 81 N GLU A 19
SHEET 1 AA3 2 VAL A 64 ASN A 66 0
SHEET 2 AA3 2 ALA A 71 GLN A 73 -1 O GLN A 73 N VAL A 64
SHEET 1 AA4 4 ASN A 256 TYR A 257 0
SHEET 2 AA4 4 VAL A 250 GLN A 251 -1 N VAL A 250 O TYR A 257
SHEET 3 AA4 4 THR A 305 TYR A 310 1 O PHE A 309 N GLN A 251
SHEET 4 AA4 4 LYS A 320 GLY A 324 -1 O CYS A 322 N ASP A 307
SHEET 1 AA5 6 VAL B 123 GLY B 125 0
SHEET 2 AA5 6 VAL B 7 VAL B 10 1 N LEU B 9 O ARG B 124
SHEET 3 AA5 6 VAL B 159 HIS B 164 1 O VAL B 162 N VAL B 8
SHEET 4 AA5 6 ILE B 187 LEU B 193 1 O VAL B 191 N LEU B 161
SHEET 5 AA5 6 LEU B 295 THR B 301 1 O HIS B 296 N SER B 192
SHEET 6 AA5 6 VAL B 349 PRO B 355 1 O LEU B 350 N CYS B 297
SHEET 1 AA6 3 PHE B 40 TRP B 43 0
SHEET 2 AA6 3 LEU B 18 LEU B 22 -1 N ALA B 20 O PHE B 40
SHEET 3 AA6 3 VAL B 78 ARG B 81 -1 O ARG B 81 N GLU B 19
SHEET 1 AA7 2 VAL B 64 ASN B 66 0
SHEET 2 AA7 2 ALA B 71 GLN B 73 -1 O GLN B 73 N VAL B 64
SHEET 1 AA8 4 ASN B 256 TYR B 257 0
SHEET 2 AA8 4 VAL B 250 GLN B 251 -1 N VAL B 250 O TYR B 257
SHEET 3 AA8 4 THR B 305 TYR B 310 1 O PHE B 309 N GLN B 251
SHEET 4 AA8 4 LYS B 320 GLY B 324 -1 O CYS B 322 N ASP B 307
SHEET 1 AA9 6 VAL C 123 GLY C 125 0
SHEET 2 AA9 6 VAL C 7 VAL C 10 1 N LEU C 9 O ARG C 124
SHEET 3 AA9 6 VAL C 159 HIS C 164 1 O VAL C 162 N VAL C 8
SHEET 4 AA9 6 ILE C 187 LEU C 193 1 O VAL C 191 N LEU C 161
SHEET 5 AA9 6 LEU C 295 THR C 301 1 O HIS C 296 N SER C 192
SHEET 6 AA9 6 VAL C 349 PRO C 355 1 O LEU C 350 N CYS C 297
SHEET 1 AB1 3 PHE C 40 TRP C 43 0
SHEET 2 AB1 3 LEU C 18 LEU C 22 -1 N ALA C 20 O PHE C 40
SHEET 3 AB1 3 VAL C 78 ARG C 81 -1 O ARG C 81 N GLU C 19
SHEET 1 AB2 2 VAL C 64 ASN C 66 0
SHEET 2 AB2 2 ALA C 71 GLN C 73 -1 O GLN C 73 N VAL C 64
SHEET 1 AB3 4 ASN C 256 TYR C 257 0
SHEET 2 AB3 4 VAL C 250 GLN C 251 -1 N VAL C 250 O TYR C 257
SHEET 3 AB3 4 THR C 305 TYR C 310 1 O PHE C 309 N GLN C 251
SHEET 4 AB3 4 LYS C 320 GLY C 324 -1 O GLY C 324 N THR C 305
SHEET 1 AB4 6 VAL D 123 GLY D 125 0
SHEET 2 AB4 6 VAL D 7 VAL D 10 1 N LEU D 9 O ARG D 124
SHEET 3 AB4 6 VAL D 159 HIS D 164 1 O VAL D 162 N VAL D 8
SHEET 4 AB4 6 ILE D 187 LEU D 193 1 O VAL D 191 N LEU D 161
SHEET 5 AB4 6 LEU D 295 THR D 301 1 O HIS D 296 N SER D 192
SHEET 6 AB4 6 VAL D 349 PRO D 355 1 O LEU D 350 N CYS D 297
SHEET 1 AB5 3 PHE D 40 TRP D 43 0
SHEET 2 AB5 3 LEU D 18 LEU D 22 -1 N ALA D 20 O PHE D 40
SHEET 3 AB5 3 VAL D 78 ARG D 81 -1 O ARG D 81 N GLU D 19
SHEET 1 AB6 2 VAL D 64 ASN D 66 0
SHEET 2 AB6 2 ALA D 71 GLN D 73 -1 O GLN D 73 N VAL D 64
SHEET 1 AB7 4 ASN D 256 TYR D 257 0
SHEET 2 AB7 4 VAL D 250 GLN D 251 -1 N VAL D 250 O TYR D 257
SHEET 3 AB7 4 THR D 305 TYR D 310 1 O PHE D 309 N GLN D 251
SHEET 4 AB7 4 LYS D 320 GLY D 324 -1 O CYS D 322 N ASP D 307
SSBOND 1 CYS A 32 CYS A 56 1555 1555 2.07
SSBOND 2 CYS B 32 CYS B 56 1555 1555 2.03
SSBOND 3 CYS C 32 CYS C 56 1555 1555 2.01
SSBOND 4 CYS D 32 CYS D 56 1555 1555 2.04
SSBOND 5 CYS A 322 CYS D 322 1555 1554 1.99
SSBOND 6 CYS B 322 CYS C 322 1555 1554 1.95
LINK ND2 ASN A 66 C1 NAG A 401 1555 1555 1.47
LINK OG SER A 165 P1 MAY A 405 1555 1555 1.58
LINK ND2 ASN A 240 C1 NAG A 402 1555 1555 1.46
LINK ND2 ASN A 256 C1 NAG A 403 1555 1555 1.48
LINK ND2 ASN A 365 C1 NAG A 404 1555 1555 1.44
LINK ND2 ASN B 66 C1 NAG B 401 1555 1555 1.42
LINK OG SER B 165 P1 MAY B 405 1555 1555 1.60
LINK ND2 ASN B 240 C1 NAG B 402 1555 1555 1.47
LINK ND2 ASN B 256 C1 NAG B 403 1555 1555 1.47
LINK ND2 ASN B 365 C1 NAG B 404 1555 1555 1.46
LINK ND2 ASN C 66 C1 NAG C 401 1555 1555 1.43
LINK OG SER C 165 P1 MAY C 405 1555 1555 1.61
LINK ND2 ASN C 240 C1 NAG C 402 1555 1555 1.43
LINK ND2 ASN C 256 C1 NAG C 403 1555 1555 1.43
LINK ND2 ASN C 365 C1 NAG C 404 1555 1555 1.43
LINK ND2 ASN D 66 C1 NAG D 401 1555 1555 1.45
LINK OG SER D 165 P1 MAY D 405 1555 1555 1.62
LINK ND2 ASN D 240 C1 NAG D 402 1555 1555 1.42
LINK ND2 ASN D 256 C1 NAG D 403 1555 1555 1.37
LINK ND2 ASN D 365 C1 NAG D 404 1555 1555 1.44
CISPEP 1 TRP A 43 LEU A 44 0 -0.95
CISPEP 2 PHE A 314 PRO A 315 0 5.44
CISPEP 3 TRP B 43 LEU B 44 0 -3.44
CISPEP 4 PHE B 314 PRO B 315 0 4.33
CISPEP 5 TRP C 43 LEU C 44 0 -3.20
CISPEP 6 PHE C 314 PRO C 315 0 2.57
CISPEP 7 TRP D 43 LEU D 44 0 -4.11
CISPEP 8 PHE D 314 PRO D 315 0 5.40
SITE 1 AC1 9 GLY A 12 ASP A 13 LEU A 94 TYR A 104
SITE 2 AC1 9 SER A 165 MET A 166 THR A 329 HIS A 359
SITE 3 AC1 9 ILE A 360
SITE 1 AC2 10 CYS A 32 SER A 33 PHE A 40 ASN A 60
SITE 2 AC2 10 HOH A 525 HOH A 557 VAL B 27 TYR B 30
SITE 3 AC2 10 CYS B 32 HOH B 502
SITE 1 AC3 5 GLN A 180 GLY A 292 GLN A 345 GLU A 346
SITE 2 AC3 5 HIS A 347
SITE 1 AC4 9 VAL A 27 TYR A 30 CYS A 32 LYS A 34
SITE 2 AC4 9 SER B 33 PHE B 40 CYS B 56 HOH B 502
SITE 3 AC4 9 HOH B 570
SITE 1 AC5 2 GLN B 294 GLN B 348
SITE 1 AC6 5 GLN B 180 GLY B 292 GLN B 345 GLU B 346
SITE 2 AC6 5 HIS B 347
SITE 1 AC7 8 CYS C 32 SER C 33 CYS C 56 ASN C 60
SITE 2 AC7 8 HOH C 539 HOH C 540 HOH C 545 HOH C 546
SITE 1 AC8 5 GLN C 180 GLY C 292 GLN C 345 GLU C 346
SITE 2 AC8 5 HIS C 347
SITE 1 AC9 4 CYS D 32 SER D 33 CYS D 56 ASN D 60
SITE 1 AD1 5 GLN D 180 GLY D 292 GLN D 345 GLU D 346
SITE 2 AD1 5 HIS D 347
SITE 1 AD2 3 ASN A 66 GLN A 73 PRO D 179
SITE 1 AD3 3 ASN A 240 GLU A 282 GLN B 267
SITE 1 AD4 8 THR A 254 ILE A 255 ASN A 256 NAG B 403
SITE 2 AD4 8 GLN D 251 THR D 252 NAG D 403 HOH D 501
SITE 1 AD5 7 LEU A 354 PRO A 355 GLY A 356 ASN A 365
SITE 2 AD5 7 THR A 367 HOH A 545 HOH A 553
SITE 1 AD6 2 ASN B 66 GLN B 73
SITE 1 AD7 5 ARG A 263 GLN A 267 ASN B 240 GLU B 282
SITE 2 AD7 5 HOH B 508
SITE 1 AD8 9 ASN A 256 NAG A 403 GLN B 251 THR B 254
SITE 2 AD8 9 ILE B 255 ASN B 256 GLN C 251 NAG C 403
SITE 3 AD8 9 NAG D 403
SITE 1 AD9 4 LEU B 354 PRO B 355 ASN B 365 HOH B 538
SITE 1 AE1 2 ASN C 66 GLN C 73
SITE 1 AE2 4 ASN C 240 GLU C 282 ARG D 263 GLN D 267
SITE 1 AE3 10 GLN B 251 NAG B 403 VAL C 248 GLN C 251
SITE 2 AE3 10 ASN C 256 THR D 254 ILE D 255 ASN D 256
SITE 3 AE3 10 NAG D 403 HOH D 501
SITE 1 AE4 4 LEU C 354 PRO C 355 SER C 357 ASN C 365
SITE 1 AE5 4 ASN D 66 THR D 68 SER D 69 GLN D 73
SITE 1 AE6 8 ARG C 263 GLN C 267 HOH C 505 ASN D 240
SITE 2 AE6 8 LEU D 259 ARG D 260 GLU D 282 HOH D 520
SITE 1 AE7 8 GLN A 251 NAG A 403 NAG B 403 THR C 254
SITE 2 AE7 8 NAG C 403 VAL D 248 GLN D 251 ASN D 256
SITE 1 AE8 4 PRO D 355 SER D 357 ASN D 365 THR D 367
SITE 1 AE9 13 GLY B 12 ASP B 13 TYR B 104 HIS B 164
SITE 2 AE9 13 MET B 166 GLY B 167 ASN B 168 LEU B 193
SITE 3 AE9 13 GLY B 194 PRO B 196 THR B 329 HIS B 359
SITE 4 AE9 13 ILE B 360
SITE 1 AF1 15 GLY C 12 ASP C 13 TRP C 43 LEU C 94
SITE 2 AF1 15 TYR C 104 HIS C 164 MET C 166 GLY C 167
SITE 3 AF1 15 ASN C 168 LEU C 193 GLY C 194 PRO C 196
SITE 4 AF1 15 ARG C 214 THR C 329 HIS C 359
SITE 1 AF2 10 GLY D 12 ASP D 13 HIS D 164 MET D 166
SITE 2 AF2 10 GLY D 167 ASN D 168 LEU D 193 GLY D 194
SITE 3 AF2 10 PRO D 196 HIS D 359
CRYST1 69.147 85.495 88.852 88.85 70.87 79.74 P 1 4
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 0.014462 -0.002619 -0.005130 0.00000
SCALE2 0.000000 0.011887 0.000491 0.00000
SCALE3 0.000000 0.000000 0.011923 0.00000
TER 3039 PRO A 379
TER 6090 PRO B 379
TER 9128 PRO C 379
TER 12163 PRO D 379
MASTER 617 0 29 73 60 0 57 612702 4 399 120
END |