HEADER MEMBRANE PROTEIN 10-FEB-11 2Y8T
TITLE CO-STRUCTURE OF AMA1 WITH A SURFACE EXPOSED REGION OF RON2 FROM
TITLE 2 TOXOPLASMA GONDII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN, PUTATIVE;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: DOMAINS I/II/III, RESIDUES 64-484;
COMPND 5 SYNONYM: AMA1, APICAL MEMBRANE ANTIGEN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RHOPTRY NECK PROTEIN 2;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: RESIDUES 235-271;
COMPND 11 SYNONYM: RON2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 5811;
SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 12 ORGANISM_TAXID: 5811
KEYWDS MEMBRANE PROTEIN, MOVING JUNCTION, INVASION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.TONKIN,M.ROQUES,M.H.LAMARQUE,M.PUGNIERE,D.DOUGUET,J.CRAWFORD,
AUTHOR 2 M.LEBRUN,M.J.BOULANGER
REVDAT 4 20-DEC-23 2Y8T 1 HETSYN
REVDAT 3 29-JUL-20 2Y8T 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 03-APR-19 2Y8T 1 SOURCE LINK
REVDAT 1 03-AUG-11 2Y8T 0
JRNL AUTH M.L.TONKIN,M.ROQUES,M.H.LAMARQUE,M.PUGNIERE,D.DOUGUET,
JRNL AUTH 2 J.CRAWFORD,M.LEBRUN,M.J.BOULANGER
JRNL TITL HOST CELL INVASION BY APICOMPLEXAN PARASITES: INSIGHTS FROM
JRNL TITL 2 THE CO-STRUCTURE OF AMA1 WITH A RON2 PEPTIDE
JRNL REF SCIENCE V. 333 463 2011
JRNL REFN ISSN 0036-8075
JRNL PMID 21778402
JRNL DOI 10.1126/SCIENCE.1204988
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64686
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3453
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4741
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 251
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 604
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.347
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6917 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9394 ; 1.943 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 853 ; 7.433 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 325 ;38.638 ;24.800
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1119 ;17.542 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;19.334 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 997 ; 0.213 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5349 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4278 ; 1.469 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6919 ; 2.549 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2639 ; 3.911 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2472 ; 6.092 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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.
REMARK 4
REMARK 4 2Y8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1290047274.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2X2Z
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 1500, 100 MM MIB PH 4.0 .
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.19000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 59
REMARK 465 SER A 60
REMARK 465 ALA A 61
REMARK 465 MET A 62
REMARK 465 GLY A 63
REMARK 465 SER A 64
REMARK 465 ALA A 65
REMARK 465 SER A 66
REMARK 465 THR A 67
REMARK 465 HIS A 340
REMARK 465 THR A 341
REMARK 465 TYR A 342
REMARK 465 PRO A 343
REMARK 465 LEU A 344
REMARK 465 THR A 345
REMARK 465 SER A 346
REMARK 465 GLN A 347
REMARK 465 ALA A 348
REMARK 465 SER A 349
REMARK 465 TRP A 350
REMARK 465 ASN A 351
REMARK 465 ASP A 352
REMARK 465 TRP A 353
REMARK 465 TRP A 354
REMARK 465 PRO A 355
REMARK 465 LEU A 356
REMARK 465 HIS A 357
REMARK 465 GLN A 358
REMARK 465 SER A 359
REMARK 465 PRO A 422
REMARK 465 SER A 423
REMARK 465 VAL A 424
REMARK 465 THR A 425
REMARK 465 GLY A 480
REMARK 465 SER A 481
REMARK 465 ASN A 482
REMARK 465 THR A 483
REMARK 465 ALA A 484
REMARK 465 ALA A 485
REMARK 465 ALA A 486
REMARK 465 LEU A 487
REMARK 465 VAL A 488
REMARK 465 PRO A 489
REMARK 465 ARG A 490
REMARK 465 GLY D 59
REMARK 465 SER D 60
REMARK 465 ALA D 61
REMARK 465 MET D 62
REMARK 465 GLY D 63
REMARK 465 SER D 64
REMARK 465 ALA D 65
REMARK 465 SER D 66
REMARK 465 THR D 67
REMARK 465 SER D 68
REMARK 465 ALA D 348
REMARK 465 SER D 349
REMARK 465 TRP D 350
REMARK 465 PRO D 422
REMARK 465 SER D 423
REMARK 465 VAL D 424
REMARK 465 THR D 425
REMARK 465 PRO D 426
REMARK 465 PRO D 427
REMARK 465 THR D 428
REMARK 465 ASP D 474
REMARK 465 GLU D 475
REMARK 465 GLN D 476
REMARK 465 ASN D 477
REMARK 465 GLU D 478
REMARK 465 CYS D 479
REMARK 465 GLY D 480
REMARK 465 SER D 481
REMARK 465 ASN D 482
REMARK 465 THR D 483
REMARK 465 ALA D 484
REMARK 465 ALA D 485
REMARK 465 ALA D 486
REMARK 465 LEU D 487
REMARK 465 VAL D 488
REMARK 465 PRO D 489
REMARK 465 ARG D 490
REMARK 465 9AT E 1333
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 O HOH A 2175 O HOH A 2272 2.04
REMARK 500 O PRO D 441 O HOH D 2223 2.10
REMARK 500 ND2 ASN D 351 O HOH D 2180 2.14
REMARK 500 OG SER A 410 OE1 GLU D 412 2.17
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 2131 O HOH A 2249 2555 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 177 CB GLU A 177 CG 0.119
REMARK 500 CYS D 435 CB CYS D 435 SG -0.180
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 LEU A 116 CB - CG - CD1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU A 126 CB - CG - CD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 205 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 MET A 236 CA - CB - CG ANGL. DEV. = -12.9 DEGREES
REMARK 500 LEU A 291 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES
REMARK 500 VAL B1314 CG1 - CB - CG2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 PRO D 71 C - N - CA ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU D 126 CB - CG - CD2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU D 235 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 VAL D 275 CG1 - CB - CG2 ANGL. DEV. = 11.8 DEGREES
REMARK 500 LEU D 344 CA - CB - CG ANGL. DEV. = 19.8 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 LEU A 99 56.52 -140.06
REMARK 500 THR A 211 -163.61 -108.45
REMARK 500 ASP A 397 103.65 -165.16
REMARK 500 TRP D 354 78.97 -113.38
REMARK 500 GLN D 358 -20.46 69.47
REMARK 500 ASP D 397 103.45 -163.96
REMARK 500 SER D 420 5.14 -65.04
REMARK 500 CYS D 435 112.09 -165.82
REMARK 500 THR D 472 -70.07 -79.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY D 69 ASN D 70 137.17
REMARK 500 GLN D 434 CYS D 435 -145.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2245 DISTANCE = 6.81 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 AMIDATED THREONINE (9AT): AMIDATED C-TERMINAL THREONINE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Y8S RELATED DB: PDB
REMARK 900 CO-STRUCTURE OF AN AMA1 MUTANT (Y230A) WITH A SURFACE EXPOSED
REMARK 900 REGION OF RON2 FROM TOXOPLASMA GONDII
REMARK 900 RELATED ID: 2Y8R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO AMA1 MUTANT (TYR230ALA) FROM TOXOPLASMA
REMARK 900 GONDII
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FOR CHAINS B AND E AUTHOR HAS PROVIDED A GENBANK REFERENCE
REMARK 999 HQ110093.
DBREF 2Y8T A 64 484 UNP B9QC59 B9QC59_TOXGO 64 484
DBREF 2Y8T B 1297 1333 UNP B9QQC1 B9QQC1_TOXGO 235 271
DBREF 2Y8T D 64 484 UNP B9QC59 B9QC59_TOXGO 64 484
DBREF 2Y8T E 1297 1333 UNP B9QQC1 B9QQC1_TOXGO 235 271
SEQADV 2Y8T GLY A 59 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T SER A 60 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA A 61 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T MET A 62 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T GLY A 63 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA A 485 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA A 486 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T LEU A 487 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T VAL A 488 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T PRO A 489 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ARG A 490 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T GLY D 59 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T SER D 60 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA D 61 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T MET D 62 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T GLY D 63 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA D 485 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ALA D 486 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T LEU D 487 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T VAL D 488 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T PRO D 489 UNP B9QC59 EXPRESSION TAG
SEQADV 2Y8T ARG D 490 UNP B9QC59 EXPRESSION TAG
SEQRES 1 A 432 GLY SER ALA MET GLY SER ALA SER THR SER GLY ASN PRO
SEQRES 2 A 432 PHE GLN ALA ASN VAL GLU MET LYS THR PHE MET GLU ARG
SEQRES 3 A 432 PHE ASN LEU THR HIS HIS HIS GLN SER GLY ILE TYR VAL
SEQRES 4 A 432 ASP LEU GLY GLN ASP LYS GLU VAL ASP GLY THR LEU TYR
SEQRES 5 A 432 ARG GLU PRO ALA GLY LEU CYS PRO ILE TRP GLY LYS HIS
SEQRES 6 A 432 ILE GLU LEU GLN GLN PRO ASP ARG PRO PRO TYR ARG ASN
SEQRES 7 A 432 ASN PHE LEU GLU ASP VAL PRO THR GLU LYS GLU TYR LYS
SEQRES 8 A 432 GLN SER GLY ASN PRO LEU PRO GLY GLY PHE ASN LEU ASN
SEQRES 9 A 432 PHE VAL THR PRO SER GLY GLN ARG ILE SER PRO PHE PRO
SEQRES 10 A 432 MET GLU LEU LEU GLU LYS ASN SER ASN ILE LYS ALA SER
SEQRES 11 A 432 THR ASP LEU GLY ARG CYS ALA GLU PHE ALA PHE LYS THR
SEQRES 12 A 432 VAL ALA MET ASP LYS ASN ASN LYS ALA THR LYS TYR ARG
SEQRES 13 A 432 TYR PRO PHE VAL TYR ASP SER LYS LYS ARG LEU CYS HIS
SEQRES 14 A 432 ILE LEU TYR VAL SER MET GLN LEU MET GLU GLY LYS LYS
SEQRES 15 A 432 TYR CYS SER VAL LYS GLY GLU PRO PRO ASP LEU THR TRP
SEQRES 16 A 432 TYR CYS PHE LYS PRO ARG LYS SER VAL THR GLU ASN HIS
SEQRES 17 A 432 HIS LEU ILE TYR GLY SER ALA TYR VAL GLY GLU ASN PRO
SEQRES 18 A 432 ASP ALA PHE ILE SER LYS CYS PRO ASN GLN ALA LEU ARG
SEQRES 19 A 432 GLY TYR ARG PHE GLY VAL TRP LYS LYS GLY ARG CYS LEU
SEQRES 20 A 432 ASP TYR THR GLU LEU THR ASP THR VAL ILE GLU ARG VAL
SEQRES 21 A 432 GLU SER LYS ALA GLN CYS TRP VAL LYS THR PHE GLU ASN
SEQRES 22 A 432 ASP GLY VAL ALA SER ASP GLN PRO HIS THR TYR PRO LEU
SEQRES 23 A 432 THR SER GLN ALA SER TRP ASN ASP TRP TRP PRO LEU HIS
SEQRES 24 A 432 GLN SER ASP GLN PRO HIS SER GLY GLY VAL GLY ARG ASN
SEQRES 25 A 432 TYR GLY PHE TYR TYR VAL ASP THR THR GLY GLU GLY LYS
SEQRES 26 A 432 CYS ALA LEU SER ASP GLN VAL PRO ASP CYS LEU VAL SER
SEQRES 27 A 432 ASP SER ALA ALA VAL SER TYR THR ALA ALA GLY SER LEU
SEQRES 28 A 432 SER GLU GLU THR PRO ASN PHE ILE ILE PRO SER ASN PRO
SEQRES 29 A 432 SER VAL THR PRO PRO THR PRO GLU THR ALA LEU GLN CYS
SEQRES 30 A 432 THR ALA ASP LYS PHE PRO ASP SER PHE GLY ALA CYS ASP
SEQRES 31 A 432 VAL GLN ALA CYS LYS ARG GLN LYS THR SER CYS VAL GLY
SEQRES 32 A 432 GLY GLN ILE GLN SER THR SER VAL ASP CYS THR ALA ASP
SEQRES 33 A 432 GLU GLN ASN GLU CYS GLY SER ASN THR ALA ALA ALA LEU
SEQRES 34 A 432 VAL PRO ARG
SEQRES 1 B 37 ASP ILE VAL GLN HIS MET GLU ASP ILE GLY GLY ALA PRO
SEQRES 2 B 37 PRO VAL SER CYS VAL THR ASN GLU ILE LEU GLY VAL THR
SEQRES 3 B 37 CYS ALA PRO GLN ALA ILE ALA LYS ALA THR 9AT
SEQRES 1 D 432 GLY SER ALA MET GLY SER ALA SER THR SER GLY ASN PRO
SEQRES 2 D 432 PHE GLN ALA ASN VAL GLU MET LYS THR PHE MET GLU ARG
SEQRES 3 D 432 PHE ASN LEU THR HIS HIS HIS GLN SER GLY ILE TYR VAL
SEQRES 4 D 432 ASP LEU GLY GLN ASP LYS GLU VAL ASP GLY THR LEU TYR
SEQRES 5 D 432 ARG GLU PRO ALA GLY LEU CYS PRO ILE TRP GLY LYS HIS
SEQRES 6 D 432 ILE GLU LEU GLN GLN PRO ASP ARG PRO PRO TYR ARG ASN
SEQRES 7 D 432 ASN PHE LEU GLU ASP VAL PRO THR GLU LYS GLU TYR LYS
SEQRES 8 D 432 GLN SER GLY ASN PRO LEU PRO GLY GLY PHE ASN LEU ASN
SEQRES 9 D 432 PHE VAL THR PRO SER GLY GLN ARG ILE SER PRO PHE PRO
SEQRES 10 D 432 MET GLU LEU LEU GLU LYS ASN SER ASN ILE LYS ALA SER
SEQRES 11 D 432 THR ASP LEU GLY ARG CYS ALA GLU PHE ALA PHE LYS THR
SEQRES 12 D 432 VAL ALA MET ASP LYS ASN ASN LYS ALA THR LYS TYR ARG
SEQRES 13 D 432 TYR PRO PHE VAL TYR ASP SER LYS LYS ARG LEU CYS HIS
SEQRES 14 D 432 ILE LEU TYR VAL SER MET GLN LEU MET GLU GLY LYS LYS
SEQRES 15 D 432 TYR CYS SER VAL LYS GLY GLU PRO PRO ASP LEU THR TRP
SEQRES 16 D 432 TYR CYS PHE LYS PRO ARG LYS SER VAL THR GLU ASN HIS
SEQRES 17 D 432 HIS LEU ILE TYR GLY SER ALA TYR VAL GLY GLU ASN PRO
SEQRES 18 D 432 ASP ALA PHE ILE SER LYS CYS PRO ASN GLN ALA LEU ARG
SEQRES 19 D 432 GLY TYR ARG PHE GLY VAL TRP LYS LYS GLY ARG CYS LEU
SEQRES 20 D 432 ASP TYR THR GLU LEU THR ASP THR VAL ILE GLU ARG VAL
SEQRES 21 D 432 GLU SER LYS ALA GLN CYS TRP VAL LYS THR PHE GLU ASN
SEQRES 22 D 432 ASP GLY VAL ALA SER ASP GLN PRO HIS THR TYR PRO LEU
SEQRES 23 D 432 THR SER GLN ALA SER TRP ASN ASP TRP TRP PRO LEU HIS
SEQRES 24 D 432 GLN SER ASP GLN PRO HIS SER GLY GLY VAL GLY ARG ASN
SEQRES 25 D 432 TYR GLY PHE TYR TYR VAL ASP THR THR GLY GLU GLY LYS
SEQRES 26 D 432 CYS ALA LEU SER ASP GLN VAL PRO ASP CYS LEU VAL SER
SEQRES 27 D 432 ASP SER ALA ALA VAL SER TYR THR ALA ALA GLY SER LEU
SEQRES 28 D 432 SER GLU GLU THR PRO ASN PHE ILE ILE PRO SER ASN PRO
SEQRES 29 D 432 SER VAL THR PRO PRO THR PRO GLU THR ALA LEU GLN CYS
SEQRES 30 D 432 THR ALA ASP LYS PHE PRO ASP SER PHE GLY ALA CYS ASP
SEQRES 31 D 432 VAL GLN ALA CYS LYS ARG GLN LYS THR SER CYS VAL GLY
SEQRES 32 D 432 GLY GLN ILE GLN SER THR SER VAL ASP CYS THR ALA ASP
SEQRES 33 D 432 GLU GLN ASN GLU CYS GLY SER ASN THR ALA ALA ALA LEU
SEQRES 34 D 432 VAL PRO ARG
SEQRES 1 E 37 ASP ILE VAL GLN HIS MET GLU ASP ILE GLY GLY ALA PRO
SEQRES 2 E 37 PRO VAL SER CYS VAL THR ASN GLU ILE LEU GLY VAL THR
SEQRES 3 E 37 CYS ALA PRO GLN ALA ILE ALA LYS ALA THR 9AT
MODRES 2Y8T ASN A 86 ASN GLYCOSYLATION SITE
MODRES 2Y8T ASN D 86 ASN GLYCOSYLATION SITE
HET 9AT B1333 8
HET NAG A1480 14
HET NAG D1474 14
HET BO3 D1475 4
HET BO3 D1476 4
HETNAM 9AT (2S,3R)-2-AMINO-3-HYDROXY-BUTANAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BO3 BORIC ACID
HETSYN 9AT AMIDATED THREONINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 9AT C4 H10 N2 O2
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 7 BO3 2(B H3 O3)
FORMUL 9 HOH *604(H2 O)
HELIX 1 1 ASN A 70 ALA A 74 5 5
HELIX 2 2 ASN A 75 ARG A 84 1 10
HELIX 3 3 THR A 144 GLY A 152 1 9
HELIX 4 4 MET A 176 LYS A 181 1 6
HELIX 5 5 THR A 189 LYS A 200 1 12
HELIX 6 6 SER A 272 GLU A 277 5 6
HELIX 7 7 ALA A 281 CYS A 286 1 6
HELIX 8 8 THR A 308 LEU A 310 5 3
HELIX 9 9 SER A 320 ASN A 331 1 12
HELIX 10 10 PRO A 414 ILE A 418 5 5
HELIX 11 11 THR A 428 LEU A 433 1 6
HELIX 12 12 THR A 436 PHE A 440 5 5
HELIX 13 13 THR A 472 CYS A 479 1 8
HELIX 14 14 ASP B 1297 ILE B 1305 1 9
HELIX 15 15 ASN D 70 ALA D 74 5 5
HELIX 16 16 ASN D 75 ARG D 84 1 10
HELIX 17 17 THR D 144 GLY D 152 1 9
HELIX 18 18 MET D 176 LYS D 181 1 6
HELIX 19 19 THR D 189 LYS D 200 1 12
HELIX 20 20 SER D 272 GLU D 277 5 6
HELIX 21 21 ASP D 280 CYS D 286 1 7
HELIX 22 22 THR D 308 LEU D 310 5 3
HELIX 23 23 SER D 320 ASN D 331 1 12
HELIX 24 24 PRO D 414 ILE D 418 5 5
HELIX 25 25 PRO D 429 LEU D 433 5 5
HELIX 26 26 THR D 436 PHE D 440 5 5
HELIX 27 27 ASP E 1297 ILE E 1305 1 9
SHEET 1 AA 2 GLN A 101 VAL A 105 0
SHEET 2 AA 2 THR A 108 GLU A 112 -1 O THR A 108 N VAL A 105
SHEET 1 AB 5 ILE A 119 TRP A 120 0
SHEET 2 AB 5 LEU A 268 GLY A 271 -1 O TYR A 270 N ILE A 119
SHEET 3 AB 5 PHE A 217 ASP A 220 -1 O PHE A 217 N GLY A 271
SHEET 4 AB 5 LEU A 225 ILE A 228 -1 O LEU A 225 N ASP A 220
SHEET 5 AB 5 PHE A 174 PRO A 175 -1 O PHE A 174 N CYS A 226
SHEET 1 AC 2 HIS A 123 LEU A 126 0
SHEET 2 AC 2 PHE A 256 ARG A 259 -1 O LYS A 257 N GLU A 125
SHEET 1 AD 3 THR A 201 ALA A 203 0
SHEET 2 AD 3 CYS B1313 ASN B1316 -1 O THR B1315 N VAL A 202
SHEET 3 AD 3 GLY B1320 CYS B1323 -1 O GLY B1320 N ASN B1316
SHEET 1 AE 2 CYS A 242 SER A 243 0
SHEET 2 AE 2 TRP A 253 TYR A 254 1 O TRP A 253 N SER A 243
SHEET 1 AF 6 ARG A 303 ASP A 306 0
SHEET 2 AF 6 LEU A 291 LYS A 300 -1 O VAL A 298 N LEU A 305
SHEET 3 AF 6 CYS A 393 THR A 404 -1 O CYS A 393 N GLY A 297
SHEET 4 AF 6 TYR A 371 VAL A 376 -1 O GLY A 372 N TYR A 403
SHEET 5 AF 6 GLY A 382 SER A 387 -1 O LYS A 383 N TYR A 375
SHEET 6 AF 6 VAL A 314 ARG A 317 -1 O VAL A 314 N LEU A 386
SHEET 1 AG 3 SER A 443 PHE A 444 0
SHEET 2 AG 3 LYS A 453 VAL A 460 -1 O THR A 457 N SER A 443
SHEET 3 AG 3 GLN A 463 ASP A 470 -1 O GLN A 463 N VAL A 460
SHEET 1 DA 2 GLN D 101 VAL D 105 0
SHEET 2 DA 2 THR D 108 GLU D 112 -1 O THR D 108 N VAL D 105
SHEET 1 DB 5 ILE D 119 TRP D 120 0
SHEET 2 DB 5 LEU D 268 GLY D 271 -1 O TYR D 270 N ILE D 119
SHEET 3 DB 5 PHE D 217 ASP D 220 -1 O PHE D 217 N GLY D 271
SHEET 4 DB 5 LEU D 225 ILE D 228 -1 O LEU D 225 N ASP D 220
SHEET 5 DB 5 PHE D 174 PRO D 175 -1 O PHE D 174 N CYS D 226
SHEET 1 DC 2 HIS D 123 LEU D 126 0
SHEET 2 DC 2 PHE D 256 ARG D 259 -1 O LYS D 257 N GLU D 125
SHEET 1 DD 3 THR D 201 ALA D 203 0
SHEET 2 DD 3 CYS E1313 ASN E1316 -1 O THR E1315 N VAL D 202
SHEET 3 DD 3 GLY E1320 CYS E1323 -1 O GLY E1320 N ASN E1316
SHEET 1 DE 2 CYS D 242 SER D 243 0
SHEET 2 DE 2 TRP D 253 TYR D 254 1 O TRP D 253 N SER D 243
SHEET 1 DF 6 ARG D 303 ASP D 306 0
SHEET 2 DF 6 LEU D 291 LYS D 300 -1 O VAL D 298 N LEU D 305
SHEET 3 DF 6 CYS D 393 THR D 404 -1 O CYS D 393 N GLY D 297
SHEET 4 DF 6 TYR D 371 VAL D 376 -1 O GLY D 372 N TYR D 403
SHEET 5 DF 6 GLY D 382 SER D 387 -1 O LYS D 383 N TYR D 375
SHEET 6 DF 6 VAL D 314 ARG D 317 -1 O VAL D 314 N LEU D 386
SHEET 1 DG 3 SER D 443 PHE D 444 0
SHEET 2 DG 3 LYS D 453 VAL D 460 -1 O THR D 457 N SER D 443
SHEET 3 DG 3 GLN D 463 ASP D 470 -1 O GLN D 463 N VAL D 460
SSBOND 1 CYS A 117 CYS A 286 1555 1555 2.09
SSBOND 2 CYS A 194 CYS A 226 1555 1555 2.14
SSBOND 3 CYS A 242 CYS A 255 1555 1555 2.11
SSBOND 4 CYS A 304 CYS A 393 1555 1555 2.07
SSBOND 5 CYS A 324 CYS A 384 1555 1555 2.20
SSBOND 6 CYS A 435 CYS A 459 1555 1555 2.11
SSBOND 7 CYS A 447 CYS A 471 1555 1555 2.07
SSBOND 8 CYS A 452 CYS A 479 1555 1555 2.11
SSBOND 9 CYS B 1313 CYS B 1323 1555 1555 2.14
SSBOND 10 CYS D 117 CYS D 286 1555 1555 2.12
SSBOND 11 CYS D 194 CYS D 226 1555 1555 2.09
SSBOND 12 CYS D 242 CYS D 255 1555 1555 2.05
SSBOND 13 CYS D 304 CYS D 393 1555 1555 2.10
SSBOND 14 CYS D 324 CYS D 384 1555 1555 2.10
SSBOND 15 CYS D 435 CYS D 459 1555 1555 2.05
SSBOND 16 CYS D 447 CYS D 471 1555 1555 2.05
SSBOND 17 CYS E 1313 CYS E 1323 1555 1555 2.14
LINK ND2 ASN A 86 C1 NAG A1480 1555 1555 1.45
LINK ND2 ASN D 86 C1 NAG D1474 1555 1555 1.43
CISPEP 1 PRO A 132 PRO A 133 0 6.25
CISPEP 2 ASN A 153 PRO A 154 0 -3.26
CISPEP 3 SER A 172 PRO A 173 0 0.53
CISPEP 4 GLU A 247 PRO A 248 0 -8.39
CISPEP 5 PRO D 132 PRO D 133 0 2.56
CISPEP 6 ASN D 153 PRO D 154 0 0.84
CISPEP 7 SER D 172 PRO D 173 0 3.23
CISPEP 8 GLU D 247 PRO D 248 0 -8.68
CISPEP 9 TRP D 354 PRO D 355 0 7.68
CRYST1 69.860 96.380 78.350 90.00 115.64 90.00 P 1 21 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 0.014314 0.000000 0.006871 0.00000
SCALE2 0.000000 0.010376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
