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HEADER TRANSFERASE 11-DEC-14 4X91
TITLE CRYSTAL STRUCTURE OF LYSOSOMAL PHOSPHOLIPASE A2 IN COMPLEX WITH
TITLE 2 ISOPROPYL DODEC-11-ENYLFLUOROPHOSPHONATE (IDFP)
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 IDFP 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, IDFP, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 11-MAR-15 4X91 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 90314
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 : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4840
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5769
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 310
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12076
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 466
REMARK 3 SOLVENT ATOMS : 513
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.31000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : -0.39000
REMARK 3 B12 (A**2) : 0.74000
REMARK 3 B13 (A**2) : 0.49000
REMARK 3 B23 (A**2) : 1.99000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.250
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.550
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13109 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12238 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17904 ; 1.448 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 28158 ; 1.066 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1551 ; 5.744 ; 5.006
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 586 ;33.357 ;23.532
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2022 ;12.866 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 81 ;13.297 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1936 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14541 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3019 ; 0.005 ; 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): 6083 ; 1.442 ; 2.298
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6082 ; 1.442 ; 2.298
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7618 ; 2.348 ; 3.441
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 4 379 B 4 379 23679 0.080 0.050
REMARK 3 2 A 4 379 C 4 379 24234 0.050 0.050
REMARK 3 3 A 4 379 D 4 379 23686 0.080 0.050
REMARK 3 4 B 4 379 C 4 379 23686 0.070 0.050
REMARK 3 5 B 4 379 D 4 379 24185 0.050 0.050
REMARK 3 6 C 4 379 D 4 379 23684 0.070 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 4 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8369 -13.9621 21.7889
REMARK 3 T TENSOR
REMARK 3 T11: 0.0781 T22: 0.0308
REMARK 3 T33: 0.0110 T12: -0.0287
REMARK 3 T13: 0.0140 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.5181 L22: 0.9290
REMARK 3 L33: 2.2308 L12: -0.2548
REMARK 3 L13: 0.1044 L23: -0.7740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: -0.0114 S13: 0.0025
REMARK 3 S21: -0.0108 S22: -0.0165 S23: -0.0095
REMARK 3 S31: 0.1753 S32: 0.0934 S33: -0.0491
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 4 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1266 -27.8367 -25.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.0355
REMARK 3 T33: 0.0064 T12: 0.0099
REMARK 3 T13: -0.0041 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.4824 L22: 1.6415
REMARK 3 L33: 1.4926 L12: 0.1018
REMARK 3 L13: 0.1016 L23: 0.6198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0237 S12: -0.0142 S13: 0.0228
REMARK 3 S21: 0.0698 S22: -0.0233 S23: 0.0166
REMARK 3 S31: 0.2063 S32: -0.0478 S33: -0.0004
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 402
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4758 15.7012 -20.8515
REMARK 3 T TENSOR
REMARK 3 T11: 0.1206 T22: 0.0270
REMARK 3 T33: 0.0107 T12: -0.0320
REMARK 3 T13: 0.0260 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.5516 L22: 1.6955
REMARK 3 L33: 3.0547 L12: 0.4368
REMARK 3 L13: -0.4355 L23: -1.6724
REMARK 3 S TENSOR
REMARK 3 S11: 0.1333 S12: -0.0081 S13: 0.0040
REMARK 3 S21: 0.2363 S22: -0.0703 S23: -0.0082
REMARK 3 S31: -0.5103 S32: 0.0762 S33: -0.0630
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 401
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3116 29.5819 26.0642
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.0456
REMARK 3 T33: 0.0257 T12: -0.0201
REMARK 3 T13: 0.0390 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 0.3736 L22: 2.5956
REMARK 3 L33: 1.6909 L12: -0.0620
REMARK 3 L13: -0.0795 L23: 0.7499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: 0.0291 S13: -0.0360
REMARK 3 S21: -0.3297 S22: -0.0202 S23: -0.0207
REMARK 3 S31: -0.2896 S32: -0.1550 S33: -0.0059
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 4X91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205209.
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) : 0.97933
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 : 95158
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
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 (%): 61.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
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 ARG A 3
REMARK 465 GLY B 0
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
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 OE1 GLU D 150 O HOH D 599 1.98
REMARK 500 ND2 ASN D 256 O5 NAG D 403 2.10
REMARK 500 ND2 ASN D 256 C2 NAG D 403 2.13
REMARK 500 SG CYS B 297 SG CYS B 338 2.15
REMARK 500 ND2 ASN A 365 O5 NAG A 404 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 O3 NAG B 403 O3 NAG C 404 1545 1.37
REMARK 500 O7 NAG C 404 O3 NAG D 403 1554 2.08
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 ARG A 188 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 205 NE - CZ - NH2 ANGL. DEV. = -3.3 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 -58.67 71.48
REMARK 500 TYR A 104 -79.87 -120.49
REMARK 500 GLU A 121 -91.77 -111.58
REMARK 500 GLU A 121 -91.75 -111.62
REMARK 500 SER A 165 -128.80 52.15
REMARK 500 ILE A 215 56.17 -163.11
REMARK 500 THR A 329 -58.65 -129.58
REMARK 500 VAL B 52 -58.21 71.47
REMARK 500 TYR B 104 -78.39 -120.22
REMARK 500 GLU B 121 -92.34 -113.10
REMARK 500 SER B 165 -126.94 52.11
REMARK 500 THR B 329 -57.95 -129.38
REMARK 500 VAL C 52 -58.70 72.02
REMARK 500 TYR C 104 -79.34 -120.25
REMARK 500 GLU C 121 -91.69 -111.59
REMARK 500 GLU C 121 -91.81 -112.33
REMARK 500 SER C 165 -127.53 53.64
REMARK 500 ILE C 215 55.63 -162.56
REMARK 500 THR C 329 -58.07 -130.97
REMARK 500 LEU C 354 79.95 -118.37
REMARK 500 VAL D 52 -59.07 72.20
REMARK 500 TYR D 104 -79.35 -120.53
REMARK 500 GLU D 121 -91.46 -112.57
REMARK 500 SER D 165 -125.75 54.24
REMARK 500 THR D 329 -58.27 -131.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IEF 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 PO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
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: AE6
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: AE7
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: AE8
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: AE9
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: AF1
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: AF2
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: AF3
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: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 402 bound
REMARK 800 to ASN C 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 403 bound
REMARK 800 to ASN C 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 404 bound
REMARK 800 to ASN C 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 405 bound
REMARK 800 to ASN C 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
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: AF9
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: AG1
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: AG2
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: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IEF B 405 and SER B
REMARK 800 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IEF B 405 and SER B
REMARK 800 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IEF C 406 and SER C
REMARK 800 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IEF 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: 4X92 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: 4X97 RELATED DB: PDB
DBREF 4X91 A 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X91 B 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X91 C 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X91 D 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
SEQADV 4X91 GLY A 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X91 GLY B 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X91 GLY C 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X91 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 IEF A 405 38
HET EPE A 406 15
HET PO4 A 407 5
HET PO4 A 408 5
HET PO4 A 409 5
HET PO4 A 410 5
HET MPD A 411 8
HET MPD A 412 8
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 14
HET NAG B 404 14
HET IEF B 405 38
HET EPE B 406 15
HET PO4 B 407 5
HET PO4 B 408 5
HET MPD B 409 8
HET MPD C 401 8
HET NAG C 402 14
HET NAG C 403 14
HET NAG C 404 14
HET NAG C 405 14
HET IEF C 406 19
HET EPE C 407 15
HET PO4 C 408 5
HET PO4 C 409 5
HET MPD C 410 8
HET MPD C 411 8
HET NAG D 401 14
HET NAG D 402 14
HET NAG D 403 14
HET NAG D 404 14
HET IEF D 405 19
HET EPE D 406 15
HET PO4 D 407 5
HET PO4 D 408 5
HET MPD D 409 8
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM IEF PROPAN-2-YL (R)-TRIDEC-12-EN-1-YLPHOSPHONOFLUORIDATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN EPE HEPES
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 9 IEF 4(C16 H32 F O2 P)
FORMUL 10 EPE 4(C8 H18 N2 O4 S)
FORMUL 11 PO4 10(O4 P 3-)
FORMUL 15 MPD 7(C6 H14 O2)
FORMUL 46 HOH *513(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 SER A 334 5 4
HELIX 16 AB7 ALA A 335 SER A 343 1 9
HELIX 17 AB8 ILE A 360 ALA A 364 5 5
HELIX 18 AB9 ASN A 365 GLY A 378 1 14
HELIX 19 AC1 ASN B 45 LEU B 50 5 6
HELIX 20 AC2 VAL B 52 ARG B 62 1 11
HELIX 21 AC3 THR B 88 PHE B 93 1 6
HELIX 22 AC4 SER B 99 SER B 103 5 5
HELIX 23 AC5 PHE B 105 TRP B 115 1 11
HELIX 24 AC6 ALA B 133 GLU B 136 5 4
HELIX 25 AC7 ASN B 137 GLY B 156 1 20
HELIX 26 AC8 MET B 166 ARG B 177 1 12
HELIX 27 AC9 PRO B 179 TYR B 186 1 8
HELIX 28 AD1 ALA B 201 GLY B 210 1 10
HELIX 29 AD2 GLY B 219 ALA B 230 1 12
HELIX 30 AD3 ALA B 230 LEU B 236 1 7
HELIX 31 AD4 ASP B 261 GLY B 270 1 10
HELIX 32 AD5 GLU B 272 GLU B 282 1 11
HELIX 33 AD6 ASN B 331 SER B 334 5 4
HELIX 34 AD7 ALA B 335 SER B 343 1 9
HELIX 35 AD8 ILE B 360 ALA B 364 5 5
HELIX 36 AD9 ASN B 365 GLY B 378 1 14
HELIX 37 AE1 ASN C 45 LEU C 50 5 6
HELIX 38 AE2 VAL C 52 ARG C 62 1 11
HELIX 39 AE3 THR C 88 PHE C 93 1 6
HELIX 40 AE4 SER C 99 SER C 103 5 5
HELIX 41 AE5 PHE C 105 TRP C 115 1 11
HELIX 42 AE6 ALA C 133 GLU C 136 5 4
HELIX 43 AE7 ASN C 137 GLY C 156 1 20
HELIX 44 AE8 MET C 166 ARG C 177 1 12
HELIX 45 AE9 PRO C 179 TYR C 186 1 8
HELIX 46 AF1 ALA C 201 GLY C 210 1 10
HELIX 47 AF2 GLY C 219 ALA C 230 1 12
HELIX 48 AF3 ALA C 230 LEU C 236 1 7
HELIX 49 AF4 ASP C 261 ILE C 269 1 9
HELIX 50 AF5 PHE C 271 GLU C 282 1 12
HELIX 51 AF6 LEU C 332 SER C 343 1 12
HELIX 52 AF7 ILE C 360 ALA C 364 5 5
HELIX 53 AF8 ASN C 365 GLY C 378 1 14
HELIX 54 AF9 ASN D 45 LEU D 50 5 6
HELIX 55 AG1 VAL D 52 ARG D 62 1 11
HELIX 56 AG2 THR D 88 PHE D 93 1 6
HELIX 57 AG3 SER D 99 SER D 103 5 5
HELIX 58 AG4 PHE D 105 TRP D 115 1 11
HELIX 59 AG5 ALA D 133 GLU D 136 5 4
HELIX 60 AG6 ASN D 137 GLY D 156 1 20
HELIX 61 AG7 MET D 166 ARG D 177 1 12
HELIX 62 AG8 PRO D 179 TYR D 186 1 8
HELIX 63 AG9 ALA D 201 GLY D 210 1 10
HELIX 64 AH1 GLY D 219 ALA D 230 1 12
HELIX 65 AH2 ALA D 230 LEU D 236 1 7
HELIX 66 AH3 ASP D 261 ILE D 269 1 9
HELIX 67 AH4 PHE D 271 GLU D 282 1 12
HELIX 68 AH5 ASN D 331 SER D 334 5 4
HELIX 69 AH6 ALA D 335 SER D 343 1 9
HELIX 70 AH7 ILE D 360 ALA D 364 5 5
HELIX 71 AH8 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 VAL A 7 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 LYS A 320 N TYR A 310
SHEET 1 AA5 6 VAL B 123 GLY B 125 0
SHEET 2 AA5 6 VAL B 7 VAL B 10 1 N VAL B 7 O ARG B 124
SHEET 3 AA5 6 VAL B 159 HIS B 164 1 O VAL B 162 N VAL B 10
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 LYS B 320 N TYR B 310
SHEET 1 AA9 6 VAL C 123 GLY C 125 0
SHEET 2 AA9 6 VAL C 7 VAL C 10 1 N VAL C 7 O ARG C 124
SHEET 3 AA9 6 VAL C 159 HIS C 164 1 O VAL C 162 N VAL C 10
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 LYS C 320 N TYR C 310
SHEET 1 AB4 6 VAL D 123 GLY D 125 0
SHEET 2 AB4 6 VAL D 7 VAL D 10 1 N VAL D 7 O ARG D 124
SHEET 3 AB4 6 VAL D 159 HIS D 164 1 O VAL D 162 N VAL D 10
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 LYS D 320 N TYR D 310
SSBOND 1 CYS A 32 CYS A 56 1555 1555 2.02
SSBOND 2 CYS B 32 CYS B 56 1555 1555 2.04
SSBOND 3 CYS C 32 CYS C 56 1555 1555 2.03
SSBOND 4 CYS D 32 CYS D 56 1555 1555 2.04
LINK ND2 ASN A 66 C1 NAG A 401 1555 1555 1.44
LINK OG SER A 165 P1 AIEF A 405 1555 1555 1.58
LINK OG SER A 165 P1 BIEF A 405 1555 1555 1.62
LINK ND2 ASN A 240 C1 NAG A 402 1555 1555 1.43
LINK ND2AASN A 256 C1 NAG A 403 1555 1555 1.47
LINK ND2 ASN A 365 C1 NAG A 404 1555 1555 1.40
LINK ND2 ASN B 66 C1 NAG B 401 1555 1555 1.44
LINK OG SER B 165 P1 AIEF B 405 1555 1555 1.60
LINK OG SER B 165 P1 BIEF B 405 1555 1555 1.63
LINK ND2 ASN B 240 C1 NAG B 402 1555 1555 1.43
LINK ND2 ASN B 256 C1 NAG B 403 1555 1555 1.42
LINK ND2 ASN B 365 C1 NAG B 404 1555 1555 1.44
LINK ND2 ASN C 66 C1 NAG C 402 1555 1555 1.43
LINK OG SER C 165 P1 IEF C 406 1555 1555 1.57
LINK ND2 ASN C 240 C1 NAG C 403 1555 1555 1.43
LINK ND2 ASN C 256 C1 NAG C 404 1555 1555 1.42
LINK ND2 ASN C 365 C1 NAG C 405 1555 1555 1.42
LINK ND2 ASN D 66 C1 NAG D 401 1555 1555 1.46
LINK OG SER D 165 P1 IEF D 405 1555 1555 1.59
LINK ND2 ASN D 240 C1 NAG D 402 1555 1555 1.45
LINK ND2 ASN D 256 C1 NAG D 403 1555 1555 1.38
LINK ND2 ASN D 365 C1 NAG D 404 1555 1555 1.42
CISPEP 1 TRP A 43 LEU A 44 0 2.01
CISPEP 2 PHE A 314 PRO A 315 0 7.12
CISPEP 3 TRP B 43 LEU B 44 0 -0.56
CISPEP 4 PHE B 314 PRO B 315 0 6.99
CISPEP 5 TRP C 43 LEU C 44 0 0.09
CISPEP 6 PHE C 314 PRO C 315 0 8.59
CISPEP 7 TRP D 43 LEU D 44 0 -0.54
CISPEP 8 PHE D 314 PRO D 315 0 7.18
SITE 1 AC1 15 GLY A 12 ASP A 13 LEU A 94 TYR A 104
SITE 2 AC1 15 TRP A 130 SER A 165 MET A 166 ARG A 214
SITE 3 AC1 15 GLN A 226 ALA A 230 THR A 233 LEU A 236
SITE 4 AC1 15 THR A 329 HIS A 359 ILE A 360
SITE 1 AC2 8 CYS A 32 SER A 33 PHE A 40 ASN A 60
SITE 2 AC2 8 HOH A 572 HOH A 581 HOH A 588 HOH A 636
SITE 1 AC3 6 TYR A 30 GLN A 180 GLY A 292 GLN A 345
SITE 2 AC3 6 GLU A 346 HIS A 347
SITE 1 AC4 4 GLN A 294 HIS A 347 GLN A 348 HOH A 503
SITE 1 AC5 3 ARG A 263 TRP A 275 GLN A 279
SITE 1 AC6 7 LYS A 87 THR A 88 PHE A 89 ARG A 119
SITE 2 AC6 7 GLY A 120 HOH A 639 HOH B 633
SITE 1 AC7 4 LEU A 14 ILE A 223 GLN A 226 GLN A 227
SITE 1 AC8 5 GLN A 73 ARG D 145 PRO D 179 ALA D 181
SITE 2 AC8 5 TRP D 182
SITE 1 AC9 9 CYS B 32 SER B 33 PHE B 40 CYS B 56
SITE 2 AC9 9 ASN B 60 HOH B 575 HOH B 607 HOH B 613
SITE 3 AC9 9 HOH B 627
SITE 1 AD1 5 GLN B 180 GLY B 292 GLN B 345 GLU B 346
SITE 2 AD1 5 HIS B 347
SITE 1 AD2 3 GLN B 294 HIS B 347 GLN B 348
SITE 1 AD3 5 TRP B 57 ASP B 211 GLN B 226 GLN B 227
SITE 2 AD3 5 IEF B 405
SITE 1 AD4 2 GLN C 73 HOH C 570
SITE 1 AD5 9 CYS C 32 SER C 33 PHE C 40 LEU C 48
SITE 2 AD5 9 CYS C 56 ASN C 60 HOH C 561 HOH C 576
SITE 3 AD5 9 HOH C 611
SITE 1 AD6 5 GLN C 180 GLY C 292 GLN C 345 GLU C 346
SITE 2 AD6 5 HIS C 347
SITE 1 AD7 3 ARG C 263 TRP C 275 GLN C 279
SITE 1 AD8 6 LEU C 14 TRP C 43 TRP C 57 ILE C 223
SITE 2 AD8 6 GLN C 226 GLN C 227
SITE 1 AD9 5 LEU C 94 VAL C 101 ILE C 360 IEF C 406
SITE 2 AD9 5 HOH C 590
SITE 1 AE1 7 CYS D 32 SER D 33 PHE D 40 LEU D 48
SITE 2 AE1 7 CYS D 56 ASN D 60 HOH D 582
SITE 1 AE2 5 GLN D 180 GLY D 292 GLN D 345 GLU D 346
SITE 2 AE2 5 HIS D 347
SITE 1 AE3 3 GLN D 294 HIS D 347 GLN D 348
SITE 1 AE4 5 LEU D 14 ASP D 211 ILE D 215 GLN D 226
SITE 2 AE4 5 GLN D 227
SITE 1 AE5 2 ASN A 66 GLN A 73
SITE 1 AE6 8 ASN A 240 GLU A 282 HOH A 509 HOH A 568
SITE 2 AE6 8 HOH A 569 ARG B 263 GLN B 267 HOH B 512
SITE 1 AE7 10 VAL A 248 GLN A 251 THR A 254 ILE A 255
SITE 2 AE7 10 ASN A 256 NAG B 403 NAG C 404 GLN D 251
SITE 3 AE7 10 TYR D 310 NAG D 403
SITE 1 AE8 6 LEU A 354 PRO A 355 ASN A 365 THR A 367
SITE 2 AE8 6 HOH A 540 HOH A 595
SITE 1 AE9 3 ASN B 66 SER B 69 GLN B 73
SITE 1 AF1 7 ARG A 263 GLN A 267 ASN B 240 GLU B 282
SITE 2 AF1 7 HOH B 514 HOH B 554 HOH B 640
SITE 1 AF2 6 ASN A 256 NAG A 403 THR B 254 ASN B 256
SITE 2 AF2 6 GLN C 251 NAG C 404
SITE 1 AF3 4 PRO B 355 ASN B 365 THR B 367 HOH B 642
SITE 1 AF4 3 ASN C 66 SER C 69 GLN C 73
SITE 1 AF5 7 ASN C 240 GLU C 282 HOH C 508 HOH C 547
SITE 2 AF5 7 HOH C 591 ARG D 263 GLN D 267
SITE 1 AF6 8 NAG A 403 GLN B 251 NAG B 403 PRO C 253
SITE 2 AF6 8 THR C 254 ILE C 255 ASN C 256 NAG D 403
SITE 1 AF7 6 LEU C 354 PRO C 355 ASN C 365 THR C 367
SITE 2 AF7 6 HOH C 575 HOH C 621
SITE 1 AF8 3 ASN D 66 SER D 69 GLN D 73
SITE 1 AF9 4 ARG C 263 ASN D 240 GLU D 282 HOH D 541
SITE 1 AG1 9 GLN A 251 TYR A 310 NAG A 403 ASN C 256
SITE 2 AG1 9 NAG C 404 VAL D 248 THR D 254 ASN D 256
SITE 3 AG1 9 HOH D 508
SITE 1 AG2 4 LEU D 354 PRO D 355 ASN D 365 HOH D 588
SITE 1 AG3 21 GLY B 12 ASP B 13 LEU B 14 LEU B 46
SITE 2 AG3 21 TYR B 104 TRP B 130 HIS B 164 MET B 166
SITE 3 AG3 21 GLY B 167 ASN B 168 LEU B 193 GLY B 194
SITE 4 AG3 21 PRO B 196 VAL B 200 GLN B 226 GLN B 227
SITE 5 AG3 21 ALA B 230 LEU B 236 HIS B 359 ILE B 360
SITE 6 AG3 21 MPD B 409
SITE 1 AG4 21 GLY B 12 ASP B 13 LEU B 14 LEU B 46
SITE 2 AG4 21 TYR B 104 TRP B 130 HIS B 164 MET B 166
SITE 3 AG4 21 GLY B 167 ASN B 168 LEU B 193 GLY B 194
SITE 4 AG4 21 PRO B 196 VAL B 200 GLN B 226 GLN B 227
SITE 5 AG4 21 ALA B 230 LEU B 236 HIS B 359 ILE B 360
SITE 6 AG4 21 MPD B 409
SITE 1 AG5 16 GLY C 12 ASP C 13 TRP C 130 HIS C 164
SITE 2 AG5 16 MET C 166 GLY C 167 ASN C 168 LEU C 193
SITE 3 AG5 16 GLY C 194 PRO C 196 VAL C 200 GLN C 226
SITE 4 AG5 16 ALA C 230 THR C 233 HIS C 359 MPD C 411
SITE 1 AG6 15 GLY D 12 ASP D 13 LEU D 94 VAL D 101
SITE 2 AG6 15 HIS D 164 MET D 166 GLY D 167 ASN D 168
SITE 3 AG6 15 LEU D 193 GLY D 194 PRO D 196 VAL D 200
SITE 4 AG6 15 THR D 329 HIS D 359 ILE D 360
CRYST1 62.830 90.172 99.345 79.08 88.88 89.11 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 0.015916 -0.000247 -0.000269 0.00000
SCALE2 0.000000 0.011091 -0.002137 0.00000
SCALE3 0.000000 0.000000 0.010253 0.00000
TER 3075 PRO A 379
TER 6114 PRO B 379
TER 9177 PRO C 379
TER 12213 PRO D 379
MASTER 640 0 41 71 60 0 88 613055 4 532 120
END |