HEADER HYDROLASE 28-OCT-16 5M7R
TITLE STRUCTURE OF HUMAN O-GLCNAC HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN O-GLCNACASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OGA,BETA-N-ACETYLGLUCOSAMINIDASE,BETA-N-
COMPND 5 ACETYLHEXOSAMINIDASE,BETA-HEXOSAMINIDASE,MENINGIOMA-EXPRESSED ANTIGEN
COMPND 6 5,N-ACETYL-BETA-D-GLUCOSAMINIDASE,N-ACETYL-BETA-GLUCOSAMINIDASE,
COMPND 7 NUCLEAR CYTOPLASMIC O-GLCNACASE AND ACETYLTRANSFERASE,NCOAT;
COMPND 8 EC: 3.2.1.169,3.2.1.-;
COMPND 9 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: MGEA5, HEXC, KIAA0679, MEA5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GOLD
KEYWDS HUMAN GLACOSIDE HYDROLASE GLCNAC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ROTH,S.CHAN,W.A.OFFEN,G.R.HEMSWORTH,L.I.WILLEMS,D.KING,V.VARGHESE,
AUTHOR 2 R.BRITTON,D.J.VOCADLO,G.J.DAVIES
REVDAT 5 17-JAN-24 5M7R 1 REMARK
REVDAT 4 30-AUG-17 5M7R 1 REMARK
REVDAT 3 24-MAY-17 5M7R 1 JRNL
REVDAT 2 05-APR-17 5M7R 1 JRNL
REVDAT 1 29-MAR-17 5M7R 0
JRNL AUTH C.ROTH,S.CHAN,W.A.OFFEN,G.R.HEMSWORTH,L.I.WILLEMS,D.T.KING,
JRNL AUTH 2 V.VARGHESE,R.BRITTON,D.J.VOCADLO,G.J.DAVIES
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHT INTO HUMAN O-GLCNACASE.
JRNL REF NAT. CHEM. BIOL. V. 13 610 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 28346405
JRNL DOI 10.1038/NCHEMBIO.2358
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64041
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1909
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4529
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.4110
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.4190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.42000
REMARK 3 B22 (A**2) : -3.42000
REMARK 3 B33 (A**2) : 6.85000
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): 0.254
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7859 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7356 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10643 ; 1.769 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16946 ; 3.671 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 924 ; 6.620 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 376 ;34.962 ;23.670
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1346 ;18.523 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;19.138 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1131 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8741 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1872 ; 0.013 ; 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): 3732 ; 4.155 ; 4.838
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3731 ; 4.156 ; 4.838
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4644 ; 6.200 ; 7.227
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 59 A 715
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0340 1.8270 32.4600
REMARK 3 T TENSOR
REMARK 3 T11: 0.4406 T22: 0.3797
REMARK 3 T33: 0.9085 T12: -0.0364
REMARK 3 T13: 0.0337 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.8466 L22: 1.3374
REMARK 3 L33: 0.7065 L12: 0.3767
REMARK 3 L13: -0.2090 L23: -0.1979
REMARK 3 S TENSOR
REMARK 3 S11: -0.0262 S12: 0.0260 S13: 0.0867
REMARK 3 S21: 0.1526 S22: 0.0035 S23: 0.0142
REMARK 3 S31: -0.0705 S32: 0.1180 S33: 0.0228
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5M7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1200002047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 641548
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 96.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.10
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 2.18600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2CHO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.14 - 0.2 M TRIAMMONIUM CITRATE PH
REMARK 280 7.5, 16-20 % PEG 3350, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 142.74500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.11500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 214.11750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.11500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.11500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.37250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.11500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.11500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 214.11750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.11500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.11500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 71.37250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 142.74500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 GLN A 7
REMARK 465 ALA A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 GLU A 11
REMARK 465 GLU A 12
REMARK 465 ARG A 13
REMARK 465 GLU A 14
REMARK 465 SER A 15
REMARK 465 GLU A 16
REMARK 465 LEU A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 ASN A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 SER A 24
REMARK 465 ALA A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 27
REMARK 465 SER A 28
REMARK 465 LEU A 29
REMARK 465 GLU A 30
REMARK 465 PRO A 31
REMARK 465 PRO A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 34
REMARK 465 PRO A 35
REMARK 465 ALA A 36
REMARK 465 PRO A 37
REMARK 465 GLY A 38
REMARK 465 GLU A 39
REMARK 465 ASP A 40
REMARK 465 ASN A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 GLY A 44
REMARK 465 ALA A 45
REMARK 465 GLY A 46
REMARK 465 GLY A 47
REMARK 465 ALA A 48
REMARK 465 ALA A 49
REMARK 465 VAL A 50
REMARK 465 ALA A 51
REMARK 465 GLY A 52
REMARK 465 ALA A 53
REMARK 465 ALA A 54
REMARK 465 GLY A 55
REMARK 465 GLY A 56
REMARK 465 ALA A 57
REMARK 465 ARG A 58
REMARK 465 GLY A 338
REMARK 465 VAL A 339
REMARK 465 ARG A 340
REMARK 465 LYS A 341
REMARK 465 ASP A 342
REMARK 465 VAL A 343
REMARK 465 VAL A 344
REMARK 465 MET A 345
REMARK 465 THR A 346
REMARK 465 ASP A 347
REMARK 465 SER A 348
REMARK 465 GLU A 349
REMARK 465 ASP A 350
REMARK 465 SER A 351
REMARK 465 THR A 352
REMARK 465 VAL A 353
REMARK 465 SER A 354
REMARK 465 ILE A 355
REMARK 465 GLN A 356
REMARK 465 ILE A 357
REMARK 465 LYS A 358
REMARK 465 LEU A 359
REMARK 465 GLU A 360
REMARK 465 ASN A 361
REMARK 465 GLU A 362
REMARK 465 GLY A 363
REMARK 465 SER A 364
REMARK 465 ASP A 365
REMARK 465 GLU A 366
REMARK 465 ASP A 367
REMARK 465 ILE A 368
REMARK 465 GLU A 369
REMARK 465 THR A 370
REMARK 465 GLN A 396
REMARK 465 TYR A 397
REMARK 465 SER A 398
REMARK 465 SER A 399
REMARK 465 ARG A 400
REMARK 465 GLN A 401
REMARK 465 VAL A 402
REMARK 465 ALA A 403
REMARK 465 HIS A 404
REMARK 465 SER A 405
REMARK 465 GLY A 406
REMARK 465 ALA A 407
REMARK 465 LYS A 408
REMARK 465 ALA A 409
REMARK 465 SER A 410
REMARK 465 VAL A 411
REMARK 465 VAL A 412
REMARK 465 ASP A 413
REMARK 465 GLY A 414
REMARK 465 THR A 415
REMARK 465 PRO A 416
REMARK 465 LEU A 417
REMARK 465 VAL A 418
REMARK 465 ALA A 419
REMARK 465 ALA A 420
REMARK 465 PRO A 421
REMARK 465 SER A 422
REMARK 465 LEU A 423
REMARK 465 ASN A 424
REMARK 465 ALA A 425
REMARK 465 THR A 426
REMARK 465 THR A 427
REMARK 465 VAL A 428
REMARK 465 VAL A 429
REMARK 465 THR A 430
REMARK 465 THR A 431
REMARK 465 VAL A 432
REMARK 465 TYR A 433
REMARK 465 GLN A 434
REMARK 465 GLU A 435
REMARK 465 PRO A 436
REMARK 465 ILE A 437
REMARK 465 MET A 438
REMARK 465 SER A 439
REMARK 465 GLN A 440
REMARK 465 GLY A 441
REMARK 465 ALA A 442
REMARK 465 ALA A 443
REMARK 465 LEU A 444
REMARK 465 SER A 445
REMARK 465 GLY A 446
REMARK 465 GLU A 447
REMARK 465 PRO A 448
REMARK 465 THR A 449
REMARK 465 THR A 450
REMARK 465 LEU A 451
REMARK 465 THR A 452
REMARK 465 LYS A 453
REMARK 465 GLU A 454
REMARK 465 GLU A 455
REMARK 465 GLU A 456
REMARK 465 LYS A 457
REMARK 465 LYS A 458
REMARK 465 GLN A 459
REMARK 465 PRO A 460
REMARK 465 ASP A 461
REMARK 465 GLU A 462
REMARK 465 GLU A 463
REMARK 465 PRO A 464
REMARK 465 MET A 465
REMARK 465 ASP A 466
REMARK 465 MET A 467
REMARK 465 VAL A 468
REMARK 465 VAL A 469
REMARK 465 GLU A 470
REMARK 465 LYS A 471
REMARK 465 GLN A 472
REMARK 465 GLU A 473
REMARK 465 GLU A 474
REMARK 465 THR A 475
REMARK 465 ASP A 476
REMARK 465 HIS A 477
REMARK 465 LYS A 478
REMARK 465 ASN A 479
REMARK 465 ASP A 480
REMARK 465 ASN A 481
REMARK 465 GLN A 482
REMARK 465 ILE A 483
REMARK 465 LEU A 484
REMARK 465 SER A 485
REMARK 465 GLU A 486
REMARK 465 ILE A 487
REMARK 465 VAL A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 490
REMARK 465 LYS A 491
REMARK 465 MET A 492
REMARK 465 ALA A 493
REMARK 465 GLU A 494
REMARK 465 GLU A 495
REMARK 465 LEU A 496
REMARK 465 LYS A 497
REMARK 465 PRO A 498
REMARK 465 MET A 499
REMARK 465 ASP A 500
REMARK 465 THR A 501
REMARK 465 ASP A 502
REMARK 465 LYS A 503
REMARK 465 GLU A 504
REMARK 465 SER A 505
REMARK 465 ILE A 506
REMARK 465 ALA A 507
REMARK 465 GLU A 508
REMARK 465 SER A 509
REMARK 465 LYS A 510
REMARK 465 SER A 511
REMARK 465 PRO A 512
REMARK 465 GLU A 513
REMARK 465 MET A 514
REMARK 465 SER A 515
REMARK 465 MET A 516
REMARK 465 GLN A 517
REMARK 465 GLU A 518
REMARK 465 ASP A 519
REMARK 465 CYS A 520
REMARK 465 ILE A 521
REMARK 465 SER A 522
REMARK 465 ASP A 523
REMARK 465 ILE A 524
REMARK 465 ALA A 525
REMARK 465 PRO A 526
REMARK 465 MET A 527
REMARK 465 GLN A 528
REMARK 465 THR A 529
REMARK 465 ASP A 530
REMARK 465 GLU A 531
REMARK 465 GLN A 532
REMARK 465 THR A 533
REMARK 465 ASN A 534
REMARK 465 LYS A 535
REMARK 465 GLU A 536
REMARK 465 CYS A 596
REMARK 465 LYS A 597
REMARK 465 GLY A 598
REMARK 465 GLY A 674
REMARK 465 ASP A 675
REMARK 465 ASP A 696
REMARK 465 GLY A 697
REMARK 465 ALA A 698
REMARK 465 ASN A 699
REMARK 465 ASP A 700
REMARK 465 LEU A 701
REMARK 465 PHE A 702
REMARK 465 PHE A 703
REMARK 465 GLN A 704
REMARK 465 PRO A 705
REMARK 465 PRO A 706
REMARK 465 PRO A 707
REMARK 465 THR A 716
REMARK 465 ILE A 717
REMARK 465 ARG A 718
REMARK 465 PRO A 719
REMARK 465 TYR A 720
REMARK 465 PHE A 721
REMARK 465 PRO A 722
REMARK 465 LYS A 723
REMARK 465 ASP A 724
REMARK 465 GLU A 725
REMARK 465 ALA A 726
REMARK 465 SER A 727
REMARK 465 VAL A 728
REMARK 465 TYR A 729
REMARK 465 LYS A 730
REMARK 465 ILE A 731
REMARK 465 CYS A 732
REMARK 465 ARG A 733
REMARK 465 GLU A 734
REMARK 465 MET A 735
REMARK 465 TYR A 736
REMARK 465 ASP A 737
REMARK 465 ASP A 738
REMARK 465 GLY A 739
REMARK 465 VAL A 740
REMARK 465 GLY A 741
REMARK 465 LEU A 742
REMARK 465 PRO A 743
REMARK 465 PHE A 744
REMARK 465 GLN A 745
REMARK 465 SER A 746
REMARK 465 GLN A 747
REMARK 465 PRO A 748
REMARK 465 ASP A 749
REMARK 465 LEU A 750
REMARK 465 ILE A 751
REMARK 465 GLY A 752
REMARK 465 ASP A 753
REMARK 465 LYS A 754
REMARK 465 LEU A 755
REMARK 465 VAL A 756
REMARK 465 GLY A 757
REMARK 465 GLY A 758
REMARK 465 LEU A 759
REMARK 465 LEU A 760
REMARK 465 SER A 761
REMARK 465 LEU A 762
REMARK 465 SER A 763
REMARK 465 LEU A 764
REMARK 465 ASP A 765
REMARK 465 TYR A 766
REMARK 465 CYS A 767
REMARK 465 PHE A 768
REMARK 465 VAL A 769
REMARK 465 LEU A 770
REMARK 465 GLU A 771
REMARK 465 ASP A 772
REMARK 465 GLU A 773
REMARK 465 ASP A 774
REMARK 465 GLY A 775
REMARK 465 ILE A 776
REMARK 465 CYS A 777
REMARK 465 GLY A 778
REMARK 465 TYR A 779
REMARK 465 ALA A 780
REMARK 465 LEU A 781
REMARK 465 GLY A 782
REMARK 465 THR A 783
REMARK 465 VAL A 784
REMARK 465 ASP A 785
REMARK 465 VAL A 786
REMARK 465 THR A 787
REMARK 465 PRO A 788
REMARK 465 PHE A 789
REMARK 465 ILE A 790
REMARK 465 LYS A 791
REMARK 465 LYS A 792
REMARK 465 CYS A 793
REMARK 465 LYS A 794
REMARK 465 ILE A 795
REMARK 465 SER A 796
REMARK 465 TRP A 797
REMARK 465 ILE A 798
REMARK 465 PRO A 799
REMARK 465 PHE A 800
REMARK 465 MET A 801
REMARK 465 GLN A 802
REMARK 465 GLU A 803
REMARK 465 LYS A 804
REMARK 465 TYR A 805
REMARK 465 THR A 806
REMARK 465 LYS A 807
REMARK 465 PRO A 808
REMARK 465 ASN A 809
REMARK 465 GLY A 810
REMARK 465 ASP A 811
REMARK 465 LYS A 812
REMARK 465 GLU A 813
REMARK 465 LEU A 814
REMARK 465 SER A 815
REMARK 465 GLU A 816
REMARK 465 ALA A 817
REMARK 465 GLU A 818
REMARK 465 LYS A 819
REMARK 465 ILE A 820
REMARK 465 MET A 821
REMARK 465 LEU A 822
REMARK 465 SER A 823
REMARK 465 PHE A 824
REMARK 465 HIS A 825
REMARK 465 GLU A 826
REMARK 465 GLU A 827
REMARK 465 GLN A 828
REMARK 465 GLU A 829
REMARK 465 VAL A 830
REMARK 465 LEU A 831
REMARK 465 PRO A 832
REMARK 465 GLU A 833
REMARK 465 THR A 834
REMARK 465 PHE A 835
REMARK 465 LEU A 836
REMARK 465 ALA A 837
REMARK 465 ASN A 838
REMARK 465 PHE A 839
REMARK 465 PRO A 840
REMARK 465 SER A 841
REMARK 465 LEU A 842
REMARK 465 ILE A 843
REMARK 465 LYS A 844
REMARK 465 MET A 845
REMARK 465 ASP A 846
REMARK 465 ILE A 847
REMARK 465 HIS A 848
REMARK 465 LYS A 849
REMARK 465 LYS A 850
REMARK 465 VAL A 851
REMARK 465 THR A 852
REMARK 465 ASP A 853
REMARK 465 PRO A 854
REMARK 465 SER A 855
REMARK 465 VAL A 856
REMARK 465 ALA A 857
REMARK 465 LYS A 858
REMARK 465 SER A 859
REMARK 465 MET A 860
REMARK 465 MET A 861
REMARK 465 ALA A 862
REMARK 465 CYS A 863
REMARK 465 LEU A 864
REMARK 465 LEU A 865
REMARK 465 SER A 866
REMARK 465 SER A 867
REMARK 465 LEU A 868
REMARK 465 LYS A 869
REMARK 465 ALA A 870
REMARK 465 ASN A 871
REMARK 465 GLY A 872
REMARK 465 SER A 873
REMARK 465 ARG A 874
REMARK 465 GLY A 875
REMARK 465 ALA A 876
REMARK 465 PHE A 877
REMARK 465 CYS A 878
REMARK 465 GLU A 879
REMARK 465 VAL A 880
REMARK 465 ARG A 881
REMARK 465 PRO A 882
REMARK 465 ASP A 883
REMARK 465 ASP A 884
REMARK 465 LYS A 885
REMARK 465 ARG A 886
REMARK 465 ILE A 887
REMARK 465 LEU A 888
REMARK 465 GLU A 889
REMARK 465 PHE A 890
REMARK 465 TYR A 891
REMARK 465 SER A 892
REMARK 465 LYS A 893
REMARK 465 LEU A 894
REMARK 465 GLY A 895
REMARK 465 CYS A 896
REMARK 465 PHE A 897
REMARK 465 GLU A 898
REMARK 465 ILE A 899
REMARK 465 ALA A 900
REMARK 465 LYS A 901
REMARK 465 MET A 902
REMARK 465 GLU A 903
REMARK 465 GLY A 904
REMARK 465 PHE A 905
REMARK 465 PRO A 906
REMARK 465 LYS A 907
REMARK 465 ASP A 908
REMARK 465 VAL A 909
REMARK 465 VAL A 910
REMARK 465 ILE A 911
REMARK 465 LEU A 912
REMARK 465 GLY A 913
REMARK 465 ARG A 914
REMARK 465 SER A 915
REMARK 465 LEU A 916
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 GLN B 3
REMARK 465 LYS B 4
REMARK 465 GLU B 5
REMARK 465 SER B 6
REMARK 465 GLN B 7
REMARK 465 ALA B 8
REMARK 465 THR B 9
REMARK 465 LEU B 10
REMARK 465 GLU B 11
REMARK 465 GLU B 12
REMARK 465 ARG B 13
REMARK 465 GLU B 14
REMARK 465 SER B 15
REMARK 465 GLU B 16
REMARK 465 LEU B 17
REMARK 465 SER B 18
REMARK 465 SER B 19
REMARK 465 ASN B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 SER B 24
REMARK 465 ALA B 25
REMARK 465 GLY B 26
REMARK 465 ALA B 27
REMARK 465 SER B 28
REMARK 465 LEU B 29
REMARK 465 GLU B 30
REMARK 465 PRO B 31
REMARK 465 PRO B 32
REMARK 465 ALA B 33
REMARK 465 ALA B 34
REMARK 465 PRO B 35
REMARK 465 ALA B 36
REMARK 465 PRO B 37
REMARK 465 GLY B 38
REMARK 465 GLU B 39
REMARK 465 ASP B 40
REMARK 465 ASN B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 GLY B 44
REMARK 465 ALA B 45
REMARK 465 GLY B 46
REMARK 465 GLY B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 VAL B 50
REMARK 465 ALA B 51
REMARK 465 GLY B 52
REMARK 465 ALA B 53
REMARK 465 ALA B 54
REMARK 465 GLY B 55
REMARK 465 GLY B 56
REMARK 465 ALA B 57
REMARK 465 ARG B 58
REMARK 465 LYS B 341
REMARK 465 ASP B 342
REMARK 465 VAL B 343
REMARK 465 VAL B 344
REMARK 465 MET B 345
REMARK 465 THR B 346
REMARK 465 ASP B 347
REMARK 465 SER B 348
REMARK 465 GLU B 349
REMARK 465 ASP B 350
REMARK 465 SER B 351
REMARK 465 THR B 352
REMARK 465 VAL B 353
REMARK 465 SER B 354
REMARK 465 ILE B 355
REMARK 465 GLN B 356
REMARK 465 ILE B 357
REMARK 465 LYS B 358
REMARK 465 LEU B 359
REMARK 465 GLU B 360
REMARK 465 ASN B 361
REMARK 465 GLU B 362
REMARK 465 GLY B 363
REMARK 465 SER B 364
REMARK 465 ASP B 365
REMARK 465 GLU B 366
REMARK 465 ASP B 367
REMARK 465 ILE B 368
REMARK 465 GLU B 369
REMARK 465 THR B 370
REMARK 465 GLN B 396
REMARK 465 TYR B 397
REMARK 465 SER B 398
REMARK 465 SER B 399
REMARK 465 ARG B 400
REMARK 465 GLN B 401
REMARK 465 VAL B 402
REMARK 465 ALA B 403
REMARK 465 HIS B 404
REMARK 465 SER B 405
REMARK 465 GLY B 406
REMARK 465 ALA B 407
REMARK 465 LYS B 408
REMARK 465 ALA B 409
REMARK 465 SER B 410
REMARK 465 VAL B 411
REMARK 465 VAL B 412
REMARK 465 ASP B 413
REMARK 465 GLY B 414
REMARK 465 THR B 415
REMARK 465 PRO B 416
REMARK 465 LEU B 417
REMARK 465 VAL B 418
REMARK 465 ALA B 419
REMARK 465 ALA B 420
REMARK 465 PRO B 421
REMARK 465 SER B 422
REMARK 465 LEU B 423
REMARK 465 ASN B 424
REMARK 465 ALA B 425
REMARK 465 THR B 426
REMARK 465 THR B 427
REMARK 465 VAL B 428
REMARK 465 VAL B 429
REMARK 465 THR B 430
REMARK 465 THR B 431
REMARK 465 VAL B 432
REMARK 465 TYR B 433
REMARK 465 GLN B 434
REMARK 465 GLU B 435
REMARK 465 PRO B 436
REMARK 465 ILE B 437
REMARK 465 MET B 438
REMARK 465 SER B 439
REMARK 465 GLN B 440
REMARK 465 GLY B 441
REMARK 465 ALA B 442
REMARK 465 ALA B 443
REMARK 465 LEU B 444
REMARK 465 SER B 445
REMARK 465 GLY B 446
REMARK 465 GLU B 447
REMARK 465 PRO B 448
REMARK 465 THR B 449
REMARK 465 THR B 450
REMARK 465 LEU B 451
REMARK 465 THR B 452
REMARK 465 LYS B 453
REMARK 465 GLU B 454
REMARK 465 GLU B 455
REMARK 465 GLU B 456
REMARK 465 LYS B 457
REMARK 465 LYS B 458
REMARK 465 GLN B 459
REMARK 465 PRO B 460
REMARK 465 ASP B 461
REMARK 465 GLU B 462
REMARK 465 GLU B 463
REMARK 465 PRO B 464
REMARK 465 MET B 465
REMARK 465 ASP B 466
REMARK 465 MET B 467
REMARK 465 VAL B 468
REMARK 465 VAL B 469
REMARK 465 GLU B 470
REMARK 465 LYS B 471
REMARK 465 GLN B 472
REMARK 465 GLU B 473
REMARK 465 GLU B 474
REMARK 465 THR B 475
REMARK 465 ASP B 476
REMARK 465 HIS B 477
REMARK 465 LYS B 478
REMARK 465 ASN B 479
REMARK 465 ASP B 480
REMARK 465 ASN B 481
REMARK 465 GLN B 482
REMARK 465 ILE B 483
REMARK 465 LEU B 484
REMARK 465 SER B 485
REMARK 465 GLU B 486
REMARK 465 ILE B 487
REMARK 465 VAL B 488
REMARK 465 GLU B 489
REMARK 465 ALA B 490
REMARK 465 LYS B 491
REMARK 465 MET B 492
REMARK 465 ALA B 493
REMARK 465 GLU B 494
REMARK 465 GLU B 495
REMARK 465 LEU B 496
REMARK 465 LYS B 497
REMARK 465 PRO B 498
REMARK 465 MET B 499
REMARK 465 ASP B 500
REMARK 465 THR B 501
REMARK 465 ASP B 502
REMARK 465 LYS B 503
REMARK 465 GLU B 504
REMARK 465 SER B 505
REMARK 465 ILE B 506
REMARK 465 ALA B 507
REMARK 465 GLU B 508
REMARK 465 SER B 509
REMARK 465 LYS B 510
REMARK 465 SER B 511
REMARK 465 PRO B 512
REMARK 465 GLU B 513
REMARK 465 MET B 514
REMARK 465 SER B 515
REMARK 465 MET B 516
REMARK 465 GLN B 517
REMARK 465 GLU B 518
REMARK 465 ASP B 519
REMARK 465 CYS B 520
REMARK 465 ILE B 521
REMARK 465 SER B 522
REMARK 465 ASP B 523
REMARK 465 ILE B 524
REMARK 465 ALA B 525
REMARK 465 PRO B 526
REMARK 465 MET B 527
REMARK 465 GLN B 528
REMARK 465 THR B 529
REMARK 465 ASP B 530
REMARK 465 GLU B 531
REMARK 465 GLN B 532
REMARK 465 THR B 533
REMARK 465 ASN B 534
REMARK 465 LYS B 535
REMARK 465 GLU B 536
REMARK 465 LYS B 597
REMARK 465 GLY B 598
REMARK 465 LYS B 599
REMARK 465 ILE B 673
REMARK 465 GLY B 674
REMARK 465 ASP B 696
REMARK 465 GLY B 697
REMARK 465 ALA B 698
REMARK 465 ASN B 699
REMARK 465 ASP B 700
REMARK 465 LEU B 701
REMARK 465 PHE B 702
REMARK 465 PHE B 703
REMARK 465 GLN B 704
REMARK 465 PRO B 705
REMARK 465 PRO B 706
REMARK 465 THR B 716
REMARK 465 ILE B 717
REMARK 465 ARG B 718
REMARK 465 PRO B 719
REMARK 465 TYR B 720
REMARK 465 PHE B 721
REMARK 465 PRO B 722
REMARK 465 LYS B 723
REMARK 465 ASP B 724
REMARK 465 GLU B 725
REMARK 465 ALA B 726
REMARK 465 SER B 727
REMARK 465 VAL B 728
REMARK 465 TYR B 729
REMARK 465 LYS B 730
REMARK 465 ILE B 731
REMARK 465 CYS B 732
REMARK 465 ARG B 733
REMARK 465 GLU B 734
REMARK 465 MET B 735
REMARK 465 TYR B 736
REMARK 465 ASP B 737
REMARK 465 ASP B 738
REMARK 465 GLY B 739
REMARK 465 VAL B 740
REMARK 465 GLY B 741
REMARK 465 LEU B 742
REMARK 465 PRO B 743
REMARK 465 PHE B 744
REMARK 465 GLN B 745
REMARK 465 SER B 746
REMARK 465 GLN B 747
REMARK 465 PRO B 748
REMARK 465 ASP B 749
REMARK 465 LEU B 750
REMARK 465 ILE B 751
REMARK 465 GLY B 752
REMARK 465 ASP B 753
REMARK 465 LYS B 754
REMARK 465 LEU B 755
REMARK 465 VAL B 756
REMARK 465 GLY B 757
REMARK 465 GLY B 758
REMARK 465 LEU B 759
REMARK 465 LEU B 760
REMARK 465 SER B 761
REMARK 465 LEU B 762
REMARK 465 SER B 763
REMARK 465 LEU B 764
REMARK 465 ASP B 765
REMARK 465 TYR B 766
REMARK 465 CYS B 767
REMARK 465 PHE B 768
REMARK 465 VAL B 769
REMARK 465 LEU B 770
REMARK 465 GLU B 771
REMARK 465 ASP B 772
REMARK 465 GLU B 773
REMARK 465 ASP B 774
REMARK 465 GLY B 775
REMARK 465 ILE B 776
REMARK 465 CYS B 777
REMARK 465 GLY B 778
REMARK 465 TYR B 779
REMARK 465 ALA B 780
REMARK 465 LEU B 781
REMARK 465 GLY B 782
REMARK 465 THR B 783
REMARK 465 VAL B 784
REMARK 465 ASP B 785
REMARK 465 VAL B 786
REMARK 465 THR B 787
REMARK 465 PRO B 788
REMARK 465 PHE B 789
REMARK 465 ILE B 790
REMARK 465 LYS B 791
REMARK 465 LYS B 792
REMARK 465 CYS B 793
REMARK 465 LYS B 794
REMARK 465 ILE B 795
REMARK 465 SER B 796
REMARK 465 TRP B 797
REMARK 465 ILE B 798
REMARK 465 PRO B 799
REMARK 465 PHE B 800
REMARK 465 MET B 801
REMARK 465 GLN B 802
REMARK 465 GLU B 803
REMARK 465 LYS B 804
REMARK 465 TYR B 805
REMARK 465 THR B 806
REMARK 465 LYS B 807
REMARK 465 PRO B 808
REMARK 465 ASN B 809
REMARK 465 GLY B 810
REMARK 465 ASP B 811
REMARK 465 LYS B 812
REMARK 465 GLU B 813
REMARK 465 LEU B 814
REMARK 465 SER B 815
REMARK 465 GLU B 816
REMARK 465 ALA B 817
REMARK 465 GLU B 818
REMARK 465 LYS B 819
REMARK 465 ILE B 820
REMARK 465 MET B 821
REMARK 465 LEU B 822
REMARK 465 SER B 823
REMARK 465 PHE B 824
REMARK 465 HIS B 825
REMARK 465 GLU B 826
REMARK 465 GLU B 827
REMARK 465 GLN B 828
REMARK 465 GLU B 829
REMARK 465 VAL B 830
REMARK 465 LEU B 831
REMARK 465 PRO B 832
REMARK 465 GLU B 833
REMARK 465 THR B 834
REMARK 465 PHE B 835
REMARK 465 LEU B 836
REMARK 465 ALA B 837
REMARK 465 ASN B 838
REMARK 465 PHE B 839
REMARK 465 PRO B 840
REMARK 465 SER B 841
REMARK 465 LEU B 842
REMARK 465 ILE B 843
REMARK 465 LYS B 844
REMARK 465 MET B 845
REMARK 465 ASP B 846
REMARK 465 ILE B 847
REMARK 465 HIS B 848
REMARK 465 LYS B 849
REMARK 465 LYS B 850
REMARK 465 VAL B 851
REMARK 465 THR B 852
REMARK 465 ASP B 853
REMARK 465 PRO B 854
REMARK 465 SER B 855
REMARK 465 VAL B 856
REMARK 465 ALA B 857
REMARK 465 LYS B 858
REMARK 465 SER B 859
REMARK 465 MET B 860
REMARK 465 MET B 861
REMARK 465 ALA B 862
REMARK 465 CYS B 863
REMARK 465 LEU B 864
REMARK 465 LEU B 865
REMARK 465 SER B 866
REMARK 465 SER B 867
REMARK 465 LEU B 868
REMARK 465 LYS B 869
REMARK 465 ALA B 870
REMARK 465 ASN B 871
REMARK 465 GLY B 872
REMARK 465 SER B 873
REMARK 465 ARG B 874
REMARK 465 GLY B 875
REMARK 465 ALA B 876
REMARK 465 PHE B 877
REMARK 465 CYS B 878
REMARK 465 GLU B 879
REMARK 465 VAL B 880
REMARK 465 ARG B 881
REMARK 465 PRO B 882
REMARK 465 ASP B 883
REMARK 465 ASP B 884
REMARK 465 LYS B 885
REMARK 465 ARG B 886
REMARK 465 ILE B 887
REMARK 465 LEU B 888
REMARK 465 GLU B 889
REMARK 465 PHE B 890
REMARK 465 TYR B 891
REMARK 465 SER B 892
REMARK 465 LYS B 893
REMARK 465 LEU B 894
REMARK 465 GLY B 895
REMARK 465 CYS B 896
REMARK 465 PHE B 897
REMARK 465 GLU B 898
REMARK 465 ILE B 899
REMARK 465 ALA B 900
REMARK 465 LYS B 901
REMARK 465 MET B 902
REMARK 465 GLU B 903
REMARK 465 GLY B 904
REMARK 465 PHE B 905
REMARK 465 PRO B 906
REMARK 465 LYS B 907
REMARK 465 ASP B 908
REMARK 465 VAL B 909
REMARK 465 VAL B 910
REMARK 465 ILE B 911
REMARK 465 LEU B 912
REMARK 465 GLY B 913
REMARK 465 ARG B 914
REMARK 465 SER B 915
REMARK 465 LEU B 916
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 677 CG GLU A 677 CD 0.099
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 159 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 167 CB - CG - CD ANGL. DEV. = 18.8 DEGREES
REMARK 500 ARG A 167 CG - CD - NE ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LEU A 303 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG A 634 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 634 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 108 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 290 NE - CZ - NH2 ANGL. DEV. = -3.8 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 GLU A 89 36.11 70.39
REMARK 500 ALA A 96 48.04 -149.22
REMARK 500 ARG A 104 -68.54 -138.70
REMARK 500 PHE A 106 48.32 -109.69
REMARK 500 ASP A 142 -29.91 -144.83
REMARK 500 PRO A 314 -155.81 -104.12
REMARK 500 ASN A 335 50.08 -143.91
REMARK 500 TYR A 566 -87.42 -93.92
REMARK 500 VAL A 594 -158.68 -127.12
REMARK 500 HIS A 666 -28.38 -152.77
REMARK 500 ALA B 96 47.90 -150.79
REMARK 500 ARG B 104 -67.23 -140.25
REMARK 500 ASP B 142 6.61 -154.18
REMARK 500 PRO B 314 -155.40 -105.80
REMARK 500 ASN B 335 46.01 -141.43
REMARK 500 TYR B 566 -87.66 -94.14
REMARK 500 VAL B 594 -167.34 -123.92
REMARK 500 HIS B 666 -29.05 -154.58
REMARK 500 SER B 712 32.23 -69.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5M7R A 1 916 UNP O60502 OGA_HUMAN 1 916
DBREF 5M7R B 1 916 UNP O60502 OGA_HUMAN 1 916
SEQRES 1 A 916 MET VAL GLN LYS GLU SER GLN ALA THR LEU GLU GLU ARG
SEQRES 2 A 916 GLU SER GLU LEU SER SER ASN PRO ALA ALA SER ALA GLY
SEQRES 3 A 916 ALA SER LEU GLU PRO PRO ALA ALA PRO ALA PRO GLY GLU
SEQRES 4 A 916 ASP ASN PRO ALA GLY ALA GLY GLY ALA ALA VAL ALA GLY
SEQRES 5 A 916 ALA ALA GLY GLY ALA ARG ARG PHE LEU CYS GLY VAL VAL
SEQRES 6 A 916 GLU GLY PHE TYR GLY ARG PRO TRP VAL MET GLU GLN ARG
SEQRES 7 A 916 LYS GLU LEU PHE ARG ARG LEU GLN LYS TRP GLU LEU ASN
SEQRES 8 A 916 THR TYR LEU TYR ALA PRO LYS ASP ASP TYR LYS HIS ARG
SEQRES 9 A 916 MET PHE TRP ARG GLU MET TYR SER VAL GLU GLU ALA GLU
SEQRES 10 A 916 GLN LEU MET THR LEU ILE SER ALA ALA ARG GLU TYR GLU
SEQRES 11 A 916 ILE GLU PHE ILE TYR ALA ILE SER PRO GLY LEU ASP ILE
SEQRES 12 A 916 THR PHE SER ASN PRO LYS GLU VAL SER THR LEU LYS ARG
SEQRES 13 A 916 LYS LEU ASP GLN VAL SER GLN PHE GLY CYS ARG SER PHE
SEQRES 14 A 916 ALA LEU LEU PHE ASP ASP ILE ASP HIS ASN MET CYS ALA
SEQRES 15 A 916 ALA ASP LYS GLU VAL PHE SER SER PHE ALA HIS ALA GLN
SEQRES 16 A 916 VAL SER ILE THR ASN GLU ILE TYR GLN TYR LEU GLY GLU
SEQRES 17 A 916 PRO GLU THR PHE LEU PHE CYS PRO THR GLU TYR CYS GLY
SEQRES 18 A 916 THR PHE CYS TYR PRO ASN VAL SER GLN SER PRO TYR LEU
SEQRES 19 A 916 ARG THR VAL GLY GLU LYS LEU LEU PRO GLY ILE GLU VAL
SEQRES 20 A 916 LEU TRP THR GLY PRO LYS VAL VAL SER LYS GLU ILE PRO
SEQRES 21 A 916 VAL GLU SER ILE GLU GLU VAL SER LYS ILE ILE LYS ARG
SEQRES 22 A 916 ALA PRO VAL ILE TRP ASP ASN ILE HIS ALA ASN ASP TYR
SEQRES 23 A 916 ASP GLN LYS ARG LEU PHE LEU GLY PRO TYR LYS GLY ARG
SEQRES 24 A 916 SER THR GLU LEU ILE PRO ARG LEU LYS GLY VAL LEU THR
SEQRES 25 A 916 ASN PRO ASN CYS GLU PHE GLU ALA ASN TYR VAL ALA ILE
SEQRES 26 A 916 HIS THR LEU ALA THR TRP TYR LYS SER ASN MET ASN GLY
SEQRES 27 A 916 VAL ARG LYS ASP VAL VAL MET THR ASP SER GLU ASP SER
SEQRES 28 A 916 THR VAL SER ILE GLN ILE LYS LEU GLU ASN GLU GLY SER
SEQRES 29 A 916 ASP GLU ASP ILE GLU THR ASP VAL LEU TYR SER PRO GLN
SEQRES 30 A 916 MET ALA LEU LYS LEU ALA LEU THR GLU TRP LEU GLN GLU
SEQRES 31 A 916 PHE GLY VAL PRO HIS GLN TYR SER SER ARG GLN VAL ALA
SEQRES 32 A 916 HIS SER GLY ALA LYS ALA SER VAL VAL ASP GLY THR PRO
SEQRES 33 A 916 LEU VAL ALA ALA PRO SER LEU ASN ALA THR THR VAL VAL
SEQRES 34 A 916 THR THR VAL TYR GLN GLU PRO ILE MET SER GLN GLY ALA
SEQRES 35 A 916 ALA LEU SER GLY GLU PRO THR THR LEU THR LYS GLU GLU
SEQRES 36 A 916 GLU LYS LYS GLN PRO ASP GLU GLU PRO MET ASP MET VAL
SEQRES 37 A 916 VAL GLU LYS GLN GLU GLU THR ASP HIS LYS ASN ASP ASN
SEQRES 38 A 916 GLN ILE LEU SER GLU ILE VAL GLU ALA LYS MET ALA GLU
SEQRES 39 A 916 GLU LEU LYS PRO MET ASP THR ASP LYS GLU SER ILE ALA
SEQRES 40 A 916 GLU SER LYS SER PRO GLU MET SER MET GLN GLU ASP CYS
SEQRES 41 A 916 ILE SER ASP ILE ALA PRO MET GLN THR ASP GLU GLN THR
SEQRES 42 A 916 ASN LYS GLU GLN PHE VAL PRO GLY PRO ASN GLU LYS PRO
SEQRES 43 A 916 LEU TYR THR ALA GLU PRO VAL THR LEU GLU ASP LEU GLN
SEQRES 44 A 916 LEU LEU ALA ASP LEU PHE TYR LEU PRO TYR GLU HIS GLY
SEQRES 45 A 916 PRO LYS GLY ALA GLN MET LEU ARG GLU PHE GLN TRP LEU
SEQRES 46 A 916 ARG ALA ASN SER SER VAL VAL SER VAL ASN CYS LYS GLY
SEQRES 47 A 916 LYS ASP SER GLU LYS ILE GLU GLU TRP ARG SER ARG ALA
SEQRES 48 A 916 ALA LYS PHE GLU GLU MET CYS GLY LEU VAL MET GLY MET
SEQRES 49 A 916 PHE THR ARG LEU SER ASN CYS ALA ASN ARG THR ILE LEU
SEQRES 50 A 916 TYR ASP MET TYR SER TYR VAL TRP ASP ILE LYS SER ILE
SEQRES 51 A 916 MET SER MET VAL LYS SER PHE VAL GLN TRP LEU GLY CYS
SEQRES 52 A 916 ARG SER HIS SER SER ALA GLN PHE LEU ILE GLY ASP GLN
SEQRES 53 A 916 GLU PRO TRP ALA PHE ARG GLY GLY LEU ALA GLY GLU PHE
SEQRES 54 A 916 GLN ARG LEU LEU PRO ILE ASP GLY ALA ASN ASP LEU PHE
SEQRES 55 A 916 PHE GLN PRO PRO PRO LEU THR PRO THR SER LYS VAL TYR
SEQRES 56 A 916 THR ILE ARG PRO TYR PHE PRO LYS ASP GLU ALA SER VAL
SEQRES 57 A 916 TYR LYS ILE CYS ARG GLU MET TYR ASP ASP GLY VAL GLY
SEQRES 58 A 916 LEU PRO PHE GLN SER GLN PRO ASP LEU ILE GLY ASP LYS
SEQRES 59 A 916 LEU VAL GLY GLY LEU LEU SER LEU SER LEU ASP TYR CYS
SEQRES 60 A 916 PHE VAL LEU GLU ASP GLU ASP GLY ILE CYS GLY TYR ALA
SEQRES 61 A 916 LEU GLY THR VAL ASP VAL THR PRO PHE ILE LYS LYS CYS
SEQRES 62 A 916 LYS ILE SER TRP ILE PRO PHE MET GLN GLU LYS TYR THR
SEQRES 63 A 916 LYS PRO ASN GLY ASP LYS GLU LEU SER GLU ALA GLU LYS
SEQRES 64 A 916 ILE MET LEU SER PHE HIS GLU GLU GLN GLU VAL LEU PRO
SEQRES 65 A 916 GLU THR PHE LEU ALA ASN PHE PRO SER LEU ILE LYS MET
SEQRES 66 A 916 ASP ILE HIS LYS LYS VAL THR ASP PRO SER VAL ALA LYS
SEQRES 67 A 916 SER MET MET ALA CYS LEU LEU SER SER LEU LYS ALA ASN
SEQRES 68 A 916 GLY SER ARG GLY ALA PHE CYS GLU VAL ARG PRO ASP ASP
SEQRES 69 A 916 LYS ARG ILE LEU GLU PHE TYR SER LYS LEU GLY CYS PHE
SEQRES 70 A 916 GLU ILE ALA LYS MET GLU GLY PHE PRO LYS ASP VAL VAL
SEQRES 71 A 916 ILE LEU GLY ARG SER LEU
SEQRES 1 B 916 MET VAL GLN LYS GLU SER GLN ALA THR LEU GLU GLU ARG
SEQRES 2 B 916 GLU SER GLU LEU SER SER ASN PRO ALA ALA SER ALA GLY
SEQRES 3 B 916 ALA SER LEU GLU PRO PRO ALA ALA PRO ALA PRO GLY GLU
SEQRES 4 B 916 ASP ASN PRO ALA GLY ALA GLY GLY ALA ALA VAL ALA GLY
SEQRES 5 B 916 ALA ALA GLY GLY ALA ARG ARG PHE LEU CYS GLY VAL VAL
SEQRES 6 B 916 GLU GLY PHE TYR GLY ARG PRO TRP VAL MET GLU GLN ARG
SEQRES 7 B 916 LYS GLU LEU PHE ARG ARG LEU GLN LYS TRP GLU LEU ASN
SEQRES 8 B 916 THR TYR LEU TYR ALA PRO LYS ASP ASP TYR LYS HIS ARG
SEQRES 9 B 916 MET PHE TRP ARG GLU MET TYR SER VAL GLU GLU ALA GLU
SEQRES 10 B 916 GLN LEU MET THR LEU ILE SER ALA ALA ARG GLU TYR GLU
SEQRES 11 B 916 ILE GLU PHE ILE TYR ALA ILE SER PRO GLY LEU ASP ILE
SEQRES 12 B 916 THR PHE SER ASN PRO LYS GLU VAL SER THR LEU LYS ARG
SEQRES 13 B 916 LYS LEU ASP GLN VAL SER GLN PHE GLY CYS ARG SER PHE
SEQRES 14 B 916 ALA LEU LEU PHE ASP ASP ILE ASP HIS ASN MET CYS ALA
SEQRES 15 B 916 ALA ASP LYS GLU VAL PHE SER SER PHE ALA HIS ALA GLN
SEQRES 16 B 916 VAL SER ILE THR ASN GLU ILE TYR GLN TYR LEU GLY GLU
SEQRES 17 B 916 PRO GLU THR PHE LEU PHE CYS PRO THR GLU TYR CYS GLY
SEQRES 18 B 916 THR PHE CYS TYR PRO ASN VAL SER GLN SER PRO TYR LEU
SEQRES 19 B 916 ARG THR VAL GLY GLU LYS LEU LEU PRO GLY ILE GLU VAL
SEQRES 20 B 916 LEU TRP THR GLY PRO LYS VAL VAL SER LYS GLU ILE PRO
SEQRES 21 B 916 VAL GLU SER ILE GLU GLU VAL SER LYS ILE ILE LYS ARG
SEQRES 22 B 916 ALA PRO VAL ILE TRP ASP ASN ILE HIS ALA ASN ASP TYR
SEQRES 23 B 916 ASP GLN LYS ARG LEU PHE LEU GLY PRO TYR LYS GLY ARG
SEQRES 24 B 916 SER THR GLU LEU ILE PRO ARG LEU LYS GLY VAL LEU THR
SEQRES 25 B 916 ASN PRO ASN CYS GLU PHE GLU ALA ASN TYR VAL ALA ILE
SEQRES 26 B 916 HIS THR LEU ALA THR TRP TYR LYS SER ASN MET ASN GLY
SEQRES 27 B 916 VAL ARG LYS ASP VAL VAL MET THR ASP SER GLU ASP SER
SEQRES 28 B 916 THR VAL SER ILE GLN ILE LYS LEU GLU ASN GLU GLY SER
SEQRES 29 B 916 ASP GLU ASP ILE GLU THR ASP VAL LEU TYR SER PRO GLN
SEQRES 30 B 916 MET ALA LEU LYS LEU ALA LEU THR GLU TRP LEU GLN GLU
SEQRES 31 B 916 PHE GLY VAL PRO HIS GLN TYR SER SER ARG GLN VAL ALA
SEQRES 32 B 916 HIS SER GLY ALA LYS ALA SER VAL VAL ASP GLY THR PRO
SEQRES 33 B 916 LEU VAL ALA ALA PRO SER LEU ASN ALA THR THR VAL VAL
SEQRES 34 B 916 THR THR VAL TYR GLN GLU PRO ILE MET SER GLN GLY ALA
SEQRES 35 B 916 ALA LEU SER GLY GLU PRO THR THR LEU THR LYS GLU GLU
SEQRES 36 B 916 GLU LYS LYS GLN PRO ASP GLU GLU PRO MET ASP MET VAL
SEQRES 37 B 916 VAL GLU LYS GLN GLU GLU THR ASP HIS LYS ASN ASP ASN
SEQRES 38 B 916 GLN ILE LEU SER GLU ILE VAL GLU ALA LYS MET ALA GLU
SEQRES 39 B 916 GLU LEU LYS PRO MET ASP THR ASP LYS GLU SER ILE ALA
SEQRES 40 B 916 GLU SER LYS SER PRO GLU MET SER MET GLN GLU ASP CYS
SEQRES 41 B 916 ILE SER ASP ILE ALA PRO MET GLN THR ASP GLU GLN THR
SEQRES 42 B 916 ASN LYS GLU GLN PHE VAL PRO GLY PRO ASN GLU LYS PRO
SEQRES 43 B 916 LEU TYR THR ALA GLU PRO VAL THR LEU GLU ASP LEU GLN
SEQRES 44 B 916 LEU LEU ALA ASP LEU PHE TYR LEU PRO TYR GLU HIS GLY
SEQRES 45 B 916 PRO LYS GLY ALA GLN MET LEU ARG GLU PHE GLN TRP LEU
SEQRES 46 B 916 ARG ALA ASN SER SER VAL VAL SER VAL ASN CYS LYS GLY
SEQRES 47 B 916 LYS ASP SER GLU LYS ILE GLU GLU TRP ARG SER ARG ALA
SEQRES 48 B 916 ALA LYS PHE GLU GLU MET CYS GLY LEU VAL MET GLY MET
SEQRES 49 B 916 PHE THR ARG LEU SER ASN CYS ALA ASN ARG THR ILE LEU
SEQRES 50 B 916 TYR ASP MET TYR SER TYR VAL TRP ASP ILE LYS SER ILE
SEQRES 51 B 916 MET SER MET VAL LYS SER PHE VAL GLN TRP LEU GLY CYS
SEQRES 52 B 916 ARG SER HIS SER SER ALA GLN PHE LEU ILE GLY ASP GLN
SEQRES 53 B 916 GLU PRO TRP ALA PHE ARG GLY GLY LEU ALA GLY GLU PHE
SEQRES 54 B 916 GLN ARG LEU LEU PRO ILE ASP GLY ALA ASN ASP LEU PHE
SEQRES 55 B 916 PHE GLN PRO PRO PRO LEU THR PRO THR SER LYS VAL TYR
SEQRES 56 B 916 THR ILE ARG PRO TYR PHE PRO LYS ASP GLU ALA SER VAL
SEQRES 57 B 916 TYR LYS ILE CYS ARG GLU MET TYR ASP ASP GLY VAL GLY
SEQRES 58 B 916 LEU PRO PHE GLN SER GLN PRO ASP LEU ILE GLY ASP LYS
SEQRES 59 B 916 LEU VAL GLY GLY LEU LEU SER LEU SER LEU ASP TYR CYS
SEQRES 60 B 916 PHE VAL LEU GLU ASP GLU ASP GLY ILE CYS GLY TYR ALA
SEQRES 61 B 916 LEU GLY THR VAL ASP VAL THR PRO PHE ILE LYS LYS CYS
SEQRES 62 B 916 LYS ILE SER TRP ILE PRO PHE MET GLN GLU LYS TYR THR
SEQRES 63 B 916 LYS PRO ASN GLY ASP LYS GLU LEU SER GLU ALA GLU LYS
SEQRES 64 B 916 ILE MET LEU SER PHE HIS GLU GLU GLN GLU VAL LEU PRO
SEQRES 65 B 916 GLU THR PHE LEU ALA ASN PHE PRO SER LEU ILE LYS MET
SEQRES 66 B 916 ASP ILE HIS LYS LYS VAL THR ASP PRO SER VAL ALA LYS
SEQRES 67 B 916 SER MET MET ALA CYS LEU LEU SER SER LEU LYS ALA ASN
SEQRES 68 B 916 GLY SER ARG GLY ALA PHE CYS GLU VAL ARG PRO ASP ASP
SEQRES 69 B 916 LYS ARG ILE LEU GLU PHE TYR SER LYS LEU GLY CYS PHE
SEQRES 70 B 916 GLU ILE ALA LYS MET GLU GLY PHE PRO LYS ASP VAL VAL
SEQRES 71 B 916 ILE LEU GLY ARG SER LEU
FORMUL 3 HOH *52(H2 O)
HELIX 1 AA1 VAL A 74 TRP A 88 1 15
HELIX 2 AA2 SER A 112 TYR A 129 1 18
HELIX 3 AA3 ASN A 147 GLN A 163 1 17
HELIX 4 AA4 CYS A 181 PHE A 188 1 8
HELIX 5 AA5 SER A 190 LEU A 206 1 17
HELIX 6 AA6 CYS A 220 CYS A 224 5 5
HELIX 7 AA7 SER A 231 LEU A 241 1 11
HELIX 8 AA8 PRO A 260 LYS A 272 1 13
HELIX 9 AA9 SER A 300 LEU A 307 5 8
HELIX 10 AB1 GLU A 317 ALA A 320 5 4
HELIX 11 AB2 ASN A 321 ASN A 335 1 15
HELIX 12 AB3 SER A 375 GLN A 389 1 15
HELIX 13 AB4 THR A 554 PHE A 565 1 12
HELIX 14 AB5 GLY A 572 ASN A 588 1 17
HELIX 15 AB6 SER A 589 SER A 593 5 5
HELIX 16 AB7 ASP A 600 SER A 629 1 30
HELIX 17 AB8 ASN A 633 GLY A 662 1 30
HELIX 18 AB9 GLU A 677 ARG A 682 5 6
HELIX 19 AC1 GLY A 683 LEU A 693 1 11
HELIX 20 AC2 VAL B 74 TRP B 88 1 15
HELIX 21 AC3 SER B 112 TYR B 129 1 18
HELIX 22 AC4 ASN B 147 GLN B 163 1 17
HELIX 23 AC5 CYS B 181 PHE B 188 1 8
HELIX 24 AC6 SER B 190 LEU B 206 1 17
HELIX 25 AC7 CYS B 220 CYS B 224 5 5
HELIX 26 AC8 SER B 231 LEU B 241 1 11
HELIX 27 AC9 PRO B 260 LYS B 272 1 13
HELIX 28 AD1 SER B 300 LEU B 307 5 8
HELIX 29 AD2 GLU B 317 ALA B 320 5 4
HELIX 30 AD3 ASN B 321 ASN B 335 1 15
HELIX 31 AD4 SER B 375 GLN B 389 1 15
HELIX 32 AD5 THR B 554 PHE B 565 1 12
HELIX 33 AD6 GLY B 572 ASN B 588 1 17
HELIX 34 AD7 SER B 589 SER B 593 5 5
HELIX 35 AD8 SER B 601 SER B 629 1 29
HELIX 36 AD9 ASN B 633 GLY B 662 1 30
HELIX 37 AE1 GLU B 677 ARG B 682 5 6
HELIX 38 AE2 GLY B 683 LEU B 693 1 11
SHEET 1 AA1 9 LEU A 61 GLU A 66 0
SHEET 2 AA1 9 THR A 92 TYR A 95 1 O LEU A 94 N GLU A 66
SHEET 3 AA1 9 GLU A 132 ILE A 137 1 O ILE A 134 N TYR A 95
SHEET 4 AA1 9 SER A 168 LEU A 172 1 O LEU A 172 N ILE A 137
SHEET 5 AA1 9 PHE A 212 CYS A 215 1 O CYS A 215 N LEU A 171
SHEET 6 AA1 9 GLU A 246 TRP A 249 1 O LEU A 248 N PHE A 214
SHEET 7 AA1 9 VAL A 276 ASP A 279 1 O VAL A 276 N VAL A 247
SHEET 8 AA1 9 GLY A 309 THR A 312 1 O LEU A 311 N ILE A 277
SHEET 9 AA1 9 LEU A 61 GLU A 66 1 N VAL A 65 O THR A 312
SHEET 1 AA2 9 LEU B 61 GLU B 66 0
SHEET 2 AA2 9 THR B 92 TYR B 95 1 O LEU B 94 N GLU B 66
SHEET 3 AA2 9 GLU B 132 ILE B 137 1 O ILE B 134 N TYR B 95
SHEET 4 AA2 9 SER B 168 LEU B 172 1 O SER B 168 N TYR B 135
SHEET 5 AA2 9 PHE B 212 CYS B 215 1 O CYS B 215 N LEU B 171
SHEET 6 AA2 9 GLU B 246 TRP B 249 1 O LEU B 248 N PHE B 214
SHEET 7 AA2 9 VAL B 276 ASP B 279 1 O VAL B 276 N VAL B 247
SHEET 8 AA2 9 GLY B 309 THR B 312 1 O GLY B 309 N ILE B 277
SHEET 9 AA2 9 LEU B 61 GLU B 66 1 N VAL B 65 O THR B 312
CISPEP 1 TYR A 225 PRO A 226 0 -4.29
CISPEP 2 TYR B 225 PRO B 226 0 -5.96
CRYST1 102.230 102.230 285.490 90.00 90.00 90.00 P 43 21 2 16
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 0.009782 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003503 0.00000
(ATOM LINES ARE NOT SHOWN.)
END