HEADER MOTOR PROTEIN 22-FEB-12 4AKH
TITLE DYNEIN MOTOR DOMAIN - AMPPNP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN
COMPND 3 HEAVY CHAIN CYTOPLASMIC;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: RESIDUES 1-218,1364-3038,3292-4092;
COMPND 6 SYNONYM: GST 26, SJ26 ANTIGEN, SJGST, DYHC;
COMPND 7 EC: 2.5.1.18;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM, SACCHAROMYCES
SOURCE 3 CEREVISIAE;
SOURCE 4 ORGANISM_TAXID: 6182, 4932;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS MOTOR PROTEIN, MOTOR PROTEIN-TRANSFERASE COMPLEX, AAA+ PROTEIN, ASCE
KEYWDS 2 PROTEIN, MOTOR PROTEIN P-LOOP NTPASE, CYTOSKELETAL MOTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SCHMIDT,E.S.GLEAVE,A.P.CARTER
REVDAT 5 20-DEC-23 4AKH 1 REMARK LINK
REVDAT 4 01-JAN-20 4AKH 1 REMARK
REVDAT 3 15-MAR-17 4AKH 1 SOURCE
REVDAT 2 16-MAY-12 4AKH 1 JRNL
REVDAT 1 14-MAR-12 4AKH 0
JRNL AUTH H.SCHMIDT,E.S.GLEAVE,A.P.CARTER
JRNL TITL INSIGHTS INTO DYNEIN MOTOR DOMAIN FUNCTION FROM A 3.3
JRNL TITL 2 ANGSTROM CRYSTAL STRUCTURE
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 492 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 22426545
JRNL DOI 10.1038/NSMB.2272
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0019
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) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 90155
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4767
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) : 3.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6342
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3880
REMARK 3 BIN FREE R VALUE SET COUNT : 343
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 41496
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 176.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.90000
REMARK 3 B22 (A**2) : -4.03000
REMARK 3 B33 (A**2) : 5.94000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.40000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.755
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.670
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.589
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 42440 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 57468 ; 1.487 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 5290 ; 5.809 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1874 ;44.628 ;24.674
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 7448 ;19.373 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 196 ;18.160 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 6574 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 31502 ; 0.006 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 4092 B 1 4092 3808 0.07 0.05
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 : 1.20
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.
REMARK 4
REMARK 4 4AKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1290051428.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-11
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 : I02
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 : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94930
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 80.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 4AI6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 59.06500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 LYS A 217
REMARK 465 SER A 218
REMARK 465 ASP A 219
REMARK 465 GLU A 1364
REMARK 465 ILE A 2944
REMARK 465 VAL A 2945
REMARK 465 PRO A 2946
REMARK 465 GLU A 2947
REMARK 465 VAL A 2948
REMARK 465 ASN A 2949
REMARK 465 LYS A 2950
REMARK 465 GLU A 2951
REMARK 465 LEU A 2952
REMARK 465 VAL A 2953
REMARK 465 PHE A 2954
REMARK 465 THR A 2955
REMARK 465 GLU A 2956
REMARK 465 PRO A 2957
REMARK 465 ILE A 2958
REMARK 465 GLN A 2959
REMARK 465 LEU A 3029
REMARK 465 LYS A 3030
REMARK 465 VAL A 3031
REMARK 465 ASN A 3032
REMARK 465 GLU A 3033
REMARK 465 LEU A 3034
REMARK 465 ASN A 3035
REMARK 465 LYS A 3036
REMARK 465 THR A 3037
REMARK 465 LEU A 3038
REMARK 465 SER A 3292
REMARK 465 ILE A 3293
REMARK 465 SER A 3294
REMARK 465 LEU A 3295
REMARK 465 VAL A 3296
REMARK 465 LYS A 3659
REMARK 465 LYS A 3660
REMARK 465 SER A 3661
REMARK 465 ARG A 3662
REMARK 465 GLU A 3663
REMARK 465 THR A 3664
REMARK 465 ARG A 3665
REMARK 465 ALA A 3666
REMARK 465 ALA A 3667
REMARK 465 ARG A 3668
REMARK 465 LYS B 217
REMARK 465 SER B 218
REMARK 465 ASP B 219
REMARK 465 GLU B 1364
REMARK 465 ILE B 2944
REMARK 465 VAL B 2945
REMARK 465 PRO B 2946
REMARK 465 GLU B 2947
REMARK 465 VAL B 2948
REMARK 465 ASN B 2949
REMARK 465 LYS B 2950
REMARK 465 GLU B 2951
REMARK 465 LEU B 2952
REMARK 465 VAL B 2953
REMARK 465 PHE B 2954
REMARK 465 THR B 2955
REMARK 465 GLU B 2956
REMARK 465 PRO B 2957
REMARK 465 ILE B 2958
REMARK 465 GLN B 2959
REMARK 465 LEU B 3029
REMARK 465 LYS B 3030
REMARK 465 VAL B 3031
REMARK 465 ASN B 3032
REMARK 465 GLU B 3033
REMARK 465 LEU B 3034
REMARK 465 ASN B 3035
REMARK 465 LYS B 3036
REMARK 465 THR B 3037
REMARK 465 LEU B 3038
REMARK 465 SER B 3292
REMARK 465 ILE B 3293
REMARK 465 SER B 3294
REMARK 465 LEU B 3295
REMARK 465 VAL B 3296
REMARK 465 LYS B 3659
REMARK 465 LYS B 3660
REMARK 465 SER B 3661
REMARK 465 ARG B 3662
REMARK 465 GLU B 3663
REMARK 465 THR B 3664
REMARK 465 ARG B 3665
REMARK 465 ALA B 3666
REMARK 465 ALA B 3667
REMARK 465 ARG B 3668
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 1 OG
REMARK 470 PRO A 2 CG CD
REMARK 470 ILE A 3 CG1 CG2 CD1
REMARK 470 LEU A 4 CG CD1 CD2
REMARK 470 TYR A 6 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 7 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 7 CZ3 CH2
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 ILE A 9 CG1 CG2 CD1
REMARK 470 LYS A 10 CG CD CE NZ
REMARK 470 LEU A 12 CG CD1 CD2
REMARK 470 VAL A 13 CG1 CG2
REMARK 470 GLN A 14 CG CD OE1 NE2
REMARK 470 PRO A 15 CG CD
REMARK 470 THR A 16 OG1 CG2
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 18 CG CD1 CD2
REMARK 470 LEU A 19 CG CD1 CD2
REMARK 470 LEU A 20 CG CD1 CD2
REMARK 470 GLU A 21 CG CD OE1 OE2
REMARK 470 TYR A 22 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 23 CG CD1 CD2
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 GLU A 25 CG CD OE1 OE2
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 TYR A 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 28 CG CD OE1 OE2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 HIS A 30 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 31 CG CD1 CD2
REMARK 470 TYR A 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 ARG A 34 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 35 CG OD1 OD2
REMARK 470 GLU A 36 CG CD OE1 OE2
REMARK 470 ASP A 38 CG OD1 OD2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 TRP A 40 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 40 CZ3 CH2
REMARK 470 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 42 CG OD1 ND2
REMARK 470 LYS A 43 CG CD CE NZ
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 PHE A 45 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 LEU A 47 CG CD1 CD2
REMARK 470 LEU A 49 CG CD1 CD2
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 PHE A 51 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 52 CG CD
REMARK 470 ASN A 53 CG OD1 ND2
REMARK 470 LEU A 54 CG CD1 CD2
REMARK 470 PRO A 55 CG CD
REMARK 470 TYR A 56 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 57 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 58 CG1 CG2 CD1
REMARK 470 ASP A 59 CG OD1 OD2
REMARK 470 ASP A 61 CG OD1 OD2
REMARK 470 VAL A 62 CG1 CG2
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 LEU A 64 CG CD1 CD2
REMARK 470 THR A 65 OG1 CG2
REMARK 470 GLN A 66 CG CD OE1 NE2
REMARK 470 SER A 67 OG
REMARK 470 MET A 68 CG SD CE
REMARK 470 ILE A 70 CG1 CG2 CD1
REMARK 470 ILE A 71 CG1 CG2 CD1
REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 73 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 74 CG1 CG2 CD1
REMARK 470 ASP A 76 CG OD1 OD2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 HIS A 78 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 79 CG OD1 ND2
REMARK 470 MET A 80 CG SD CE
REMARK 470 LEU A 81 CG CD1 CD2
REMARK 470 CYS A 84 SG
REMARK 470 PRO A 85 CG CD
REMARK 470 LYS A 86 CG CD CE NZ
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 ILE A 91 CG1 CG2 CD1
REMARK 470 SER A 92 OG
REMARK 470 MET A 93 CG SD CE
REMARK 470 LEU A 94 CG CD1 CD2
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 VAL A 98 CG1 CG2
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 ASP A 100 CG OD1 OD2
REMARK 470 ILE A 101 CG1 CG2 CD1
REMARK 470 ARG A 102 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 103 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 105 CG1 CG2
REMARK 470 SER A 106 OG
REMARK 470 ARG A 107 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 108 CG1 CG2 CD1
REMARK 470 TYR A 110 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 111 OG
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 ASP A 113 CG OD1 OD2
REMARK 470 PHE A 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 115 CG CD OE1 OE2
REMARK 470 THR A 116 OG1 CG2
REMARK 470 LEU A 117 CG CD1 CD2
REMARK 470 LYS A 118 CG CD CE NZ
REMARK 470 VAL A 119 CG1 CG2
REMARK 470 ASP A 120 CG OD1 OD2
REMARK 470 PHE A 121 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 122 CG CD1 CD2
REMARK 470 SER A 123 OG
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 LEU A 125 CG CD1 CD2
REMARK 470 PRO A 126 CG CD
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 MET A 128 CG SD CE
REMARK 470 LEU A 129 CG CD1 CD2
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 MET A 131 CG SD CE
REMARK 470 PHE A 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 133 CG CD OE1 OE2
REMARK 470 ASP A 134 CG OD1 OD2
REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 136 CG CD1 CD2
REMARK 470 CYS A 137 SG
REMARK 470 HIS A 138 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 139 CG CD CE NZ
REMARK 470 THR A 140 OG1 CG2
REMARK 470 TYR A 141 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 ASN A 143 CG OD1 ND2
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 HIS A 146 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 147 CG1 CG2
REMARK 470 THR A 148 OG1 CG2
REMARK 470 HIS A 149 CG ND1 CD2 CE1 NE2
REMARK 470 PRO A 150 CG CD
REMARK 470 ASP A 151 CG OD1 OD2
REMARK 470 PHE A 152 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 153 CG SD CE
REMARK 470 LEU A 154 CG CD1 CD2
REMARK 470 TYR A 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 156 CG OD1 OD2
REMARK 470 LEU A 158 CG CD1 CD2
REMARK 470 ASP A 159 CG OD1 OD2
REMARK 470 VAL A 160 CG1 CG2
REMARK 470 VAL A 161 CG1 CG2
REMARK 470 LEU A 162 CG CD1 CD2
REMARK 470 TYR A 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 164 CG SD CE
REMARK 470 ASP A 165 CG OD1 OD2
REMARK 470 PRO A 166 CG CD
REMARK 470 MET A 167 CG SD CE
REMARK 470 CYS A 168 SG
REMARK 470 LEU A 169 CG CD1 CD2
REMARK 470 ASP A 170 CG OD1 OD2
REMARK 470 PHE A 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 173 CG CD
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 LEU A 175 CG CD1 CD2
REMARK 470 VAL A 176 CG1 CG2
REMARK 470 CYS A 177 SG
REMARK 470 PHE A 178 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 ARG A 181 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 182 CG1 CG2 CD1
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 ILE A 185 CG1 CG2 CD1
REMARK 470 PRO A 186 CG CD
REMARK 470 GLN A 187 CG CD OE1 NE2
REMARK 470 ILE A 188 CG1 CG2 CD1
REMARK 470 ASP A 189 CG OD1 OD2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 TYR A 191 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 192 CG CD1 CD2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 SER A 194 OG
REMARK 470 SER A 195 OG
REMARK 470 LYS A 196 CG CD CE NZ
REMARK 470 TYR A 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 198 CG1 CG2 CD1
REMARK 470 TRP A 200 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 200 CZ3 CH2
REMARK 470 PRO A 201 CG CD
REMARK 470 LEU A 202 CG CD1 CD2
REMARK 470 GLN A 203 CG CD OE1 NE2
REMARK 470 TRP A 205 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 205 CZ3 CH2
REMARK 470 GLN A 206 CG CD OE1 NE2
REMARK 470 THR A 208 OG1 CG2
REMARK 470 PHE A 209 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 213 CG OD1 OD2
REMARK 470 HIS A 214 CG ND1 CD2 CE1 NE2
REMARK 470 PRO A 215 CG CD
REMARK 470 PRO A 216 CG CD
REMARK 470 SER B 1 OG
REMARK 470 PRO B 2 CG CD
REMARK 470 ILE B 3 CG1 CG2 CD1
REMARK 470 LEU B 4 CG CD1 CD2
REMARK 470 TYR B 6 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP B 7 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 7 CZ3 CH2
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 ILE B 9 CG1 CG2 CD1
REMARK 470 LYS B 10 CG CD CE NZ
REMARK 470 LEU B 12 CG CD1 CD2
REMARK 470 VAL B 13 CG1 CG2
REMARK 470 GLN B 14 CG CD OE1 NE2
REMARK 470 PRO B 15 CG CD
REMARK 470 THR B 16 OG1 CG2
REMARK 470 ARG B 17 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 18 CG CD1 CD2
REMARK 470 LEU B 19 CG CD1 CD2
REMARK 470 LEU B 20 CG CD1 CD2
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 TYR B 22 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 23 CG CD1 CD2
REMARK 470 GLU B 24 CG CD OE1 OE2
REMARK 470 GLU B 25 CG CD OE1 OE2
REMARK 470 LYS B 26 CG CD CE NZ
REMARK 470 TYR B 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 28 CG CD OE1 OE2
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 HIS B 30 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 31 CG CD1 CD2
REMARK 470 TYR B 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 33 CG CD OE1 OE2
REMARK 470 ARG B 34 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 35 CG OD1 OD2
REMARK 470 GLU B 36 CG CD OE1 OE2
REMARK 470 ASP B 38 CG OD1 OD2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 TRP B 40 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 40 CZ3 CH2
REMARK 470 ARG B 41 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 42 CG OD1 ND2
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 PHE B 45 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 46 CG CD OE1 OE2
REMARK 470 LEU B 47 CG CD1 CD2
REMARK 470 LEU B 49 CG CD1 CD2
REMARK 470 GLU B 50 CG CD OE1 OE2
REMARK 470 PHE B 51 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO B 52 CG CD
REMARK 470 ASN B 53 CG OD1 ND2
REMARK 470 LEU B 54 CG CD1 CD2
REMARK 470 PRO B 55 CG CD
REMARK 470 TYR B 56 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 57 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 58 CG1 CG2 CD1
REMARK 470 ASP B 59 CG OD1 OD2
REMARK 470 ASP B 61 CG OD1 OD2
REMARK 470 VAL B 62 CG1 CG2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 LEU B 64 CG CD1 CD2
REMARK 470 THR B 65 OG1 CG2
REMARK 470 GLN B 66 CG CD OE1 NE2
REMARK 470 SER B 67 OG
REMARK 470 MET B 68 CG SD CE
REMARK 470 ILE B 70 CG1 CG2 CD1
REMARK 470 ILE B 71 CG1 CG2 CD1
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 73 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 74 CG1 CG2 CD1
REMARK 470 ASP B 76 CG OD1 OD2
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 HIS B 78 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 79 CG OD1 ND2
REMARK 470 MET B 80 CG SD CE
REMARK 470 LEU B 81 CG CD1 CD2
REMARK 470 CYS B 84 SG
REMARK 470 PRO B 85 CG CD
REMARK 470 LYS B 86 CG CD CE NZ
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 90 CG CD OE1 OE2
REMARK 470 ILE B 91 CG1 CG2 CD1
REMARK 470 SER B 92 OG
REMARK 470 MET B 93 CG SD CE
REMARK 470 LEU B 94 CG CD1 CD2
REMARK 470 GLU B 95 CG CD OE1 OE2
REMARK 470 VAL B 98 CG1 CG2
REMARK 470 LEU B 99 CG CD1 CD2
REMARK 470 ASP B 100 CG OD1 OD2
REMARK 470 ILE B 101 CG1 CG2 CD1
REMARK 470 ARG B 102 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 103 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL B 105 CG1 CG2
REMARK 470 SER B 106 OG
REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 108 CG1 CG2 CD1
REMARK 470 TYR B 110 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 111 OG
REMARK 470 LYS B 112 CG CD CE NZ
REMARK 470 ASP B 113 CG OD1 OD2
REMARK 470 PHE B 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 THR B 116 OG1 CG2
REMARK 470 LEU B 117 CG CD1 CD2
REMARK 470 LYS B 118 CG CD CE NZ
REMARK 470 VAL B 119 CG1 CG2
REMARK 470 ASP B 120 CG OD1 OD2
REMARK 470 PHE B 121 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 122 CG CD1 CD2
REMARK 470 SER B 123 OG
REMARK 470 LYS B 124 CG CD CE NZ
REMARK 470 LEU B 125 CG CD1 CD2
REMARK 470 PRO B 126 CG CD
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 MET B 128 CG SD CE
REMARK 470 LEU B 129 CG CD1 CD2
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 MET B 131 CG SD CE
REMARK 470 PHE B 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 133 CG CD OE1 OE2
REMARK 470 ASP B 134 CG OD1 OD2
REMARK 470 ARG B 135 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 136 CG CD1 CD2
REMARK 470 CYS B 137 SG
REMARK 470 HIS B 138 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 139 CG CD CE NZ
REMARK 470 THR B 140 OG1 CG2
REMARK 470 TYR B 141 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 142 CG CD1 CD2
REMARK 470 ASN B 143 CG OD1 ND2
REMARK 470 ASP B 145 CG OD1 OD2
REMARK 470 HIS B 146 CG ND1 CD2 CE1 NE2
REMARK 470 VAL B 147 CG1 CG2
REMARK 470 THR B 148 OG1 CG2
REMARK 470 HIS B 149 CG ND1 CD2 CE1 NE2
REMARK 470 PRO B 150 CG CD
REMARK 470 ASP B 151 CG OD1 OD2
REMARK 470 PHE B 152 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 153 CG SD CE
REMARK 470 LEU B 154 CG CD1 CD2
REMARK 470 TYR B 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 156 CG OD1 OD2
REMARK 470 LEU B 158 CG CD1 CD2
REMARK 470 ASP B 159 CG OD1 OD2
REMARK 470 VAL B 160 CG1 CG2
REMARK 470 VAL B 161 CG1 CG2
REMARK 470 LEU B 162 CG CD1 CD2
REMARK 470 TYR B 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET B 164 CG SD CE
REMARK 470 ASP B 165 CG OD1 OD2
REMARK 470 PRO B 166 CG CD
REMARK 470 MET B 167 CG SD CE
REMARK 470 CYS B 168 SG
REMARK 470 LEU B 169 CG CD1 CD2
REMARK 470 ASP B 170 CG OD1 OD2
REMARK 470 PHE B 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO B 173 CG CD
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 LEU B 175 CG CD1 CD2
REMARK 470 VAL B 176 CG1 CG2
REMARK 470 CYS B 177 SG
REMARK 470 PHE B 178 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 LYS B 180 CG CD CE NZ
REMARK 470 ARG B 181 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 182 CG1 CG2 CD1
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 ILE B 185 CG1 CG2 CD1
REMARK 470 PRO B 186 CG CD
REMARK 470 GLN B 187 CG CD OE1 NE2
REMARK 470 ILE B 188 CG1 CG2 CD1
REMARK 470 ASP B 189 CG OD1 OD2
REMARK 470 LYS B 190 CG CD CE NZ
REMARK 470 TYR B 191 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 192 CG CD1 CD2
REMARK 470 LYS B 193 CG CD CE NZ
REMARK 470 SER B 194 OG
REMARK 470 SER B 195 OG
REMARK 470 LYS B 196 CG CD CE NZ
REMARK 470 TYR B 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 198 CG1 CG2 CD1
REMARK 470 TRP B 200 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 200 CZ3 CH2
REMARK 470 PRO B 201 CG CD
REMARK 470 LEU B 202 CG CD1 CD2
REMARK 470 GLN B 203 CG CD OE1 NE2
REMARK 470 TRP B 205 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 205 CZ3 CH2
REMARK 470 GLN B 206 CG CD OE1 NE2
REMARK 470 THR B 208 OG1 CG2
REMARK 470 PHE B 209 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 213 CG OD1 OD2
REMARK 470 HIS B 214 CG ND1 CD2 CE1 NE2
REMARK 470 PRO B 215 CG CD
REMARK 470 PRO B 216 CG CD
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 PRO A 216 CE1 PHE A 1365 2.05
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 TRP B3306 CE3 TRP B3306 CZ3 -0.106
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 A1741 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 LEU A2012 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 PRO A2028 C - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO B2028 C - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 24 12.62 45.47
REMARK 500 ASN A 53 -172.49 179.99
REMARK 500 ASP A 59 -100.02 -132.69
REMARK 500 GLN A 66 106.03 88.55
REMARK 500 ASN A 79 75.30 45.61
REMARK 500 GLU A 115 -9.04 -52.55
REMARK 500 THR A 148 -162.00 -119.07
REMARK 500 PHE A 178 -36.76 -38.59
REMARK 500 ASP A1494 2.98 82.42
REMARK 500 GLU A1498 -18.52 -49.72
REMARK 500 PRO A1535 2.68 -61.73
REMARK 500 HIS A1555 -55.03 70.81
REMARK 500 PHE A1566 -51.36 -124.84
REMARK 500 GLU A1576 -67.38 76.98
REMARK 500 ASP A1739 -37.73 -156.30
REMARK 500 ASP A1742 48.87 75.17
REMARK 500 LEU A1744 -10.00 -48.62
REMARK 500 SER A1752 25.69 49.35
REMARK 500 LYS A1876 124.74 -39.77
REMARK 500 GLU A1940 -123.74 54.35
REMARK 500 PHE A1987 -93.19 -122.89
REMARK 500 LEU A2123 67.31 28.59
REMARK 500 MET A2166 13.58 -141.44
REMARK 500 TYR A2298 30.76 -95.08
REMARK 500 SER A2357 125.35 -39.10
REMARK 500 LYS A2411 2.98 83.82
REMARK 500 LEU A2471 -133.61 55.17
REMARK 500 GLN A2513 -24.67 103.89
REMARK 500 SER A2563 -52.67 65.54
REMARK 500 GLU A2727 -161.06 -100.38
REMARK 500 ALA A2761 -128.88 61.84
REMARK 500 ARG A2763 -3.28 76.65
REMARK 500 PRO A2784 119.94 -38.28
REMARK 500 HIS A2789 40.74 -106.43
REMARK 500 ILE A2936 79.52 -116.71
REMARK 500 ARG A3305 9.29 -64.62
REMARK 500 THR A3332 -64.61 -92.04
REMARK 500 ILE A3462 -18.39 -48.97
REMARK 500 ASP A3483 -72.19 -142.49
REMARK 500 GLU A3809 -135.35 44.22
REMARK 500 SER A3818 -159.75 -115.90
REMARK 500 PRO A3981 -6.92 -56.30
REMARK 500 PHE A4015 -65.51 -90.70
REMARK 500 ASP A4019 -50.78 69.94
REMARK 500 GLN A4064 -1.18 -58.90
REMARK 500 GLU B 24 15.67 44.44
REMARK 500 GLU B 46 41.64 -105.56
REMARK 500 ASN B 53 175.26 176.96
REMARK 500 ASP B 59 -107.11 -139.04
REMARK 500 GLN B 66 112.15 90.48
REMARK 500
REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS.
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 LEU B 2119 LYS B 2120 -148.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B2620 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A5097 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A2081 OG1
REMARK 620 2 GLU A2195 OE2 70.0
REMARK 620 3 ATP A5093 O3G 122.7 61.3
REMARK 620 4 ATP A5093 O1B 76.9 77.2 64.9
REMARK 620 5 ATP A5093 O2A 70.0 135.7 132.0 76.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B5097 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B2081 OG1
REMARK 620 2 GLU B2511 OE2 129.6
REMARK 620 3 ATP B5093 O2A 71.3 94.4
REMARK 620 4 ATP B5093 O1B 63.0 157.1 70.5
REMARK 620 5 ATP B5093 O3G 119.3 106.4 131.9 74.5
REMARK 620 N 1 2 3 4
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 5093
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 5094
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 5093
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 5094
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5095
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5096
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5095
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5096
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 5097
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 5097
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B8X RELATED DB: PDB
REMARK 900 GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING
REMARK 900 SIGNAL OF THE TRANSCRIPTION FACTOR AML-1
REMARK 900 RELATED ID: 1DUG RELATED DB: PDB
REMARK 900 STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING ANDFACTOR
REMARK 900 XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIERPROTEIN DRIVEN
REMARK 900 CRYSTALLIZATION
REMARK 900 RELATED ID: 1GNE RELATED DB: PDB
REMARK 900 GLUTATHIONE S-TRANSFERASE FUSED WITH A CONSERVED NEUTRALIZING
REMARK 900 EPITOPE ON GP41 OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1, COMPLEXED
REMARK 900 WITH GLUTATHIONE
REMARK 900 RELATED ID: 1GTA RELATED DB: PDB
REMARK 900 GLUTATHIONE S-TRANSFERASE (26 KDA)
REMARK 900 RELATED ID: 1GTB RELATED DB: PDB
REMARK 900 RELATED ID: 1M99 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S- TRANSFERASEFROM
REMARK 900 SCHISTOSOMA JAPONICUM COMPLEXED WITH GLUTATHIONESULFONIC ACID
REMARK 900 RELATED ID: 1M9A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S- TRANSFERASEFROM
REMARK 900 SCHISTOSOMA JAPONICUM COMPLEXED WITH S- HEXYLGLUTATHIONE
REMARK 900 RELATED ID: 1M9B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S- TRANSFERASEFROM
REMARK 900 SCHISTOSOMA JAPONICUM COMPLEXED WITH GAMMA- GLUTAMYL[S-(2-
REMARK 900 IODOBENZYL)CYSTEINYL]GLYCINE
REMARK 900 RELATED ID: 1U87 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S- TRANSFERASEY7F
REMARK 900 MUTANT FROM SCHISTOSOMA JAPONICUM COMPLEXED WITHGLUTATHIONE
REMARK 900 RELATED ID: 1U88 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S- TRANSFERASEY7F
REMARK 900 MUTANT FROM SCHISTOSOMA JAPONICUM COMPLEXED WITH S-OCTYL GLUTATHIONE
REMARK 900 RELATED ID: 1UA5 RELATED DB: PDB
REMARK 900 NON-FUSION GST FROM S. JAPONICUM IN COMPLEX WITH GLUTATHIONE
REMARK 900 RELATED ID: 1Y6E RELATED DB: PDB
REMARK 900 ORTHORHOMBIC GLUTATHIONE S-TRANSFERASE OF SCHISTOSOMAJAPONICUM
REMARK 900 RELATED ID: 4AI6 RELATED DB: PDB
REMARK 900 DYNEIN MOTOR DOMAIN - ADP COMPLEX RELATED ENTRIES
REMARK 900 RELATED ID: 4AKG RELATED DB: PDB
REMARK 900 DYNEIN MOTOR DOMAIN - ATP COMPLEX
REMARK 900 RELATED ID: 4AKI RELATED DB: PDB
REMARK 900 DYNEIN MOTOR DOMAIN - LUAC DERIVATIVE
DBREF 4AKH A 1 217 UNP P08515 GST26_SCHJA 2 218
DBREF 4AKH A 1364 3038 UNP P36022 DYHC_YEAST 1364 3038
DBREF 4AKH A 3292 4092 UNP P36022 DYHC_YEAST 3292 4092
DBREF 4AKH B 1 217 UNP P08515 GST26_SCHJA 2 218
DBREF 4AKH B 1364 3038 UNP P36022 DYHC_YEAST 1364 3038
DBREF 4AKH B 3292 4092 UNP P36022 DYHC_YEAST 3292 4092
SEQADV 4AKH SER A 218 UNP P36022 LINKER
SEQADV 4AKH ASP A 219 UNP P36022 LINKER
SEQADV 4AKH ILE A 1630 UNP P36022 LEU 1630 CONFLICT
SEQADV 4AKH ASP A 3782 UNP P36022 GLU 3782 CONFLICT
SEQADV 4AKH SER B 218 UNP P36022 LINKER
SEQADV 4AKH ASP B 219 UNP P36022 LINKER
SEQADV 4AKH ILE B 1630 UNP P36022 LEU 1630 CONFLICT
SEQADV 4AKH ASP B 3782 UNP P36022 GLU 3782 CONFLICT
SEQRES 1 A 2695 SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES 2 A 2695 GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES 3 A 2695 TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES 4 A 2695 TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES 5 A 2695 ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES 6 A 2695 GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES 7 A 2695 ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES 8 A 2695 SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES 9 A 2695 VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES 10 A 2695 LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES 11 A 2695 MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES 12 A 2695 GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES 13 A 2695 ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES 14 A 2695 ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES 15 A 2695 GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES 16 A 2695 LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES 17 A 2695 PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP GLU PHE
SEQRES 18 A 2695 VAL ILE GLU LYS SER LEU ASN ARG ILE LYS LYS PHE TRP
SEQRES 19 A 2695 LYS GLU ALA GLN TYR GLU VAL ILE GLU HIS SER SER GLY
SEQRES 20 A 2695 LEU LYS LEU VAL ARG GLU TRP ASP VAL LEU GLU GLN ALA
SEQRES 21 A 2695 CYS LYS GLU ASP LEU GLU GLU LEU VAL SER MET LYS ALA
SEQRES 22 A 2695 SER ASN TYR TYR LYS ILE PHE GLU GLN ASP CYS LEU ASP
SEQRES 23 A 2695 LEU GLU SER LYS LEU THR LYS LEU SER GLU ILE GLN VAL
SEQRES 24 A 2695 ASN TRP VAL GLU VAL GLN PHE TYR TRP LEU ASP LEU TYR
SEQRES 25 A 2695 GLY ILE LEU GLY GLU ASN LEU ASP ILE GLN ASN PHE LEU
SEQRES 26 A 2695 PRO LEU GLU THR SER LYS PHE LYS SER LEU THR SER GLU
SEQRES 27 A 2695 TYR LYS MET ILE THR THR ARG ALA PHE GLN LEU ASP THR
SEQRES 28 A 2695 THR ILE GLU VAL ILE HIS ILE PRO ASN PHE ASP THR THR
SEQRES 29 A 2695 LEU LYS LEU THR ILE ASP SER LEU LYS MET ILE LYS SER
SEQRES 30 A 2695 SER LEU SER THR PHE LEU GLU ARG GLN ARG ARG GLN PHE
SEQRES 31 A 2695 PRO ARG PHE TYR PHE LEU GLY ASN ASP ASP LEU LEU LYS
SEQRES 32 A 2695 ILE ILE GLY SER GLY LYS HIS HIS ASP GLN VAL SER LYS
SEQRES 33 A 2695 PHE MET LYS LYS MET PHE GLY SER ILE GLU SER ILE ILE
SEQRES 34 A 2695 PHE LEU GLU ASP PHE ILE THR GLY VAL ARG SER VAL GLU
SEQRES 35 A 2695 GLY GLU VAL LEU ASN LEU ASN GLU LYS ILE GLU LEU LYS
SEQRES 36 A 2695 ASP SER ILE GLN ALA GLN GLU TRP LEU ASN ILE LEU ASP
SEQRES 37 A 2695 THR GLU ILE LYS LEU SER VAL PHE THR GLN PHE ARG ASP
SEQRES 38 A 2695 CYS LEU GLY GLN ILE LYS ASP GLY THR ASP ILE GLU VAL
SEQRES 39 A 2695 VAL VAL SER LYS TYR ILE PHE GLN ALA ILE LEU LEU SER
SEQRES 40 A 2695 ALA GLN VAL MET TRP THR GLU LEU VAL GLU LYS CYS LEU
SEQRES 41 A 2695 GLN THR ASN GLN PHE SER LYS TYR TRP LYS GLU VAL ASP
SEQRES 42 A 2695 MET LYS ILE LYS GLY LEU LEU ASP LYS LEU ASN LYS SER
SEQRES 43 A 2695 SER ASP ASN VAL LYS LYS LYS ILE GLU ALA LEU LEU VAL
SEQRES 44 A 2695 GLU TYR LEU HIS PHE ASN ASN VAL ILE GLY GLN LEU LYS
SEQRES 45 A 2695 ASN CYS SER THR LYS GLU GLU ALA ARG LEU LEU TRP ALA
SEQRES 46 A 2695 LYS VAL GLN LYS PHE TYR GLN LYS ASN ASP THR LEU ASP
SEQRES 47 A 2695 ASP LEU ASN SER VAL PHE ILE SER GLN SER GLY TYR LEU
SEQRES 48 A 2695 LEU GLN TYR LYS PHE GLU TYR ILE GLY ILE PRO GLU ARG
SEQRES 49 A 2695 LEU ILE TYR THR PRO LEU LEU LEU ILE GLY PHE ALA THR
SEQRES 50 A 2695 LEU THR ASP SER LEU HIS GLN LYS TYR GLY GLY CYS PHE
SEQRES 51 A 2695 PHE GLY PRO ALA GLY THR GLY LYS THR GLU THR VAL LYS
SEQRES 52 A 2695 ALA PHE GLY GLN ASN LEU GLY ARG VAL VAL VAL VAL PHE
SEQRES 53 A 2695 ASN CYS ASP ASP SER PHE ASP TYR GLN VAL LEU SER ARG
SEQRES 54 A 2695 LEU LEU VAL GLY ILE THR GLN ILE GLY ALA TRP GLY CYS
SEQRES 55 A 2695 PHE ASP GLU PHE ASN ARG LEU ASP GLU LYS VAL LEU SER
SEQRES 56 A 2695 ALA VAL SER ALA ASN ILE GLN GLN ILE GLN ASN GLY LEU
SEQRES 57 A 2695 GLN VAL GLY LYS SER HIS ILE THR LEU LEU GLU GLU GLU
SEQRES 58 A 2695 THR PRO LEU SER PRO HIS THR ALA VAL PHE ILE THR LEU
SEQRES 59 A 2695 ASN PRO GLY TYR ASN GLY ARG SER GLU LEU PRO GLU ASN
SEQRES 60 A 2695 LEU LYS LYS SER PHE ARG GLU PHE SER MET LYS SER PRO
SEQRES 61 A 2695 GLN SER GLY THR ILE ALA GLU MET ILE LEU GLN ILE MET
SEQRES 62 A 2695 GLY PHE GLU ASP SER LYS SER LEU ALA SER LYS ILE VAL
SEQRES 63 A 2695 HIS PHE LEU GLU LEU LEU SER SER LYS CYS SER SER MET
SEQRES 64 A 2695 ASN HIS TYR HIS PHE GLY LEU ARG THR LEU LYS GLY VAL
SEQRES 65 A 2695 LEU ARG ASN CYS SER PRO LEU ILE SER GLU PHE GLY GLU
SEQRES 66 A 2695 GLY GLU LYS THR VAL VAL GLU SER LEU LYS ARG VAL ILE
SEQRES 67 A 2695 LEU PRO SER LEU GLY ASP THR ASP GLU LEU VAL PHE LYS
SEQRES 68 A 2695 ASP GLU LEU SER LYS ILE PHE ASP SER ALA GLY THR PRO
SEQRES 69 A 2695 LEU ASN SER LYS ALA ILE VAL GLN CYS LEU LYS ASP ALA
SEQRES 70 A 2695 GLY GLN ARG SER GLY PHE SER MET SER GLU GLU PHE LEU
SEQRES 71 A 2695 LYS LYS CYS MET GLN PHE TYR TYR MET GLN LYS THR GLN
SEQRES 72 A 2695 GLN ALA LEU ILE LEU VAL GLY LYS ALA GLY CYS GLY LYS
SEQRES 73 A 2695 THR ALA THR TRP LYS THR VAL ILE ASP ALA MET ALA ILE
SEQRES 74 A 2695 PHE ASP GLY HIS ALA ASN VAL VAL TYR VAL ILE ASP THR
SEQRES 75 A 2695 LYS VAL LEU THR LYS GLU SER LEU TYR GLY SER MET LEU
SEQRES 76 A 2695 LYS ALA THR LEU GLU TRP ARG ASP GLY LEU PHE THR SER
SEQRES 77 A 2695 ILE LEU ARG ARG VAL ASN ASP ASP ILE THR GLY THR PHE
SEQRES 78 A 2695 LYS ASN SER ARG ILE TRP VAL VAL PHE ASP SER ASP LEU
SEQRES 79 A 2695 ASP PRO GLU TYR VAL GLU ALA MET ASN SER VAL LEU ASP
SEQRES 80 A 2695 ASP ASN LYS ILE LEU THR LEU PRO ASN GLY GLU ARG LEU
SEQRES 81 A 2695 PRO ILE PRO PRO ASN PHE ARG ILE LEU PHE GLU THR ASP
SEQRES 82 A 2695 ASN LEU ASP HIS THR THR PRO ALA THR ILE THR ARG CYS
SEQRES 83 A 2695 GLY LEU LEU TRP PHE SER THR ASP VAL CYS SER ILE SER
SEQRES 84 A 2695 SER LYS ILE ASP HIS LEU LEU ASN LYS SER TYR GLU ALA
SEQRES 85 A 2695 LEU ASP ASN LYS LEU SER MET PHE GLU LEU ASP LYS LEU
SEQRES 86 A 2695 LYS ASP LEU ILE SER ASP SER PHE ASP MET ALA SER LEU
SEQRES 87 A 2695 THR ASN ILE PHE THR CYS SER ASN ASP LEU VAL HIS ILE
SEQRES 88 A 2695 LEU GLY VAL ARG THR PHE ASN LYS LEU GLU THR ALA VAL
SEQRES 89 A 2695 GLN LEU ALA VAL HIS LEU ILE SER SER TYR ARG GLN TRP
SEQRES 90 A 2695 PHE GLN ASN LEU ASP ASP LYS SER LEU LYS ASP VAL ILE
SEQRES 91 A 2695 THR LEU LEU ILE LYS ARG SER LEU LEU TYR ALA LEU ALA
SEQRES 92 A 2695 GLY ASP SER THR GLY GLU SER GLN ARG ALA PHE ILE GLN
SEQRES 93 A 2695 THR ILE ASN THR TYR PHE GLY HIS ASP SER GLN GLU LEU
SEQRES 94 A 2695 SER ASP TYR SER THR ILE VAL ILE ALA ASN ASP LYS LEU
SEQRES 95 A 2695 SER PHE SER SER PHE CYS SER GLU ILE PRO SER VAL SER
SEQRES 96 A 2695 LEU GLU ALA HIS GLU VAL MET ARG PRO ASP ILE VAL ILE
SEQRES 97 A 2695 PRO THR ILE ASP THR ILE LYS HIS GLU LYS ILE PHE TYR
SEQRES 98 A 2695 ASP LEU LEU ASN SER LYS ARG GLY ILE ILE LEU CYS GLY
SEQRES 99 A 2695 PRO PRO GLY SER GLY LYS THR MET ILE MET ASN ASN ALA
SEQRES 100 A 2695 LEU ARG ASN SER SER LEU TYR ASP VAL VAL GLY ILE ASN
SEQRES 101 A 2695 PHE SER LYS ASP THR THR THR GLU HIS ILE LEU SER ALA
SEQRES 102 A 2695 LEU HIS ARG HIS THR ASN TYR VAL THR THR SER LYS GLY
SEQRES 103 A 2695 LEU THR LEU LEU PRO LYS SER ASP ILE LYS ASN LEU VAL
SEQRES 104 A 2695 LEU PHE CYS ASP GLU ILE ASN LEU PRO LYS LEU ASP LYS
SEQRES 105 A 2695 TYR GLY SER GLN ASN VAL VAL LEU PHE LEU ARG GLN LEU
SEQRES 106 A 2695 MET GLU LYS GLN GLY PHE TRP LYS THR PRO GLU ASN LYS
SEQRES 107 A 2695 TRP VAL THR ILE GLU ARG ILE HIS ILE VAL GLY ALA CYS
SEQRES 108 A 2695 ASN PRO PRO THR ASP PRO GLY ARG ILE PRO MET SER GLU
SEQRES 109 A 2695 ARG PHE THR ARG HIS ALA ALA ILE LEU TYR LEU GLY TYR
SEQRES 110 A 2695 PRO SER GLY LYS SER LEU SER GLN ILE TYR GLU ILE TYR
SEQRES 111 A 2695 TYR LYS ALA ILE PHE LYS LEU VAL PRO GLU PHE ARG SER
SEQRES 112 A 2695 TYR THR GLU PRO PHE ALA ARG ALA SER VAL HIS LEU TYR
SEQRES 113 A 2695 ASN GLU CYS LYS ALA ARG TYR SER THR GLY LEU GLN SER
SEQRES 114 A 2695 HIS TYR LEU PHE SER PRO ARG GLU LEU THR ARG LEU VAL
SEQRES 115 A 2695 ARG GLY VAL TYR THR ALA ILE ASN THR GLY PRO ARG GLN
SEQRES 116 A 2695 THR LEU ARG SER LEU ILE ARG LEU TRP ALA TYR GLU ALA
SEQRES 117 A 2695 TRP ARG ILE PHE ALA ASP ARG LEU VAL GLY VAL LYS GLU
SEQRES 118 A 2695 LYS ASN SER PHE GLU GLN LEU LEU TYR GLU THR VAL ASP
SEQRES 119 A 2695 LYS TYR LEU PRO ASN GLN ASP LEU GLY ASN ILE SER SER
SEQRES 120 A 2695 THR SER LEU LEU PHE SER GLY LEU LEU SER LEU ASP PHE
SEQRES 121 A 2695 LYS GLU VAL ASN LYS THR ASP LEU VAL ASN PHE ILE GLU
SEQRES 122 A 2695 GLU ARG PHE LYS THR PHE CYS ASP GLU GLU LEU GLU VAL
SEQRES 123 A 2695 PRO MET VAL ILE HIS GLU SER MET VAL ASP HIS ILE LEU
SEQRES 124 A 2695 ARG ILE ASP ARG ALA LEU LYS GLN VAL GLN GLY HIS MET
SEQRES 125 A 2695 MET LEU ILE GLY ALA SER ARG THR GLY LYS THR ILE LEU
SEQRES 126 A 2695 THR ARG PHE VAL ALA TRP LEU ASN GLY LEU LYS ILE VAL
SEQRES 127 A 2695 GLN PRO LYS ILE HIS ARG HIS SER ASN LEU SER ASP PHE
SEQRES 128 A 2695 ASP MET ILE LEU LYS LYS ALA ILE SER ASP CYS SER LEU
SEQRES 129 A 2695 LYS GLU SER ARG THR CYS LEU ILE ILE ASP GLU SER ASN
SEQRES 130 A 2695 ILE LEU GLU THR ALA PHE LEU GLU ARG MET ASN THR LEU
SEQRES 131 A 2695 LEU ALA ASN ALA ASP ILE PRO ASP LEU PHE GLN GLY GLU
SEQRES 132 A 2695 GLU TYR ASP LYS LEU LEU ASN ASN LEU ARG ASN LYS THR
SEQRES 133 A 2695 ARG SER LEU GLY LEU LEU LEU ASP THR GLU GLN GLU LEU
SEQRES 134 A 2695 TYR ASP TRP PHE VAL GLY GLU ILE ALA LYS ASN LEU HIS
SEQRES 135 A 2695 VAL VAL PHE THR ILE CYS ASP PRO THR ASN ASN LYS SER
SEQRES 136 A 2695 SER ALA MET ILE SER SER PRO ALA LEU PHE ASN ARG CYS
SEQRES 137 A 2695 ILE ILE ASN TRP MET GLY ASP TRP ASP THR LYS THR MET
SEQRES 138 A 2695 SER GLN VAL ALA ASN ASN MET VAL ASP VAL ILE PRO MET
SEQRES 139 A 2695 GLU PHE THR ASP PHE ILE VAL PRO GLU VAL ASN LYS GLU
SEQRES 140 A 2695 LEU VAL PHE THR GLU PRO ILE GLN THR ILE ARG ASP ALA
SEQRES 141 A 2695 VAL VAL ASN ILE LEU ILE HIS PHE ASP ARG ASN PHE TYR
SEQRES 142 A 2695 GLN LYS MET LYS VAL GLY VAL ASN PRO ARG SER PRO GLY
SEQRES 143 A 2695 TYR PHE ILE ASP GLY LEU ARG ALA LEU VAL LYS LEU VAL
SEQRES 144 A 2695 THR ALA LYS TYR GLN ASP LEU GLN GLU ASN GLN ARG PHE
SEQRES 145 A 2695 VAL ASN VAL GLY LEU GLU LYS LEU ASN GLU SER VAL LEU
SEQRES 146 A 2695 LYS VAL ASN GLU LEU ASN LYS THR LEU SER ILE SER LEU
SEQRES 147 A 2695 VAL LYS SER LEU THR PHE GLU LYS GLU ARG TRP LEU ASN
SEQRES 148 A 2695 THR THR LYS GLN PHE SER LYS THR SER GLN GLU LEU ILE
SEQRES 149 A 2695 GLY ASN CYS ILE ILE SER SER ILE TYR GLU THR TYR PHE
SEQRES 150 A 2695 GLY HIS LEU ASN GLU ARG GLU ARG ALA ASP MET LEU VAL
SEQRES 151 A 2695 ILE LEU LYS ARG LEU LEU GLY LYS PHE ALA VAL LYS TYR
SEQRES 152 A 2695 ASP VAL ASN TYR ARG PHE ILE ASP TYR LEU VAL THR LEU
SEQRES 153 A 2695 ASP GLU LYS MET LYS TRP LEU GLU CYS GLY LEU ASP LYS
SEQRES 154 A 2695 ASN ASP TYR PHE LEU GLU ASN MET SER ILE VAL MET ASN
SEQRES 155 A 2695 SER GLN ASP ALA VAL PRO PHE LEU LEU ASP PRO SER SER
SEQRES 156 A 2695 HIS MET ILE THR VAL ILE SER ASN TYR TYR GLY ASN LYS
SEQRES 157 A 2695 THR VAL LEU LEU SER PHE LEU GLU GLU GLY PHE VAL LYS
SEQRES 158 A 2695 ARG LEU GLU ASN ALA ILE ARG PHE GLY SER VAL VAL ILE
SEQRES 159 A 2695 ILE GLN ASP GLY GLU PHE PHE ASP PRO ILE ILE SER ARG
SEQRES 160 A 2695 LEU ILE SER ARG GLU PHE ASN HIS ALA GLY ASN ARG VAL
SEQRES 161 A 2695 THR VAL GLU ILE GLY ASP HIS GLU VAL ASP VAL SER GLY
SEQRES 162 A 2695 ASP PHE LYS LEU PHE ILE HIS SER CYS ASP PRO SER GLY
SEQRES 163 A 2695 ASP ILE PRO ILE PHE LEU ARG SER ARG VAL ARG LEU VAL
SEQRES 164 A 2695 HIS PHE VAL THR ASN LYS GLU SER ILE GLU THR ARG ILE
SEQRES 165 A 2695 PHE ASP ILE THR LEU THR GLU GLU ASN ALA GLU MET GLN
SEQRES 166 A 2695 ARG LYS ARG GLU ASP LEU ILE LYS LEU ASN THR GLU TYR
SEQRES 167 A 2695 LYS LEU LYS LEU LYS ASN LEU GLU LYS ARG LEU LEU GLU
SEQRES 168 A 2695 GLU LEU ASN ASN SER GLN GLY ASN MET LEU GLU ASN ASP
SEQRES 169 A 2695 GLU LEU MET VAL THR LEU ASN ASN LEU LYS LYS GLU ALA
SEQRES 170 A 2695 MET ASN ILE GLU LYS LYS LEU SER GLU SER GLU GLU PHE
SEQRES 171 A 2695 PHE PRO GLN PHE ASP ASN LEU VAL GLU GLU TYR SER ILE
SEQRES 172 A 2695 ILE GLY LYS HIS SER VAL LYS ILE PHE SER MET LEU GLU
SEQRES 173 A 2695 LYS PHE GLY GLN PHE HIS TRP PHE TYR GLY ILE SER ILE
SEQRES 174 A 2695 GLY GLN PHE LEU SER CYS PHE LYS ARG VAL PHE ILE LYS
SEQRES 175 A 2695 LYS SER ARG GLU THR ARG ALA ALA ARG THR ARG VAL ASP
SEQRES 176 A 2695 GLU ILE LEU TRP LEU LEU TYR GLN GLU VAL TYR CYS GLN
SEQRES 177 A 2695 PHE SER THR ALA LEU ASP LYS LYS PHE LYS MET ILE MET
SEQRES 178 A 2695 ALA MET THR MET PHE CYS LEU TYR LYS PHE ASP ILE GLU
SEQRES 179 A 2695 SER GLU GLN TYR LYS GLU ALA VAL LEU THR MET ILE GLY
SEQRES 180 A 2695 VAL LEU SER GLU SER SER ASP GLY VAL PRO LYS LEU THR
SEQRES 181 A 2695 VAL ASP THR ASN ASN ASP LEU ARG TYR LEU TRP ASP TYR
SEQRES 182 A 2695 VAL THR THR LYS SER TYR ILE SER ALA LEU ASN TRP PHE
SEQRES 183 A 2695 LYS ASN GLU PHE PHE VAL ASP GLU TRP ASN ILE ALA ASP
SEQRES 184 A 2695 VAL VAL ALA ASN SER ASP ASN ASN TYR PHE THR MET ALA
SEQRES 185 A 2695 SER GLU ARG ASP VAL ASP GLY THR PHE LYS LEU ILE GLU
SEQRES 186 A 2695 LEU ALA LYS ALA SER LYS GLU SER LEU LYS ILE ILE PRO
SEQRES 187 A 2695 LEU GLY SER ILE GLU ASN LEU ASN TYR ALA GLN GLU GLU
SEQRES 188 A 2695 ILE SER LYS SER LYS ILE GLU GLY GLY TRP ILE LEU LEU
SEQRES 189 A 2695 GLN ASN ILE GLN MET SER LEU SER TRP VAL LYS THR TYR
SEQRES 190 A 2695 LEU HIS LYS HIS VAL GLU GLU THR LYS ALA ALA GLU GLU
SEQRES 191 A 2695 HIS GLU LYS PHE LYS MET PHE MET THR CYS HIS LEU THR
SEQRES 192 A 2695 GLY ASP LYS LEU PRO ALA PRO LEU LEU GLN ARG THR ASP
SEQRES 193 A 2695 ARG PHE VAL TYR GLU ASP ILE PRO GLY ILE LEU ASP THR
SEQRES 194 A 2695 VAL LYS ASP LEU TRP GLY SER GLN PHE PHE THR GLY LYS
SEQRES 195 A 2695 ILE SER GLY VAL TRP SER VAL TYR CYS THR PHE LEU LEU
SEQRES 196 A 2695 SER TRP PHE HIS ALA LEU ILE THR ALA ARG THR ARG LEU
SEQRES 197 A 2695 VAL PRO HIS GLY PHE SER LYS LYS TYR TYR PHE ASN ASP
SEQRES 198 A 2695 CYS ASP PHE GLN PHE ALA SER VAL TYR LEU GLU ASN VAL
SEQRES 199 A 2695 LEU ALA THR ASN SER THR ASN ASN ILE PRO TRP ALA GLN
SEQRES 200 A 2695 VAL ARG ASP HIS ILE ALA THR ILE VAL TYR GLY GLY LYS
SEQRES 201 A 2695 ILE ASP GLU GLU LYS ASP LEU GLU VAL VAL ALA LYS LEU
SEQRES 202 A 2695 CYS ALA HIS VAL PHE CYS GLY SER ASP ASN LEU GLN ILE
SEQRES 203 A 2695 VAL PRO GLY VAL ARG ILE PRO GLN PRO LEU LEU GLN GLN
SEQRES 204 A 2695 SER GLU GLU GLU GLU ARG ALA ARG LEU THR ALA ILE LEU
SEQRES 205 A 2695 SER ASN THR ILE GLU PRO ALA ASP SER LEU SER SER TRP
SEQRES 206 A 2695 LEU GLN LEU PRO ARG GLU SER ILE LEU ASN TYR GLU ARG
SEQRES 207 A 2695 LEU GLN ALA LYS GLU VAL ALA SER SER THR GLU GLN LEU
SEQRES 208 A 2695 LEU GLN GLU MET
SEQRES 1 B 2695 SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES 2 B 2695 GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES 3 B 2695 TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES 4 B 2695 TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES 5 B 2695 ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES 6 B 2695 GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES 7 B 2695 ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES 8 B 2695 SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES 9 B 2695 VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES 10 B 2695 LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES 11 B 2695 MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES 12 B 2695 GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES 13 B 2695 ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES 14 B 2695 ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES 15 B 2695 GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES 16 B 2695 LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES 17 B 2695 PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP GLU PHE
SEQRES 18 B 2695 VAL ILE GLU LYS SER LEU ASN ARG ILE LYS LYS PHE TRP
SEQRES 19 B 2695 LYS GLU ALA GLN TYR GLU VAL ILE GLU HIS SER SER GLY
SEQRES 20 B 2695 LEU LYS LEU VAL ARG GLU TRP ASP VAL LEU GLU GLN ALA
SEQRES 21 B 2695 CYS LYS GLU ASP LEU GLU GLU LEU VAL SER MET LYS ALA
SEQRES 22 B 2695 SER ASN TYR TYR LYS ILE PHE GLU GLN ASP CYS LEU ASP
SEQRES 23 B 2695 LEU GLU SER LYS LEU THR LYS LEU SER GLU ILE GLN VAL
SEQRES 24 B 2695 ASN TRP VAL GLU VAL GLN PHE TYR TRP LEU ASP LEU TYR
SEQRES 25 B 2695 GLY ILE LEU GLY GLU ASN LEU ASP ILE GLN ASN PHE LEU
SEQRES 26 B 2695 PRO LEU GLU THR SER LYS PHE LYS SER LEU THR SER GLU
SEQRES 27 B 2695 TYR LYS MET ILE THR THR ARG ALA PHE GLN LEU ASP THR
SEQRES 28 B 2695 THR ILE GLU VAL ILE HIS ILE PRO ASN PHE ASP THR THR
SEQRES 29 B 2695 LEU LYS LEU THR ILE ASP SER LEU LYS MET ILE LYS SER
SEQRES 30 B 2695 SER LEU SER THR PHE LEU GLU ARG GLN ARG ARG GLN PHE
SEQRES 31 B 2695 PRO ARG PHE TYR PHE LEU GLY ASN ASP ASP LEU LEU LYS
SEQRES 32 B 2695 ILE ILE GLY SER GLY LYS HIS HIS ASP GLN VAL SER LYS
SEQRES 33 B 2695 PHE MET LYS LYS MET PHE GLY SER ILE GLU SER ILE ILE
SEQRES 34 B 2695 PHE LEU GLU ASP PHE ILE THR GLY VAL ARG SER VAL GLU
SEQRES 35 B 2695 GLY GLU VAL LEU ASN LEU ASN GLU LYS ILE GLU LEU LYS
SEQRES 36 B 2695 ASP SER ILE GLN ALA GLN GLU TRP LEU ASN ILE LEU ASP
SEQRES 37 B 2695 THR GLU ILE LYS LEU SER VAL PHE THR GLN PHE ARG ASP
SEQRES 38 B 2695 CYS LEU GLY GLN ILE LYS ASP GLY THR ASP ILE GLU VAL
SEQRES 39 B 2695 VAL VAL SER LYS TYR ILE PHE GLN ALA ILE LEU LEU SER
SEQRES 40 B 2695 ALA GLN VAL MET TRP THR GLU LEU VAL GLU LYS CYS LEU
SEQRES 41 B 2695 GLN THR ASN GLN PHE SER LYS TYR TRP LYS GLU VAL ASP
SEQRES 42 B 2695 MET LYS ILE LYS GLY LEU LEU ASP LYS LEU ASN LYS SER
SEQRES 43 B 2695 SER ASP ASN VAL LYS LYS LYS ILE GLU ALA LEU LEU VAL
SEQRES 44 B 2695 GLU TYR LEU HIS PHE ASN ASN VAL ILE GLY GLN LEU LYS
SEQRES 45 B 2695 ASN CYS SER THR LYS GLU GLU ALA ARG LEU LEU TRP ALA
SEQRES 46 B 2695 LYS VAL GLN LYS PHE TYR GLN LYS ASN ASP THR LEU ASP
SEQRES 47 B 2695 ASP LEU ASN SER VAL PHE ILE SER GLN SER GLY TYR LEU
SEQRES 48 B 2695 LEU GLN TYR LYS PHE GLU TYR ILE GLY ILE PRO GLU ARG
SEQRES 49 B 2695 LEU ILE TYR THR PRO LEU LEU LEU ILE GLY PHE ALA THR
SEQRES 50 B 2695 LEU THR ASP SER LEU HIS GLN LYS TYR GLY GLY CYS PHE
SEQRES 51 B 2695 PHE GLY PRO ALA GLY THR GLY LYS THR GLU THR VAL LYS
SEQRES 52 B 2695 ALA PHE GLY GLN ASN LEU GLY ARG VAL VAL VAL VAL PHE
SEQRES 53 B 2695 ASN CYS ASP ASP SER PHE ASP TYR GLN VAL LEU SER ARG
SEQRES 54 B 2695 LEU LEU VAL GLY ILE THR GLN ILE GLY ALA TRP GLY CYS
SEQRES 55 B 2695 PHE ASP GLU PHE ASN ARG LEU ASP GLU LYS VAL LEU SER
SEQRES 56 B 2695 ALA VAL SER ALA ASN ILE GLN GLN ILE GLN ASN GLY LEU
SEQRES 57 B 2695 GLN VAL GLY LYS SER HIS ILE THR LEU LEU GLU GLU GLU
SEQRES 58 B 2695 THR PRO LEU SER PRO HIS THR ALA VAL PHE ILE THR LEU
SEQRES 59 B 2695 ASN PRO GLY TYR ASN GLY ARG SER GLU LEU PRO GLU ASN
SEQRES 60 B 2695 LEU LYS LYS SER PHE ARG GLU PHE SER MET LYS SER PRO
SEQRES 61 B 2695 GLN SER GLY THR ILE ALA GLU MET ILE LEU GLN ILE MET
SEQRES 62 B 2695 GLY PHE GLU ASP SER LYS SER LEU ALA SER LYS ILE VAL
SEQRES 63 B 2695 HIS PHE LEU GLU LEU LEU SER SER LYS CYS SER SER MET
SEQRES 64 B 2695 ASN HIS TYR HIS PHE GLY LEU ARG THR LEU LYS GLY VAL
SEQRES 65 B 2695 LEU ARG ASN CYS SER PRO LEU ILE SER GLU PHE GLY GLU
SEQRES 66 B 2695 GLY GLU LYS THR VAL VAL GLU SER LEU LYS ARG VAL ILE
SEQRES 67 B 2695 LEU PRO SER LEU GLY ASP THR ASP GLU LEU VAL PHE LYS
SEQRES 68 B 2695 ASP GLU LEU SER LYS ILE PHE ASP SER ALA GLY THR PRO
SEQRES 69 B 2695 LEU ASN SER LYS ALA ILE VAL GLN CYS LEU LYS ASP ALA
SEQRES 70 B 2695 GLY GLN ARG SER GLY PHE SER MET SER GLU GLU PHE LEU
SEQRES 71 B 2695 LYS LYS CYS MET GLN PHE TYR TYR MET GLN LYS THR GLN
SEQRES 72 B 2695 GLN ALA LEU ILE LEU VAL GLY LYS ALA GLY CYS GLY LYS
SEQRES 73 B 2695 THR ALA THR TRP LYS THR VAL ILE ASP ALA MET ALA ILE
SEQRES 74 B 2695 PHE ASP GLY HIS ALA ASN VAL VAL TYR VAL ILE ASP THR
SEQRES 75 B 2695 LYS VAL LEU THR LYS GLU SER LEU TYR GLY SER MET LEU
SEQRES 76 B 2695 LYS ALA THR LEU GLU TRP ARG ASP GLY LEU PHE THR SER
SEQRES 77 B 2695 ILE LEU ARG ARG VAL ASN ASP ASP ILE THR GLY THR PHE
SEQRES 78 B 2695 LYS ASN SER ARG ILE TRP VAL VAL PHE ASP SER ASP LEU
SEQRES 79 B 2695 ASP PRO GLU TYR VAL GLU ALA MET ASN SER VAL LEU ASP
SEQRES 80 B 2695 ASP ASN LYS ILE LEU THR LEU PRO ASN GLY GLU ARG LEU
SEQRES 81 B 2695 PRO ILE PRO PRO ASN PHE ARG ILE LEU PHE GLU THR ASP
SEQRES 82 B 2695 ASN LEU ASP HIS THR THR PRO ALA THR ILE THR ARG CYS
SEQRES 83 B 2695 GLY LEU LEU TRP PHE SER THR ASP VAL CYS SER ILE SER
SEQRES 84 B 2695 SER LYS ILE ASP HIS LEU LEU ASN LYS SER TYR GLU ALA
SEQRES 85 B 2695 LEU ASP ASN LYS LEU SER MET PHE GLU LEU ASP LYS LEU
SEQRES 86 B 2695 LYS ASP LEU ILE SER ASP SER PHE ASP MET ALA SER LEU
SEQRES 87 B 2695 THR ASN ILE PHE THR CYS SER ASN ASP LEU VAL HIS ILE
SEQRES 88 B 2695 LEU GLY VAL ARG THR PHE ASN LYS LEU GLU THR ALA VAL
SEQRES 89 B 2695 GLN LEU ALA VAL HIS LEU ILE SER SER TYR ARG GLN TRP
SEQRES 90 B 2695 PHE GLN ASN LEU ASP ASP LYS SER LEU LYS ASP VAL ILE
SEQRES 91 B 2695 THR LEU LEU ILE LYS ARG SER LEU LEU TYR ALA LEU ALA
SEQRES 92 B 2695 GLY ASP SER THR GLY GLU SER GLN ARG ALA PHE ILE GLN
SEQRES 93 B 2695 THR ILE ASN THR TYR PHE GLY HIS ASP SER GLN GLU LEU
SEQRES 94 B 2695 SER ASP TYR SER THR ILE VAL ILE ALA ASN ASP LYS LEU
SEQRES 95 B 2695 SER PHE SER SER PHE CYS SER GLU ILE PRO SER VAL SER
SEQRES 96 B 2695 LEU GLU ALA HIS GLU VAL MET ARG PRO ASP ILE VAL ILE
SEQRES 97 B 2695 PRO THR ILE ASP THR ILE LYS HIS GLU LYS ILE PHE TYR
SEQRES 98 B 2695 ASP LEU LEU ASN SER LYS ARG GLY ILE ILE LEU CYS GLY
SEQRES 99 B 2695 PRO PRO GLY SER GLY LYS THR MET ILE MET ASN ASN ALA
SEQRES 100 B 2695 LEU ARG ASN SER SER LEU TYR ASP VAL VAL GLY ILE ASN
SEQRES 101 B 2695 PHE SER LYS ASP THR THR THR GLU HIS ILE LEU SER ALA
SEQRES 102 B 2695 LEU HIS ARG HIS THR ASN TYR VAL THR THR SER LYS GLY
SEQRES 103 B 2695 LEU THR LEU LEU PRO LYS SER ASP ILE LYS ASN LEU VAL
SEQRES 104 B 2695 LEU PHE CYS ASP GLU ILE ASN LEU PRO LYS LEU ASP LYS
SEQRES 105 B 2695 TYR GLY SER GLN ASN VAL VAL LEU PHE LEU ARG GLN LEU
SEQRES 106 B 2695 MET GLU LYS GLN GLY PHE TRP LYS THR PRO GLU ASN LYS
SEQRES 107 B 2695 TRP VAL THR ILE GLU ARG ILE HIS ILE VAL GLY ALA CYS
SEQRES 108 B 2695 ASN PRO PRO THR ASP PRO GLY ARG ILE PRO MET SER GLU
SEQRES 109 B 2695 ARG PHE THR ARG HIS ALA ALA ILE LEU TYR LEU GLY TYR
SEQRES 110 B 2695 PRO SER GLY LYS SER LEU SER GLN ILE TYR GLU ILE TYR
SEQRES 111 B 2695 TYR LYS ALA ILE PHE LYS LEU VAL PRO GLU PHE ARG SER
SEQRES 112 B 2695 TYR THR GLU PRO PHE ALA ARG ALA SER VAL HIS LEU TYR
SEQRES 113 B 2695 ASN GLU CYS LYS ALA ARG TYR SER THR GLY LEU GLN SER
SEQRES 114 B 2695 HIS TYR LEU PHE SER PRO ARG GLU LEU THR ARG LEU VAL
SEQRES 115 B 2695 ARG GLY VAL TYR THR ALA ILE ASN THR GLY PRO ARG GLN
SEQRES 116 B 2695 THR LEU ARG SER LEU ILE ARG LEU TRP ALA TYR GLU ALA
SEQRES 117 B 2695 TRP ARG ILE PHE ALA ASP ARG LEU VAL GLY VAL LYS GLU
SEQRES 118 B 2695 LYS ASN SER PHE GLU GLN LEU LEU TYR GLU THR VAL ASP
SEQRES 119 B 2695 LYS TYR LEU PRO ASN GLN ASP LEU GLY ASN ILE SER SER
SEQRES 120 B 2695 THR SER LEU LEU PHE SER GLY LEU LEU SER LEU ASP PHE
SEQRES 121 B 2695 LYS GLU VAL ASN LYS THR ASP LEU VAL ASN PHE ILE GLU
SEQRES 122 B 2695 GLU ARG PHE LYS THR PHE CYS ASP GLU GLU LEU GLU VAL
SEQRES 123 B 2695 PRO MET VAL ILE HIS GLU SER MET VAL ASP HIS ILE LEU
SEQRES 124 B 2695 ARG ILE ASP ARG ALA LEU LYS GLN VAL GLN GLY HIS MET
SEQRES 125 B 2695 MET LEU ILE GLY ALA SER ARG THR GLY LYS THR ILE LEU
SEQRES 126 B 2695 THR ARG PHE VAL ALA TRP LEU ASN GLY LEU LYS ILE VAL
SEQRES 127 B 2695 GLN PRO LYS ILE HIS ARG HIS SER ASN LEU SER ASP PHE
SEQRES 128 B 2695 ASP MET ILE LEU LYS LYS ALA ILE SER ASP CYS SER LEU
SEQRES 129 B 2695 LYS GLU SER ARG THR CYS LEU ILE ILE ASP GLU SER ASN
SEQRES 130 B 2695 ILE LEU GLU THR ALA PHE LEU GLU ARG MET ASN THR LEU
SEQRES 131 B 2695 LEU ALA ASN ALA ASP ILE PRO ASP LEU PHE GLN GLY GLU
SEQRES 132 B 2695 GLU TYR ASP LYS LEU LEU ASN ASN LEU ARG ASN LYS THR
SEQRES 133 B 2695 ARG SER LEU GLY LEU LEU LEU ASP THR GLU GLN GLU LEU
SEQRES 134 B 2695 TYR ASP TRP PHE VAL GLY GLU ILE ALA LYS ASN LEU HIS
SEQRES 135 B 2695 VAL VAL PHE THR ILE CYS ASP PRO THR ASN ASN LYS SER
SEQRES 136 B 2695 SER ALA MET ILE SER SER PRO ALA LEU PHE ASN ARG CYS
SEQRES 137 B 2695 ILE ILE ASN TRP MET GLY ASP TRP ASP THR LYS THR MET
SEQRES 138 B 2695 SER GLN VAL ALA ASN ASN MET VAL ASP VAL ILE PRO MET
SEQRES 139 B 2695 GLU PHE THR ASP PHE ILE VAL PRO GLU VAL ASN LYS GLU
SEQRES 140 B 2695 LEU VAL PHE THR GLU PRO ILE GLN THR ILE ARG ASP ALA
SEQRES 141 B 2695 VAL VAL ASN ILE LEU ILE HIS PHE ASP ARG ASN PHE TYR
SEQRES 142 B 2695 GLN LYS MET LYS VAL GLY VAL ASN PRO ARG SER PRO GLY
SEQRES 143 B 2695 TYR PHE ILE ASP GLY LEU ARG ALA LEU VAL LYS LEU VAL
SEQRES 144 B 2695 THR ALA LYS TYR GLN ASP LEU GLN GLU ASN GLN ARG PHE
SEQRES 145 B 2695 VAL ASN VAL GLY LEU GLU LYS LEU ASN GLU SER VAL LEU
SEQRES 146 B 2695 LYS VAL ASN GLU LEU ASN LYS THR LEU SER ILE SER LEU
SEQRES 147 B 2695 VAL LYS SER LEU THR PHE GLU LYS GLU ARG TRP LEU ASN
SEQRES 148 B 2695 THR THR LYS GLN PHE SER LYS THR SER GLN GLU LEU ILE
SEQRES 149 B 2695 GLY ASN CYS ILE ILE SER SER ILE TYR GLU THR TYR PHE
SEQRES 150 B 2695 GLY HIS LEU ASN GLU ARG GLU ARG ALA ASP MET LEU VAL
SEQRES 151 B 2695 ILE LEU LYS ARG LEU LEU GLY LYS PHE ALA VAL LYS TYR
SEQRES 152 B 2695 ASP VAL ASN TYR ARG PHE ILE ASP TYR LEU VAL THR LEU
SEQRES 153 B 2695 ASP GLU LYS MET LYS TRP LEU GLU CYS GLY LEU ASP LYS
SEQRES 154 B 2695 ASN ASP TYR PHE LEU GLU ASN MET SER ILE VAL MET ASN
SEQRES 155 B 2695 SER GLN ASP ALA VAL PRO PHE LEU LEU ASP PRO SER SER
SEQRES 156 B 2695 HIS MET ILE THR VAL ILE SER ASN TYR TYR GLY ASN LYS
SEQRES 157 B 2695 THR VAL LEU LEU SER PHE LEU GLU GLU GLY PHE VAL LYS
SEQRES 158 B 2695 ARG LEU GLU ASN ALA ILE ARG PHE GLY SER VAL VAL ILE
SEQRES 159 B 2695 ILE GLN ASP GLY GLU PHE PHE ASP PRO ILE ILE SER ARG
SEQRES 160 B 2695 LEU ILE SER ARG GLU PHE ASN HIS ALA GLY ASN ARG VAL
SEQRES 161 B 2695 THR VAL GLU ILE GLY ASP HIS GLU VAL ASP VAL SER GLY
SEQRES 162 B 2695 ASP PHE LYS LEU PHE ILE HIS SER CYS ASP PRO SER GLY
SEQRES 163 B 2695 ASP ILE PRO ILE PHE LEU ARG SER ARG VAL ARG LEU VAL
SEQRES 164 B 2695 HIS PHE VAL THR ASN LYS GLU SER ILE GLU THR ARG ILE
SEQRES 165 B 2695 PHE ASP ILE THR LEU THR GLU GLU ASN ALA GLU MET GLN
SEQRES 166 B 2695 ARG LYS ARG GLU ASP LEU ILE LYS LEU ASN THR GLU TYR
SEQRES 167 B 2695 LYS LEU LYS LEU LYS ASN LEU GLU LYS ARG LEU LEU GLU
SEQRES 168 B 2695 GLU LEU ASN ASN SER GLN GLY ASN MET LEU GLU ASN ASP
SEQRES 169 B 2695 GLU LEU MET VAL THR LEU ASN ASN LEU LYS LYS GLU ALA
SEQRES 170 B 2695 MET ASN ILE GLU LYS LYS LEU SER GLU SER GLU GLU PHE
SEQRES 171 B 2695 PHE PRO GLN PHE ASP ASN LEU VAL GLU GLU TYR SER ILE
SEQRES 172 B 2695 ILE GLY LYS HIS SER VAL LYS ILE PHE SER MET LEU GLU
SEQRES 173 B 2695 LYS PHE GLY GLN PHE HIS TRP PHE TYR GLY ILE SER ILE
SEQRES 174 B 2695 GLY GLN PHE LEU SER CYS PHE LYS ARG VAL PHE ILE LYS
SEQRES 175 B 2695 LYS SER ARG GLU THR ARG ALA ALA ARG THR ARG VAL ASP
SEQRES 176 B 2695 GLU ILE LEU TRP LEU LEU TYR GLN GLU VAL TYR CYS GLN
SEQRES 177 B 2695 PHE SER THR ALA LEU ASP LYS LYS PHE LYS MET ILE MET
SEQRES 178 B 2695 ALA MET THR MET PHE CYS LEU TYR LYS PHE ASP ILE GLU
SEQRES 179 B 2695 SER GLU GLN TYR LYS GLU ALA VAL LEU THR MET ILE GLY
SEQRES 180 B 2695 VAL LEU SER GLU SER SER ASP GLY VAL PRO LYS LEU THR
SEQRES 181 B 2695 VAL ASP THR ASN ASN ASP LEU ARG TYR LEU TRP ASP TYR
SEQRES 182 B 2695 VAL THR THR LYS SER TYR ILE SER ALA LEU ASN TRP PHE
SEQRES 183 B 2695 LYS ASN GLU PHE PHE VAL ASP GLU TRP ASN ILE ALA ASP
SEQRES 184 B 2695 VAL VAL ALA ASN SER ASP ASN ASN TYR PHE THR MET ALA
SEQRES 185 B 2695 SER GLU ARG ASP VAL ASP GLY THR PHE LYS LEU ILE GLU
SEQRES 186 B 2695 LEU ALA LYS ALA SER LYS GLU SER LEU LYS ILE ILE PRO
SEQRES 187 B 2695 LEU GLY SER ILE GLU ASN LEU ASN TYR ALA GLN GLU GLU
SEQRES 188 B 2695 ILE SER LYS SER LYS ILE GLU GLY GLY TRP ILE LEU LEU
SEQRES 189 B 2695 GLN ASN ILE GLN MET SER LEU SER TRP VAL LYS THR TYR
SEQRES 190 B 2695 LEU HIS LYS HIS VAL GLU GLU THR LYS ALA ALA GLU GLU
SEQRES 191 B 2695 HIS GLU LYS PHE LYS MET PHE MET THR CYS HIS LEU THR
SEQRES 192 B 2695 GLY ASP LYS LEU PRO ALA PRO LEU LEU GLN ARG THR ASP
SEQRES 193 B 2695 ARG PHE VAL TYR GLU ASP ILE PRO GLY ILE LEU ASP THR
SEQRES 194 B 2695 VAL LYS ASP LEU TRP GLY SER GLN PHE PHE THR GLY LYS
SEQRES 195 B 2695 ILE SER GLY VAL TRP SER VAL TYR CYS THR PHE LEU LEU
SEQRES 196 B 2695 SER TRP PHE HIS ALA LEU ILE THR ALA ARG THR ARG LEU
SEQRES 197 B 2695 VAL PRO HIS GLY PHE SER LYS LYS TYR TYR PHE ASN ASP
SEQRES 198 B 2695 CYS ASP PHE GLN PHE ALA SER VAL TYR LEU GLU ASN VAL
SEQRES 199 B 2695 LEU ALA THR ASN SER THR ASN ASN ILE PRO TRP ALA GLN
SEQRES 200 B 2695 VAL ARG ASP HIS ILE ALA THR ILE VAL TYR GLY GLY LYS
SEQRES 201 B 2695 ILE ASP GLU GLU LYS ASP LEU GLU VAL VAL ALA LYS LEU
SEQRES 202 B 2695 CYS ALA HIS VAL PHE CYS GLY SER ASP ASN LEU GLN ILE
SEQRES 203 B 2695 VAL PRO GLY VAL ARG ILE PRO GLN PRO LEU LEU GLN GLN
SEQRES 204 B 2695 SER GLU GLU GLU GLU ARG ALA ARG LEU THR ALA ILE LEU
SEQRES 205 B 2695 SER ASN THR ILE GLU PRO ALA ASP SER LEU SER SER TRP
SEQRES 206 B 2695 LEU GLN LEU PRO ARG GLU SER ILE LEU ASN TYR GLU ARG
SEQRES 207 B 2695 LEU GLN ALA LYS GLU VAL ALA SER SER THR GLU GLN LEU
SEQRES 208 B 2695 LEU GLN GLU MET
HET ATP A5093 31
HET ANP A5094 31
HET SO4 A5095 5
HET SO4 A5096 5
HET MG A5097 1
HET ATP B5093 31
HET ANP B5094 31
HET SO4 B5095 5
HET SO4 B5096 5
HET MG B5097 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 4 ANP 2(C10 H17 N6 O12 P3)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 7 MG 2(MG 2+)
HELIX 1 1 GLN A 14 TYR A 22 1 9
HELIX 2 2 GLY A 37 LYS A 43 1 7
HELIX 3 3 SER A 67 ASP A 76 1 10
HELIX 4 4 PRO A 85 ARG A 107 1 23
HELIX 5 5 LYS A 118 ARG A 135 1 18
HELIX 6 6 HIS A 149 MET A 164 1 16
HELIX 7 7 PRO A 173 ALA A 184 1 12
HELIX 8 8 PRO A 186 LEU A 192 1 7
HELIX 9 9 VAL A 1366 TRP A 1378 1 13
HELIX 10 10 ASP A 1399 SER A 1414 1 16
HELIX 11 11 GLU A 1425 ILE A 1458 1 34
HELIX 12 12 ASP A 1464 PHE A 1468 1 5
HELIX 13 13 PRO A 1470 PHE A 1491 1 22
HELIX 14 14 PHE A 1505 GLN A 1533 1 29
HELIX 15 15 PHE A 1537 LEU A 1540 1 4
HELIX 16 16 ASN A 1542 GLY A 1550 1 9
HELIX 17 17 SER A 1559 PHE A 1566 1 8
HELIX 18 18 ALA A 1604 LYS A 1631 1 28
HELIX 19 19 ILE A 1636 VAL A 1640 1 5
HELIX 20 20 PHE A 1645 THR A 1666 1 22
HELIX 21 21 PHE A 1669 ASN A 1688 1 20
HELIX 22 22 ASP A 1692 ASN A 1717 1 26
HELIX 23 23 LYS A 1721 LYS A 1730 1 10
HELIX 24 24 PRO A 1773 HIS A 1787 1 15
HELIX 25 25 LYS A 1802 GLN A 1811 1 10
HELIX 26 26 TYR A 1828 ILE A 1841 1 14
HELIX 27 27 GLU A 1855 VAL A 1874 1 20
HELIX 28 28 GLU A 1910 LYS A 1913 1 4
HELIX 29 29 GLY A 1927 GLY A 1938 1 12
HELIX 30 30 SER A 1942 LYS A 1959 1 18
HELIX 31 31 LEU A 1970 GLU A 1986 1 17
HELIX 32 32 GLU A 1991 VAL A 2001 1 11
HELIX 33 33 ASP A 2008 ILE A 2021 1 14
HELIX 34 34 ALA A 2033 SER A 2045 1 13
HELIX 35 35 GLU A 2051 THR A 2066 1 16
HELIX 36 36 LYS A 2080 PHE A 2094 1 15
HELIX 37 37 LYS A 2111 LEU A 2114 1 4
HELIX 38 38 LEU A 2129 ASP A 2140 1 12
HELIX 39 39 PRO A 2160 GLU A 2164 1 5
HELIX 40 40 MET A 2166 LEU A 2170 1 5
HELIX 41 41 PRO A 2204 ARG A 2209 1 6
HELIX 42 42 ILE A 2222 ASP A 2238 1 17
HELIX 43 43 MET A 2243 SER A 2256 1 14
HELIX 44 44 MET A 2259 ASN A 2270 1 12
HELIX 45 45 THR A 2280 SER A 2297 1 18
HELIX 46 46 ASP A 2307 ALA A 2327 1 21
HELIX 47 47 GLU A 2333 TYR A 2345 1 13
HELIX 48 48 ILE A 2395 SER A 2410 1 16
HELIX 49 49 LYS A 2424 ASN A 2434 1 11
HELIX 50 50 THR A 2451 HIS A 2461 1 11
HELIX 51 51 ASN A 2501 GLU A 2511 1 11
HELIX 52 52 SER A 2566 ILE A 2578 1 13
HELIX 53 53 THR A 2589 ARG A 2606 1 18
HELIX 54 54 PRO A 2619 ASN A 2634 1 16
HELIX 55 55 LEU A 2641 PHE A 2656 1 16
HELIX 56 56 LYS A 2664 TYR A 2680 1 17
HELIX 57 57 LYS A 2709 GLU A 2726 1 18
HELIX 58 58 GLU A 2736 LYS A 2750 1 15
HELIX 59 59 LYS A 2766 LEU A 2776 1 11
HELIX 60 60 LEU A 2792 LEU A 2808 1 17
HELIX 61 61 THR A 2825 ALA A 2836 1 12
HELIX 62 62 GLU A 2847 LEU A 2863 1 17
HELIX 63 63 GLU A 2870 ASN A 2884 1 15
HELIX 64 64 ASN A 2897 SER A 2904 1 8
HELIX 65 65 PRO A 2906 ARG A 2911 1 6
HELIX 66 66 THR A 2922 MET A 2932 1 11
HELIX 67 67 ILE A 2961 LYS A 2979 1 19
HELIX 68 68 TYR A 2991 SER A 3027 1 37
HELIX 69 69 THR A 3300 GLU A 3304 1 5
HELIX 70 70 ASN A 3308 THR A 3332 1 25
HELIX 71 71 GLU A 3339 LYS A 3355 1 17
HELIX 72 72 PHE A 3366 LEU A 3370 1 5
HELIX 73 73 LEU A 3373 CYS A 3382 1 10
HELIX 74 74 ASP A 3388 ASN A 3399 1 12
HELIX 75 75 MET A 3414 TYR A 3422 1 9
HELIX 76 76 PHE A 3436 ARG A 3445 1 10
HELIX 77 77 SER A 3463 ILE A 3466 1 4
HELIX 78 78 ILE A 3507 ARG A 3512 1 6
HELIX 79 79 GLU A 3523 THR A 3535 1 13
HELIX 80 80 ALA A 3539 ASN A 3572 1 34
HELIX 81 81 ASN A 3580 MET A 3584 1 5
HELIX 82 82 THR A 3586 PHE A 3638 1 53
HELIX 83 83 ILE A 3646 ARG A 3655 1 10
HELIX 84 84 ARG A 3670 PHE A 3686 1 17
HELIX 85 85 LYS A 3692 ILE A 3710 1 19
HELIX 86 86 GLU A 3713 LEU A 3726 1 14
HELIX 87 87 ASP A 3743 THR A 3752 1 10
HELIX 88 88 TYR A 3756 ASN A 3765 1 10
HELIX 89 89 ILE A 3774 ASN A 3780 1 7
HELIX 90 90 THR A 3797 LYS A 3805 1 9
HELIX 91 91 ILE A 3819 GLU A 3835 1 17
HELIX 92 92 LEU A 3848 THR A 3853 1 6
HELIX 93 93 TYR A 3854 GLU A 3861 1 8
HELIX 94 94 ALA A 3886 ARG A 3891 1 6
HELIX 95 95 ILE A 3903 SER A 3913 1 11
HELIX 96 96 VAL A 3923 ARG A 3944 1 22
HELIX 97 97 ASP A 3958 THR A 3974 1 17
HELIX 98 98 ALA A 3983 THR A 3991 1 9
HELIX 99 99 GLU A 4001 VAL A 4014 1 14
HELIX 100 100 GLU A 4038 ASN A 4051 1 14
HELIX 101 101 SER A 4058 SER A 4061 1 4
HELIX 102 102 ARG A 4067 GLN A 4090 1 24
HELIX 103 103 GLN B 14 TYR B 22 1 9
HELIX 104 104 GLY B 37 LYS B 43 1 7
HELIX 105 105 SER B 67 ASP B 76 1 10
HELIX 106 106 PRO B 85 ARG B 107 1 23
HELIX 107 107 PHE B 114 ARG B 135 1 22
HELIX 108 108 PRO B 150 MET B 164 1 15
HELIX 109 109 PRO B 173 ALA B 184 1 12
HELIX 110 110 PRO B 186 LEU B 192 1 7
HELIX 111 111 VAL B 1366 TRP B 1378 1 13
HELIX 112 112 ASP B 1399 SER B 1414 1 16
HELIX 113 113 PHE B 1424 ILE B 1458 1 35
HELIX 114 114 LEU B 1463 PHE B 1468 1 6
HELIX 115 115 PRO B 1470 PHE B 1491 1 22
HELIX 116 116 PHE B 1505 GLN B 1533 1 29
HELIX 117 117 PHE B 1537 LEU B 1540 1 4
HELIX 118 118 ASN B 1542 GLY B 1550 1 9
HELIX 119 119 SER B 1559 PHE B 1566 1 8
HELIX 120 120 ALA B 1604 LYS B 1631 1 28
HELIX 121 121 ILE B 1636 VAL B 1640 1 5
HELIX 122 122 PHE B 1645 THR B 1666 1 22
HELIX 123 123 PHE B 1669 ASN B 1688 1 20
HELIX 124 124 ASP B 1692 ASN B 1717 1 26
HELIX 125 125 LYS B 1721 LYS B 1730 1 10
HELIX 126 126 PRO B 1773 HIS B 1787 1 15
HELIX 127 127 LYS B 1802 GLN B 1811 1 10
HELIX 128 128 TYR B 1828 ILE B 1841 1 14
HELIX 129 129 GLU B 1855 VAL B 1874 1 20
HELIX 130 130 GLU B 1910 LYS B 1913 1 4
HELIX 131 131 SER B 1926 GLY B 1938 1 13
HELIX 132 132 SER B 1942 LYS B 1959 1 18
HELIX 133 133 LEU B 1970 GLU B 1986 1 17
HELIX 134 134 GLU B 1991 VAL B 2001 1 11
HELIX 135 135 ASP B 2008 ILE B 2021 1 14
HELIX 136 136 ALA B 2033 SER B 2045 1 13
HELIX 137 137 GLU B 2051 THR B 2066 1 16
HELIX 138 138 LYS B 2080 PHE B 2094 1 15
HELIX 139 139 LYS B 2111 LEU B 2114 1 4
HELIX 140 140 LEU B 2129 ASP B 2140 1 12
HELIX 141 141 PRO B 2160 GLU B 2164 1 5
HELIX 142 142 MET B 2166 LEU B 2170 1 5
HELIX 143 143 PRO B 2204 ARG B 2209 1 6
HELIX 144 144 ILE B 2222 ASP B 2238 1 17
HELIX 145 145 MET B 2243 SER B 2256 1 14
HELIX 146 146 MET B 2259 ASN B 2270 1 12
HELIX 147 147 THR B 2280 SER B 2297 1 18
HELIX 148 148 ASP B 2307 ALA B 2327 1 21
HELIX 149 149 GLU B 2333 TYR B 2345 1 13
HELIX 150 150 ILE B 2395 SER B 2410 1 16
HELIX 151 151 LYS B 2424 ASN B 2434 1 11
HELIX 152 152 THR B 2451 HIS B 2459 1 9
HELIX 153 153 ASN B 2501 GLU B 2511 1 11
HELIX 154 154 GLU B 2548 THR B 2551 1 4
HELIX 155 155 SER B 2566 ILE B 2578 1 13
HELIX 156 156 THR B 2589 ARG B 2606 1 18
HELIX 157 157 PRO B 2619 ASN B 2634 1 16
HELIX 158 158 LEU B 2641 PHE B 2656 1 16
HELIX 159 159 LYS B 2664 TYR B 2680 1 17
HELIX 160 160 LYS B 2709 GLU B 2726 1 18
HELIX 161 161 GLU B 2736 LYS B 2750 1 15
HELIX 162 162 LYS B 2766 LEU B 2776 1 11
HELIX 163 163 LEU B 2792 LEU B 2808 1 17
HELIX 164 164 THR B 2825 ALA B 2836 1 12
HELIX 165 165 GLU B 2847 LEU B 2863 1 17
HELIX 166 166 GLU B 2870 ASN B 2884 1 15
HELIX 167 167 ASN B 2897 SER B 2904 1 8
HELIX 168 168 PRO B 2906 ARG B 2911 1 6
HELIX 169 169 THR B 2922 MET B 2932 1 11
HELIX 170 170 ILE B 2961 LYS B 2979 1 19
HELIX 171 171 TYR B 2991 SER B 3027 1 37
HELIX 172 172 THR B 3300 GLU B 3304 1 5
HELIX 173 173 LEU B 3307 THR B 3332 1 26
HELIX 174 174 GLU B 3339 LYS B 3355 1 17
HELIX 175 175 PHE B 3366 LEU B 3370 1 5
HELIX 176 176 LEU B 3373 CYS B 3382 1 10
HELIX 177 177 ASP B 3388 ASN B 3399 1 12
HELIX 178 178 MET B 3414 TYR B 3422 1 9
HELIX 179 179 PHE B 3436 ARG B 3445 1 10
HELIX 180 180 SER B 3463 ILE B 3466 1 4
HELIX 181 181 ILE B 3507 ARG B 3512 1 6
HELIX 182 182 GLU B 3523 GLU B 3537 1 15
HELIX 183 183 ALA B 3539 ASN B 3572 1 34
HELIX 184 184 ASN B 3580 MET B 3584 1 5
HELIX 185 185 THR B 3586 PHE B 3638 1 53
HELIX 186 186 ILE B 3646 ARG B 3655 1 10
HELIX 187 187 ARG B 3670 PHE B 3686 1 17
HELIX 188 188 LYS B 3692 ILE B 3710 1 19
HELIX 189 189 GLU B 3713 LEU B 3726 1 14
HELIX 190 190 ASP B 3743 THR B 3752 1 10
HELIX 191 191 TYR B 3756 ASN B 3765 1 10
HELIX 192 192 ILE B 3774 ASN B 3780 1 7
HELIX 193 193 THR B 3797 ALA B 3806 1 10
HELIX 194 194 ILE B 3819 GLU B 3835 1 17
HELIX 195 195 LEU B 3848 THR B 3853 1 6
HELIX 196 196 TYR B 3854 GLU B 3861 1 8
HELIX 197 197 ALA B 3886 ARG B 3891 1 6
HELIX 198 198 ILE B 3903 SER B 3913 1 11
HELIX 199 199 VAL B 3923 ARG B 3944 1 22
HELIX 200 200 ASP B 3958 THR B 3974 1 17
HELIX 201 201 TRP B 3982 THR B 3991 1 10
HELIX 202 202 GLU B 4001 VAL B 4014 1 14
HELIX 203 203 GLU B 4038 ASN B 4051 1 14
HELIX 204 204 SER B 4058 SER B 4061 1 4
HELIX 205 205 ARG B 4067 GLN B 4090 1 24
SHEET 1 1 1 ILE A 3 TRP A 7 0
SHEET 1 2 1 GLU A 28 TYR A 32 0
SHEET 1 3 1 TYR A 56 ILE A 58 0
SHEET 1 4 1 LYS A 63 THR A 65 0
SHEET 1 5 1 GLU A1384 GLU A1387 0
SHEET 1 6 1 LYS A1393 ARG A1396 0
SHEET 1 7 1 ILE A1569 PHE A1574 0
SHEET 1 8 1 PHE A1578 SER A1584 0
SHEET 1 9 1 VAL A1589 GLU A1597 0
SHEET 1 10 1 LYS A1733 GLN A1736 0
SHEET 1 11 1 VAL A1747 GLN A1751 0
SHEET 1 12 1 TYR A1754 GLN A1757 0
SHEET 1 13 1 GLY A1791 PHE A1795 0
SHEET 1 14 1 VAL A1818 ASN A1821 0
SHEET 1 15 1 TRP A1844 ASP A1848 0
SHEET 1 16 1 HIS A1878 LEU A1881 0
SHEET 1 17 1 GLU A1884 PRO A1887 0
SHEET 1 18 1 ALA A1893 LEU A1898 0
SHEET 1 19 1 PHE A1916 SER A1920 0
SHEET 1 20 1 ALA A2069 VAL A2073 0
SHEET 1 21 1 ASN A2099 ILE A2104 0
SHEET 1 22 1 SER A2117 LEU A2119 0
SHEET 1 23 1 LEU A2123 ARG A2126 0
SHEET 1 24 1 ARG A2149 PHE A2154 0
SHEET 1 25 1 LYS A2174 LEU A2178 0
SHEET 1 26 1 GLU A2182 ILE A2186 0
SHEET 1 27 1 ARG A2191 THR A2196 0
SHEET 1 28 1 GLY A2211 TRP A2214 0
SHEET 1 29 1 GLY A2413 CYS A2417 0
SHEET 1 30 1 ASP A2439 ASN A2444 0
SHEET 1 31 1 VAL A2465 THR A2467 0
SHEET 1 32 1 LEU A2471 LEU A2474 0
SHEET 1 33 1 LEU A2482 ASP A2487 0
SHEET 1 34 1 GLY A2514 TRP A2516 0
SHEET 1 35 1 TRP A2523 ILE A2526 0
SHEET 1 36 1 ILE A2529 CYS A2535 0
SHEET 1 37 1 ALA A2554 TYR A2558 0
SHEET 1 38 1 PHE A2696 SER A2697 0
SHEET 1 39 1 LYS A2705 GLU A2706 0
SHEET 1 40 1 GLY A2754 ILE A2759 0
SHEET 1 41 1 LYS A2780 GLN A2783 0
SHEET 1 42 1 THR A2813 ASP A2818 0
SHEET 1 43 1 HIS A2886 ILE A2891 0
SHEET 1 44 1 ILE A2913 TRP A2916 0
SHEET 1 45 1 VAL A3404 LEU A3408 0
SHEET 1 46 1 THR A3426 LEU A3429 0
SHEET 1 47 1 VAL A3449 ILE A3452 0
SHEET 1 48 1 PHE A3470 ALA A3473 0
SHEET 1 49 1 ARG A3476 ILE A3481 0
SHEET 1 50 1 HIS A3484 VAL A3488 0
SHEET 1 51 1 LYS A3493 SER A3498 0
SHEET 1 52 1 VAL A3513 HIS A3517 0
SHEET 1 53 1 TYR A3785 SER A3790 0
SHEET 1 54 1 LYS A3812 PRO A3815 0
SHEET 1 55 1 ILE A3839 GLN A3842 0
SHEET 1 56 1 MET A3873 HIS A3878 0
SHEET 1 57 1 ASP A3893 VAL A3896 0
SHEET 1 58 1 ILE B 3 TRP B 7 0
SHEET 1 59 1 GLU B 28 TYR B 32 0
SHEET 1 60 1 TYR B 56 ILE B 58 0
SHEET 1 61 1 LYS B 63 THR B 65 0
SHEET 1 62 1 GLU B1384 GLU B1387 0
SHEET 1 63 1 LYS B1393 ARG B1396 0
SHEET 1 64 1 ILE B1569 PHE B1574 0
SHEET 1 65 1 PHE B1578 SER B1584 0
SHEET 1 66 1 VAL B1589 GLU B1597 0
SHEET 1 67 1 LYS B1733 GLN B1736 0
SHEET 1 68 1 VAL B1747 GLN B1751 0
SHEET 1 69 1 TYR B1754 GLN B1757 0
SHEET 1 70 1 GLY B1791 PHE B1795 0
SHEET 1 71 1 VAL B1818 ASN B1821 0
SHEET 1 72 1 TRP B1844 ASP B1848 0
SHEET 1 73 1 HIS B1878 LEU B1881 0
SHEET 1 74 1 GLU B1884 PRO B1887 0
SHEET 1 75 1 ALA B1893 LEU B1898 0
SHEET 1 76 1 PHE B1916 SER B1920 0
SHEET 1 77 1 ALA B2069 VAL B2073 0
SHEET 1 78 1 ASN B2099 ILE B2104 0
SHEET 1 79 1 SER B2117 LEU B2119 0
SHEET 1 80 1 LEU B2123 ARG B2126 0
SHEET 1 81 1 ARG B2149 PHE B2154 0
SHEET 1 82 1 LYS B2174 LEU B2178 0
SHEET 1 83 1 GLU B2182 ILE B2186 0
SHEET 1 84 1 PHE B2190 THR B2196 0
SHEET 1 85 1 GLY B2211 TRP B2214 0
SHEET 1 86 1 GLY B2413 CYS B2417 0
SHEET 1 87 1 ASP B2439 ASN B2444 0
SHEET 1 88 1 VAL B2465 THR B2467 0
SHEET 1 89 1 LEU B2471 LEU B2474 0
SHEET 1 90 1 LEU B2482 ASP B2487 0
SHEET 1 91 1 GLY B2514 TRP B2516 0
SHEET 1 92 1 TRP B2523 ILE B2526 0
SHEET 1 93 1 ILE B2529 CYS B2535 0
SHEET 1 94 1 ALA B2554 TYR B2558 0
SHEET 1 95 1 PHE B2696 SER B2697 0
SHEET 1 96 1 LYS B2705 GLU B2706 0
SHEET 1 97 1 GLY B2754 ILE B2759 0
SHEET 1 98 1 LYS B2780 GLN B2783 0
SHEET 1 99 1 THR B2813 ASP B2818 0
SHEET 1 100 1 HIS B2886 ILE B2891 0
SHEET 1 101 1 ILE B2913 TRP B2916 0
SHEET 1 102 1 PRO B3405 LEU B3408 0
SHEET 1 103 1 THR B3426 LEU B3429 0
SHEET 1 104 1 VAL B3449 ILE B3452 0
SHEET 1 105 1 PHE B3470 ALA B3473 0
SHEET 1 106 1 ARG B3476 ILE B3481 0
SHEET 1 107 1 HIS B3484 VAL B3488 0
SHEET 1 108 1 LYS B3493 SER B3498 0
SHEET 1 109 1 ARG B3514 HIS B3517 0
SHEET 1 110 1 TYR B3785 SER B3790 0
SHEET 1 111 1 LYS B3812 PRO B3815 0
SHEET 1 112 1 ILE B3839 GLN B3842 0
SHEET 1 113 1 MET B3873 HIS B3878 0
SHEET 1 114 1 ASP B3893 VAL B3896 0
LINK OG1 THR A2081 MG MG A5097 1555 1555 2.28
LINK OE2 GLU A2195 MG MG A5097 1555 1555 2.73
LINK O3G ATP A5093 MG MG A5097 1555 1555 2.04
LINK O1B ATP A5093 MG MG A5097 1555 1555 2.51
LINK O2A ATP A5093 MG MG A5097 1555 1555 2.34
LINK OG1 THR B2081 MG MG B5097 1555 1555 1.87
LINK OE2 GLU B2511 MG MG B5097 1555 1555 2.60
LINK O2A ATP B5093 MG MG B5097 1555 1555 2.20
LINK O1B ATP B5093 MG MG B5097 1555 1555 2.68
LINK O3G ATP B5093 MG MG B5097 1555 1555 1.83
CISPEP 1 LEU A 54 PRO A 55 0 -1.60
CISPEP 2 TRP A 200 PRO A 201 0 6.39
CISPEP 3 VAL A 3946 PRO A 3947 0 8.39
CISPEP 4 LEU B 54 PRO B 55 0 -0.95
CISPEP 5 TRP B 200 PRO B 201 0 4.93
CISPEP 6 VAL B 3946 PRO B 3947 0 6.75
SITE 1 AC1 19 SER A2048 LYS A2075 GLY A2077 CYS A2078
SITE 2 AC1 19 GLY A2079 LYS A2080 THR A2081 ALA A2082
SITE 3 AC1 19 GLU A2195 VAL A2219 CYS A2220 SER A2224
SITE 4 AC1 19 LYS A2225 HIS A2228 ARG A2507 GLU A2511
SITE 5 AC1 19 ARG A2549 ARG A2552 MG A5097
SITE 1 AC2 17 VAL A2391 ILE A2392 THR A2397 GLY A2421
SITE 2 AC2 17 SER A2422 GLY A2423 LYS A2424 THR A2425
SITE 3 AC2 17 MET A2426 ASP A2487 ALA A2534 ILE A2570
SITE 4 AC2 17 TYR A2571 TYR A2574 PRO A2619 ARG A2620
SITE 5 AC2 17 THR A2623
SITE 1 AC3 19 SER B2048 GLY B2077 CYS B2078 GLY B2079
SITE 2 AC3 19 LYS B2080 THR B2081 ALA B2082 ASP B2155
SITE 3 AC3 19 GLU B2195 VAL B2219 CYS B2220 SER B2224
SITE 4 AC3 19 LYS B2225 HIS B2228 ARG B2507 GLU B2511
SITE 5 AC3 19 ARG B2549 ARG B2552 MG B5097
SITE 1 AC4 16 VAL B2391 ILE B2392 THR B2394 THR B2397
SITE 2 AC4 16 GLY B2421 SER B2422 GLY B2423 LYS B2424
SITE 3 AC4 16 THR B2425 MET B2426 ASP B2487 ILE B2570
SITE 4 AC4 16 TYR B2571 TYR B2574 ARG B2620 THR B2623
SITE 1 AC5 7 SER B2762 ARG B2763 THR B2764 GLY B2765
SITE 2 AC5 7 LYS B2766 THR B2767 ARG B3512
SITE 1 AC6 5 ALA B1798 GLY B1799 THR B1800 GLY B1801
SITE 2 AC6 5 LYS B1802
SITE 1 AC7 6 PRO A1797 GLY A1799 THR A1800 GLY A1801
SITE 2 AC7 6 LYS A1802 THR A1803
SITE 1 AC8 5 ARG A2763 THR A2764 GLY A2765 LYS A2766
SITE 2 AC8 5 THR A2767
SITE 1 AC9 4 THR A2081 GLU A2195 GLU A2511 ATP A5093
SITE 1 BC1 4 THR B2081 GLU B2195 GLU B2511 ATP B5093
CRYST1 175.560 118.130 201.020 90.00 90.29 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 0.005696 0.000000 0.000029 0.00000
SCALE2 0.000000 0.008465 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004975 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
