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HEADER TRANSFERASE 11-DEC-14 4X90
TITLE CRYSTAL STRUCTURE OF LYSOSOMAL PHOSPHOLIPASE A2
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
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, ESTERASE, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 11-MAR-15 4X90 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. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 174210
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9229
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11158
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 586
REMARK 3 BIN FREE R VALUE : 0.2200
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 : 420
REMARK 3 SOLVENT ATOMS : 1065
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.71000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : -1.30000
REMARK 3 B12 (A**2) : -0.24000
REMARK 3 B13 (A**2) : 0.13000
REMARK 3 B23 (A**2) : 0.20000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.093
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.506
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13498 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12557 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18501 ; 1.441 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 28856 ; 1.168 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1624 ; 5.816 ; 5.006
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 609 ;33.364 ;23.563
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2088 ;11.529 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;13.245 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2015 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15191 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3170 ; 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): 6274 ; 1.271 ; 1.770
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6273 ; 1.271 ; 1.769
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7893 ; 2.040 ; 2.644
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 23512 0.090 0.050
REMARK 3 2 A 4 379 C 4 379 23567 0.090 0.050
REMARK 3 3 A 4 379 D 4 379 24248 0.060 0.050
REMARK 3 4 B 4 379 C 4 379 24220 0.060 0.050
REMARK 3 5 B 4 379 D 4 379 23549 0.090 0.050
REMARK 3 6 C 4 379 D 4 379 23467 0.090 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 404
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0334 -14.4982 21.4187
REMARK 3 T TENSOR
REMARK 3 T11: 0.0110 T22: 0.0144
REMARK 3 T33: 0.0315 T12: -0.0047
REMARK 3 T13: 0.0036 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.1993 L22: 0.3876
REMARK 3 L33: 1.1202 L12: -0.1050
REMARK 3 L13: 0.0419 L23: -0.3366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: -0.0017 S13: -0.0216
REMARK 3 S21: -0.0116 S22: 0.0104 S23: 0.0066
REMARK 3 S31: 0.0946 S32: -0.0071 S33: -0.0146
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 403
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3093 29.5096 25.8511
REMARK 3 T TENSOR
REMARK 3 T11: 0.0156 T22: 0.0162
REMARK 3 T33: 0.0260 T12: 0.0084
REMARK 3 T13: 0.0022 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.1432 L22: 1.1837
REMARK 3 L33: 1.1073 L12: -0.0543
REMARK 3 L13: -0.0645 L23: 0.6691
REMARK 3 S TENSOR
REMARK 3 S11: 0.0203 S12: 0.0322 S13: -0.0170
REMARK 3 S21: -0.0625 S22: -0.0244 S23: 0.0079
REMARK 3 S31: -0.1103 S32: -0.0835 S33: 0.0040
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 403
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3867 -29.2064 -25.7174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0085 T22: 0.0362
REMARK 3 T33: 0.0500 T12: 0.0092
REMARK 3 T13: -0.0004 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.2288 L22: 0.9620
REMARK 3 L33: 0.8193 L12: 0.1253
REMARK 3 L13: 0.0800 L23: 0.4987
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.0228 S13: 0.0079
REMARK 3 S21: 0.0304 S22: -0.0180 S23: -0.0066
REMARK 3 S31: 0.0515 S32: -0.0450 S33: 0.0065
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 404
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8805 14.8439 -21.3974
REMARK 3 T TENSOR
REMARK 3 T11: 0.0087 T22: 0.0227
REMARK 3 T33: 0.0456 T12: -0.0007
REMARK 3 T13: -0.0015 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.1624 L22: 0.7004
REMARK 3 L33: 1.0835 L12: 0.0941
REMARK 3 L13: -0.0541 L23: -0.3937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.0032 S13: 0.0157
REMARK 3 S21: 0.0214 S22: 0.0108 S23: -0.0132
REMARK 3 S31: -0.0919 S32: -0.0094 S33: -0.0190
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 4X90 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_1000205001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-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 : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97937
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 183439
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.63100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
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 CB ALA C 335 O HOH C 772 0.87
REMARK 500 CB ALA B 335 O HOH B 734 0.92
REMARK 500 CB ALA D 335 O HOH D 743 1.08
REMARK 500 C1 NAG A 403 O HOH A 501 1.14
REMARK 500 CB ALA A 335 O HOH A 552 1.40
REMARK 500 C6 NAG D 404 O HOH D 502 1.73
REMARK 500 C6 NAG A 403 O HOH A 503 1.81
REMARK 500 CB ALA D 335 O HOH D 717 1.83
REMARK 500 N2 NAG B 403 O HOH B 501 1.96
REMARK 500 OE2 GLU A 146 O HOH A 780 1.96
REMARK 500 CB ALA B 335 O HOH B 735 1.96
REMARK 500 O5 NAG A 403 O HOH A 501 1.98
REMARK 500 CA ALA D 335 O HOH D 717 1.98
REMARK 500 CA ALA B 335 O HOH B 735 2.05
REMARK 500 CB ALA A 335 O HOH A 703 2.05
REMARK 500 C2 NAG A 403 O HOH A 501 2.08
REMARK 500 O HOH B 722 O HOH D 757 2.10
REMARK 500 CB SER C 334 O HOH C 774 2.11
REMARK 500 CD GLU A 146 O HOH A 780 2.12
REMARK 500 CB ALA C 335 O HOH C 773 2.13
REMARK 500 CB SER B 334 O HOH B 697 2.14
REMARK 500 CA ALA C 335 O HOH C 773 2.15
REMARK 500 O HOH D 519 O HOH D 523 2.17
REMARK 500 O HOH A 727 O HOH A 761 2.17
REMARK 500 SG CYS C 297 O HOH C 737 2.18
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 528 O HOH C 534 1556 2.02
REMARK 500 O HOH C 533 O HOH C 537 1655 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 205 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ASP A 23 70.55 -151.46
REMARK 500 VAL A 52 -57.34 73.22
REMARK 500 TYR A 104 -80.84 -124.06
REMARK 500 GLU A 121 -90.77 -113.64
REMARK 500 GLU A 121 -90.69 -113.82
REMARK 500 SER A 165 -130.00 54.89
REMARK 500 ILE A 215 58.10 -169.34
REMARK 500 THR A 329 -54.08 -129.62
REMARK 500 ASP B 23 70.44 -150.85
REMARK 500 VAL B 52 -58.11 73.33
REMARK 500 TYR B 104 -79.87 -122.45
REMARK 500 GLU B 121 -91.46 -113.36
REMARK 500 SER B 165 -127.57 54.25
REMARK 500 THR B 329 -55.06 -127.99
REMARK 500 ASP C 23 69.95 -151.01
REMARK 500 VAL C 52 -58.25 74.28
REMARK 500 TYR C 104 -78.70 -122.44
REMARK 500 GLU C 121 -90.98 -113.47
REMARK 500 SER C 165 -128.02 54.50
REMARK 500 THR C 329 -55.16 -128.40
REMARK 500 ASP D 23 70.88 -151.01
REMARK 500 VAL D 52 -57.95 72.71
REMARK 500 TYR D 104 -81.55 -123.67
REMARK 500 GLU D 121 -91.01 -112.41
REMARK 500 GLU D 121 -91.78 -119.63
REMARK 500 SER D 165 -129.83 55.20
REMARK 500 ILE D 215 59.15 -168.68
REMARK 500 THR D 329 -53.59 -128.45
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 EPE A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL 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 MPD A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD 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 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
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: AF1
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: AF2
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: AF3
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: AF4
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: AF5
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: AF6
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: AF7
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: AF8
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: AF9
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: AG1
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: AG2
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: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 402 bound
REMARK 800 to ASN D 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 403 bound
REMARK 800 to ASN D 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 404 bound
REMARK 800 to ASN D 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 405 bound
REMARK 800 to ASN D 365
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X91 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 4X90 A 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X90 B 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X90 C 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X90 D 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
SEQADV 4X90 GLY A 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X90 GLY B 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X90 GLY C 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X90 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 28
HET NAG A 404 14
HET EPE A 405 15
HET CL A 406 1
HET PO4 A 407 5
HET MPD A 408 8
HET MPD A 409 8
HET MPD A 410 8
HET MPD A 411 8
HET MPD A 412 8
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 28
HET NAG B 404 14
HET EPE B 405 15
HET CL B 406 1
HET PO4 B 407 5
HET MPD B 408 8
HET MPD B 409 8
HET NAG C 401 14
HET NAG C 402 14
HET NAG C 403 28
HET NAG C 404 14
HET EPE C 405 15
HET CL C 406 1
HET PO4 C 407 5
HET MPD C 408 8
HET MPD C 409 8
HET MPD D 401 8
HET NAG D 402 14
HET NAG D 403 14
HET NAG D 404 28
HET NAG D 405 14
HET EPE D 406 15
HET CL D 407 1
HET PO4 D 408 5
HET MPD D 409 8
HET MPD D 410 8
HET MPD D 411 8
HET MPD D 412 8
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM CL CHLORIDE ION
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 EPE 4(C8 H18 N2 O4 S)
FORMUL 10 CL 4(CL 1-)
FORMUL 11 PO4 4(O4 P 3-)
FORMUL 12 MPD 14(C6 H14 O2)
FORMUL 47 HOH *1065(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 LYS A 333 5 3
HELIX 16 AB7 SER A 334 GLN A 342 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 PHE B 271 GLU B 282 1 12
HELIX 33 AD6 ASN B 331 LYS B 333 5 3
HELIX 34 AD7 SER B 334 GLN B 342 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 GLY C 270 1 10
HELIX 50 AF5 GLU C 272 GLU C 282 1 11
HELIX 51 AF6 ASN C 331 LYS C 333 5 3
HELIX 52 AF7 SER C 334 GLN C 342 1 9
HELIX 53 AF8 ILE C 360 ALA C 364 5 5
HELIX 54 AF9 ASN C 365 GLY C 378 1 14
HELIX 55 AG1 ASN D 45 LEU D 50 5 6
HELIX 56 AG2 VAL D 52 ARG D 62 1 11
HELIX 57 AG3 THR D 88 PHE D 93 1 6
HELIX 58 AG4 SER D 99 SER D 103 5 5
HELIX 59 AG5 PHE D 105 TRP D 115 1 11
HELIX 60 AG6 ALA D 133 GLU D 136 5 4
HELIX 61 AG7 ASN D 137 GLY D 156 1 20
HELIX 62 AG8 MET D 166 ARG D 177 1 12
HELIX 63 AG9 PRO D 179 TYR D 186 1 8
HELIX 64 AH1 ALA D 201 GLY D 210 1 10
HELIX 65 AH2 GLY D 219 ALA D 230 1 12
HELIX 66 AH3 ALA D 230 LEU D 236 1 7
HELIX 67 AH4 ASP D 261 ILE D 269 1 9
HELIX 68 AH5 PHE D 271 GLU D 282 1 12
HELIX 69 AH6 ASN D 331 LYS D 333 5 3
HELIX 70 AH7 SER D 334 GLN D 342 1 9
HELIX 71 AH8 ILE D 360 ALA D 364 5 5
HELIX 72 AH9 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 THR A 258 0
SHEET 2 AA4 4 VAL A 248 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 GLY B 324 N THR B 305
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 CYS C 322 N ASP C 307
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 THR D 258 0
SHEET 2 AB7 4 VAL D 248 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 2.04
SSBOND 2 CYS B 32 CYS B 56 1555 1555 2.05
SSBOND 3 CYS C 32 CYS C 56 1555 1555 2.06
SSBOND 4 CYS D 32 CYS D 56 1555 1555 2.05
LINK ND2 ASN A 66 C1 NAG A 401 1555 1555 1.45
LINK ND2 ASN A 240 C1 NAG A 402 1555 1555 1.43
LINK ND2AASN A 256 C1 ANAG A 403 1555 1555 1.45
LINK ND2BASN A 256 C1 BNAG A 403 1555 1555 1.45
LINK ND2 ASN A 365 C1 NAG A 404 1555 1555 1.43
LINK ND2 ASN B 66 C1 NAG B 401 1555 1555 1.45
LINK ND2 ASN B 240 C1 NAG B 402 1555 1555 1.44
LINK ND2AASN B 256 C1 ANAG B 403 1555 1555 1.44
LINK ND2BASN B 256 C1 BNAG B 403 1555 1555 1.45
LINK ND2 ASN B 365 C1 NAG B 404 1555 1555 1.43
LINK ND2 ASN C 66 C1 NAG C 401 1555 1555 1.46
LINK ND2 ASN C 240 C1 NAG C 402 1555 1555 1.44
LINK ND2AASN C 256 C1 ANAG C 403 1555 1555 1.45
LINK ND2BASN C 256 C1 BNAG C 403 1555 1555 1.44
LINK ND2 ASN C 365 C1 NAG C 404 1555 1555 1.42
LINK ND2 ASN D 66 C1 NAG D 402 1555 1555 1.44
LINK ND2 ASN D 240 C1 NAG D 403 1555 1555 1.43
LINK ND2AASN D 256 C1 ANAG D 404 1555 1555 1.45
LINK ND2BASN D 256 C1 BNAG D 404 1555 1555 1.45
LINK ND2 ASN D 365 C1 NAG D 405 1555 1555 1.43
CISPEP 1 TRP A 43 LEU A 44 0 -0.96
CISPEP 2 PHE A 314 PRO A 315 0 0.82
CISPEP 3 TRP B 43 LEU B 44 0 -1.78
CISPEP 4 PHE B 314 PRO B 315 0 3.23
CISPEP 5 TRP C 43 LEU C 44 0 -1.40
CISPEP 6 PHE C 314 PRO C 315 0 1.93
CISPEP 7 TRP D 43 LEU D 44 0 -0.63
CISPEP 8 PHE D 314 PRO D 315 0 2.66
SITE 1 AC1 6 CYS A 32 SER A 33 ASN A 60 HOH A 553
SITE 2 AC1 6 HOH A 619 HOH A 719
SITE 1 AC2 3 GLN A 294 HIS A 347 GLN A 348
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 6 ASP A 13 ASP A 211 GLN A 227 MPD A 409
SITE 2 AC4 6 MPD A 411 HOH A 575
SITE 1 AC5 7 ASP A 13 SER A 165 VAL A 200 THR A 203
SITE 2 AC5 7 LEU A 236 MPD A 408 HOH A 532
SITE 1 AC6 1 ARG A 214
SITE 1 AC7 6 TRP A 57 ILE A 215 GLN A 226 GLN A 227
SITE 2 AC7 6 MPD A 408 HOH A 575
SITE 1 AC8 8 GLN A 73 HOH A 618 HOH A 655 ARG B 145
SITE 2 AC8 8 PRO B 179 ALA B 181 TRP B 182 HOH B 597
SITE 1 AC9 8 CYS B 32 SER B 33 ILE B 53 CYS B 56
SITE 2 AC9 8 ASN B 60 HOH B 585 HOH B 640 HOH B 694
SITE 1 AD1 3 GLN B 294 HIS B 347 GLN B 348
SITE 1 AD2 5 GLN B 180 GLY B 292 GLN B 345 GLU B 346
SITE 2 AD2 5 HIS B 347
SITE 1 AD3 5 ASP B 13 ASP B 211 GLN B 227 MPD B 409
SITE 2 AD3 5 HOH B 586
SITE 1 AD4 7 ASP B 13 SER B 165 VAL B 200 THR B 203
SITE 2 AD4 7 LEU B 236 MPD B 408 HOH B 528
SITE 1 AD5 9 CYS C 32 SER C 33 PHE C 40 CYS C 56
SITE 2 AD5 9 ASN C 60 HOH C 581 HOH C 607 HOH C 681
SITE 3 AD5 9 HOH C 701
SITE 1 AD6 3 GLN C 294 HIS C 347 GLN C 348
SITE 1 AD7 5 GLN C 180 GLY C 292 GLN C 345 GLU C 346
SITE 2 AD7 5 HIS C 347
SITE 1 AD8 6 ASP C 13 ASP C 211 GLN C 227 MPD C 409
SITE 2 AD8 6 HOH C 726 HOH C 767
SITE 1 AD9 7 ASP C 13 SER C 165 VAL C 200 THR C 203
SITE 2 AD9 7 MPD C 408 HOH C 545 HOH C 767
SITE 1 AE1 7 ARG C 145 PRO C 179 ALA C 181 GLN D 73
SITE 2 AE1 7 HOH D 614 HOH D 716 HOH D 731
SITE 1 AE2 6 CYS D 32 SER D 33 ASN D 60 HOH D 565
SITE 2 AE2 6 HOH D 574 HOH D 607
SITE 1 AE3 3 TYR D 30 GLN D 294 GLN D 348
SITE 1 AE4 5 GLN D 180 GLY D 292 GLN D 345 GLU D 346
SITE 2 AE4 5 HIS D 347
SITE 1 AE5 6 ASP D 13 ASP D 211 ARG D 214 GLN D 227
SITE 2 AE5 6 MPD D 410 MPD D 412
SITE 1 AE6 7 ASP D 13 SER D 165 VAL D 200 LYS D 202
SITE 2 AE6 7 LEU D 236 MPD D 409 HOH D 534
SITE 1 AE7 2 ARG D 214 HOH D 641
SITE 1 AE8 7 LEU D 14 TRP D 57 ILE D 215 ILE D 223
SITE 2 AE8 7 GLN D 226 GLN D 227 MPD D 409
SITE 1 AE9 6 ASN A 66 GLN A 73 HOH A 648 HOH A 679
SITE 2 AE9 6 HOH A 731 HOH A 772
SITE 1 AF1 7 ASN A 240 GLU A 282 HOH A 515 HOH A 649
SITE 2 AF1 7 HOH A 718 ARG C 263 GLN C 267
SITE 1 AF2 20 GLN A 251 THR A 254 ILE A 255 ASN A 256
SITE 2 AF2 20 HOH A 501 HOH A 502 HOH A 503 HOH A 504
SITE 3 AF2 20 GLN B 251 ASN B 256 TYR B 310 NAG B 403
SITE 4 AF2 20 HOH B 501 THR C 254 ILE C 255 ASN C 256
SITE 5 AF2 20 NAG C 403 HOH C 501 HOH C 507 NAG D 404
SITE 1 AF3 9 LEU A 354 PRO A 355 SER A 357 ASN A 365
SITE 2 AF3 9 THR A 367 HOH A 599 HOH A 600 HOH A 690
SITE 3 AF3 9 HOH A 727
SITE 1 AF4 2 ASN B 66 GLN B 73
SITE 1 AF5 8 ASN B 240 GLU B 282 HOH B 502 HOH B 504
SITE 2 AF5 8 HOH B 518 HOH B 654 ARG D 263 GLN D 267
SITE 1 AF6 17 TYR A 310 NAG A 403 HOH A 505 VAL B 248
SITE 2 AF6 17 GLN B 251 THR B 254 ILE B 255 ASN B 256
SITE 3 AF6 17 HOH B 501 HOH B 503 HOH B 543 NAG C 403
SITE 4 AF6 17 HOH C 507 THR D 254 ASN D 256 NAG D 404
SITE 5 AF6 17 HOH D 503
SITE 1 AF7 7 LEU B 354 PRO B 355 ASN B 365 THR B 367
SITE 2 AF7 7 HOH B 551 HOH B 569 HOH B 647
SITE 1 AF8 3 ASN C 66 SER C 69 GLN C 73
SITE 1 AF9 6 ARG A 263 GLN A 267 ASN C 240 GLU C 282
SITE 2 AF9 6 HOH C 502 HOH C 503
SITE 1 AG1 12 ASN A 256 NAG A 403 HOH A 501 HOH A 504
SITE 2 AG1 12 NAG B 403 VAL C 248 GLN C 251 THR C 254
SITE 3 AG1 12 ILE C 255 ASN C 256 HOH C 501 NAG D 404
SITE 1 AG2 8 LEU C 354 PRO C 355 SER C 357 ASN C 365
SITE 2 AG2 8 HOH C 571 HOH C 593 HOH C 672 HOH C 733
SITE 1 AG3 6 ASN D 66 GLN D 73 HOH D 673 HOH D 685
SITE 2 AG3 6 HOH D 703 HOH D 747
SITE 1 AG4 7 ARG B 263 GLN B 267 ASN D 240 GLU D 282
SITE 2 AG4 7 HOH D 507 HOH D 664 HOH D 705
SITE 1 AG5 20 NAG A 403 THR B 254 ILE B 255 ASN B 256
SITE 2 AG5 20 NAG B 403 HOH B 501 GLN C 251 THR C 252
SITE 3 AG5 20 ASN C 256 TYR C 310 NAG C 403 HOH C 501
SITE 4 AG5 20 HOH C 507 GLN D 251 THR D 254 ILE D 255
SITE 5 AG5 20 ASN D 256 HOH D 501 HOH D 502 HOH D 503
SITE 1 AG6 7 LEU D 354 PRO D 355 SER D 357 ASN D 365
SITE 2 AG6 7 THR D 367 HOH D 718 HOH D 758
CRYST1 62.806 91.151 100.266 78.13 88.46 88.50 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 0.015922 -0.000416 -0.000349 0.00000
SCALE2 0.000000 0.010975 -0.002300 0.00000
SCALE3 0.000000 0.000000 0.010194 0.00000
TER 3159 PRO A 379
TER 6302 PRO B 379
TER 9436 PRO C 379
TER 12596 PRO D 379
MASTER 659 0 42 72 60 0 88 613561 4 500 120
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