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HEADER HYDROLASE 06-MAY-16 5JRL
TITLE CRYSTAL STRUCTURE OF THE SPHINGOPYXIN I LASSO PEPTIDE ISOPEPTIDASE
TITLE 2 SPI-ISOP (NATIVE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASES/ACYLAMINOACYL-PEPTIDASES-LIKE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: SPI-ISOP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOPYXIS ALASKENSIS RB2256;
SOURCE 3 ORGANISM_TAXID: 317655;
SOURCE 4 GENE: SALA_2532;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS LASSO PEPTIDE ISOPEPTIDASE, SERINE PROTEASE, BETA-PROPELLER,
KEYWDS 2 ALPHA/BETA-HYDROLASE, CATALYTIC TRIAD, OXYANION HOLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FAGE,J.D.HEGEMANN,G.BANGE,M.A.MARAHIEL
REVDAT 1 14-SEP-16 5JRL 0
JRNL AUTH C.D.FAGE,J.D.HEGEMANN,A.J.NEBEL,R.M.STEINBACH,S.ZHU,U.LINNE,
JRNL AUTH 2 K.HARMS,G.BANGE,M.A.MARAHIEL
JRNL TITL CRYSTAL STRUCTURE AND CHARACTERIZATION OF SPI-ISOP, AN
JRNL TITL 2 ISOPEPTIDASE THAT HYDROLYZES THE LASSO PEPTIDE SPHINGOPYXIN
JRNL TITL 3 I
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2016
JRNL REFN ESSN 1521-3773
JRNL DOI 10.1002/ANIE.201605232
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10-2152
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 52720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 2557
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.4000 - 8.3727 0.99 2828 157 0.1829 0.2100
REMARK 3 2 8.3727 - 6.6512 0.99 2834 122 0.1940 0.2028
REMARK 3 3 6.6512 - 5.8120 1.00 2807 129 0.1981 0.2260
REMARK 3 4 5.8120 - 5.2813 1.00 2782 168 0.2029 0.2240
REMARK 3 5 5.2813 - 4.9032 1.00 2755 175 0.1896 0.2318
REMARK 3 6 4.9032 - 4.6143 1.00 2811 121 0.1928 0.2700
REMARK 3 7 4.6143 - 4.3834 1.00 2813 115 0.2024 0.2992
REMARK 3 8 4.3834 - 4.1927 1.00 2776 153 0.2106 0.2567
REMARK 3 9 4.1927 - 4.0314 1.00 2742 175 0.2151 0.2611
REMARK 3 10 4.0314 - 3.8923 1.00 2774 140 0.2263 0.3027
REMARK 3 11 3.8923 - 3.7707 1.00 2800 132 0.2515 0.3227
REMARK 3 12 3.7707 - 3.6629 1.00 2786 123 0.2680 0.3139
REMARK 3 13 3.6629 - 3.5665 1.00 2800 126 0.2717 0.3622
REMARK 3 14 3.5665 - 3.4795 1.00 2810 122 0.2852 0.3183
REMARK 3 15 3.4795 - 3.4005 1.00 2768 154 0.2887 0.3425
REMARK 3 16 3.4005 - 3.3281 1.00 2770 143 0.3092 0.3522
REMARK 3 17 3.3281 - 3.2615 1.00 2730 157 0.3104 0.3492
REMARK 3 18 3.2615 - 3.2000 1.00 2777 145 0.3362 0.4346
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 81.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 21351
REMARK 3 ANGLE : 0.519 28994
REMARK 3 CHIRALITY : 0.042 3172
REMARK 3 PLANARITY : 0.004 3812
REMARK 3 DIHEDRAL : 9.529 12819
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221119.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS OCT 15, 2015
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52747
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.394
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 5JRK
REMARK 200
REMARK 200 REMARK: PLATE-LIKE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 20%(W/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
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 68.29300
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, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 64.39812
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -68.29300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 329.39629
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 64.39812
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 68.29300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 329.39629
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 ILE A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 VAL A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 SER A 21
REMARK 465 PRO A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 GLN A 25
REMARK 465 ALA A 26
REMARK 465 GLY A 27
REMARK 465 GLU A 28
REMARK 465 SER A 29
REMARK 465 GLY A 150
REMARK 465 GLY A 151
REMARK 465 SER A 251
REMARK 465 ASP A 252
REMARK 465 GLY A 253
REMARK 465 THR A 254
REMARK 465 LEU A 255
REMARK 465 GLY A 256
REMARK 465 GLY A 257
REMARK 465 ALA A 258
REMARK 465 PHE A 259
REMARK 465 LEU A 274
REMARK 465 ALA A 275
REMARK 465 LYS A 276
REMARK 465 GLN A 277
REMARK 465 ARG A 278
REMARK 465 ASP A 279
REMARK 465 CYS A 722
REMARK 465 ALA A 723
REMARK 465 ALA A 724
REMARK 465 ALA A 725
REMARK 465 PRO A 726
REMARK 465 SER A 727
REMARK 465 ALA A 728
REMARK 465 TRP A 729
REMARK 465 SER A 730
REMARK 465 HIS A 731
REMARK 465 PRO A 732
REMARK 465 GLN A 733
REMARK 465 PHE A 734
REMARK 465 GLU A 735
REMARK 465 LYS A 736
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ILE B 3
REMARK 465 ALA B 4
REMARK 465 LEU B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 GLY B 8
REMARK 465 LEU B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 VAL B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 LEU B 20
REMARK 465 SER B 21
REMARK 465 PRO B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 GLN B 25
REMARK 465 ALA B 26
REMARK 465 GLY B 27
REMARK 465 GLU B 28
REMARK 465 SER B 29
REMARK 465 GLY B 149
REMARK 465 GLY B 150
REMARK 465 GLY B 151
REMARK 465 GLY B 233
REMARK 465 GLY B 234
REMARK 465 GLY B 235
REMARK 465 ARG B 236
REMARK 465 ASP B 252
REMARK 465 GLY B 253
REMARK 465 THR B 254
REMARK 465 LEU B 255
REMARK 465 GLY B 256
REMARK 465 GLY B 257
REMARK 465 ALA B 258
REMARK 465 PHE B 259
REMARK 465 LEU B 274
REMARK 465 ALA B 275
REMARK 465 LYS B 276
REMARK 465 GLN B 277
REMARK 465 ARG B 278
REMARK 465 ASP B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 SER B 282
REMARK 465 ALA B 310
REMARK 465 GLU B 311
REMARK 465 GLY B 312
REMARK 465 ALA B 723
REMARK 465 ALA B 724
REMARK 465 ALA B 725
REMARK 465 PRO B 726
REMARK 465 SER B 727
REMARK 465 ALA B 728
REMARK 465 TRP B 729
REMARK 465 SER B 730
REMARK 465 HIS B 731
REMARK 465 PRO B 732
REMARK 465 GLN B 733
REMARK 465 PHE B 734
REMARK 465 GLU B 735
REMARK 465 LYS B 736
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 ILE C 3
REMARK 465 ALA C 4
REMARK 465 LEU C 5
REMARK 465 ARG C 6
REMARK 465 SER C 7
REMARK 465 GLY C 8
REMARK 465 LEU C 9
REMARK 465 PRO C 10
REMARK 465 ALA C 11
REMARK 465 VAL C 12
REMARK 465 ALA C 13
REMARK 465 LEU C 14
REMARK 465 LEU C 15
REMARK 465 ALA C 16
REMARK 465 ALA C 17
REMARK 465 ALA C 18
REMARK 465 ALA C 19
REMARK 465 LEU C 20
REMARK 465 SER C 21
REMARK 465 PRO C 22
REMARK 465 ALA C 23
REMARK 465 ALA C 24
REMARK 465 GLN C 25
REMARK 465 ALA C 26
REMARK 465 GLY C 27
REMARK 465 GLU C 28
REMARK 465 SER C 29
REMARK 465 LYS C 30
REMARK 465 GLY C 150
REMARK 465 GLY C 151
REMARK 465 GLY C 233
REMARK 465 GLY C 234
REMARK 465 GLY C 235
REMARK 465 SER C 251
REMARK 465 ASP C 252
REMARK 465 GLY C 253
REMARK 465 THR C 254
REMARK 465 LEU C 255
REMARK 465 GLY C 256
REMARK 465 GLY C 257
REMARK 465 ALA C 275
REMARK 465 LYS C 276
REMARK 465 GLN C 277
REMARK 465 ARG C 278
REMARK 465 ASP C 279
REMARK 465 LEU C 280
REMARK 465 LEU C 281
REMARK 465 SER C 282
REMARK 465 MET C 283
REMARK 465 SER C 284
REMARK 465 ALA C 310
REMARK 465 GLU C 311
REMARK 465 GLY C 312
REMARK 465 ARG C 313
REMARK 465 ARG C 721
REMARK 465 CYS C 722
REMARK 465 ALA C 723
REMARK 465 ALA C 724
REMARK 465 ALA C 725
REMARK 465 PRO C 726
REMARK 465 SER C 727
REMARK 465 ALA C 728
REMARK 465 TRP C 729
REMARK 465 SER C 730
REMARK 465 HIS C 731
REMARK 465 PRO C 732
REMARK 465 GLN C 733
REMARK 465 PHE C 734
REMARK 465 GLU C 735
REMARK 465 LYS C 736
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 ILE D 3
REMARK 465 ALA D 4
REMARK 465 LEU D 5
REMARK 465 ARG D 6
REMARK 465 SER D 7
REMARK 465 GLY D 8
REMARK 465 LEU D 9
REMARK 465 PRO D 10
REMARK 465 ALA D 11
REMARK 465 VAL D 12
REMARK 465 ALA D 13
REMARK 465 LEU D 14
REMARK 465 LEU D 15
REMARK 465 ALA D 16
REMARK 465 ALA D 17
REMARK 465 ALA D 18
REMARK 465 ALA D 19
REMARK 465 LEU D 20
REMARK 465 SER D 21
REMARK 465 PRO D 22
REMARK 465 ALA D 23
REMARK 465 ALA D 24
REMARK 465 GLN D 25
REMARK 465 ALA D 26
REMARK 465 GLY D 27
REMARK 465 GLU D 28
REMARK 465 SER D 29
REMARK 465 LYS D 30
REMARK 465 GLY D 150
REMARK 465 GLY D 151
REMARK 465 ASP D 252
REMARK 465 GLY D 253
REMARK 465 THR D 254
REMARK 465 LEU D 255
REMARK 465 GLY D 256
REMARK 465 GLY D 257
REMARK 465 ALA D 275
REMARK 465 LYS D 276
REMARK 465 GLN D 277
REMARK 465 ARG D 278
REMARK 465 ASP D 279
REMARK 465 LEU D 280
REMARK 465 LEU D 281
REMARK 465 SER D 282
REMARK 465 MET D 283
REMARK 465 SER D 284
REMARK 465 GLY D 300
REMARK 465 SER D 301
REMARK 465 ALA D 310
REMARK 465 GLU D 311
REMARK 465 GLY D 312
REMARK 465 ALA D 723
REMARK 465 ALA D 724
REMARK 465 ALA D 725
REMARK 465 PRO D 726
REMARK 465 SER D 727
REMARK 465 ALA D 728
REMARK 465 TRP D 729
REMARK 465 SER D 730
REMARK 465 HIS D 731
REMARK 465 PRO D 732
REMARK 465 GLN D 733
REMARK 465 PHE D 734
REMARK 465 GLU D 735
REMARK 465 LYS D 736
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 LEU D 286 CG CD1 CD2
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 OG SER D 562 OG SER D 580 2.19
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 TYR D 478 C PRO D 479 N 0.192
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 88 -71.91 -93.10
REMARK 500 ASP A 188 -120.43 57.13
REMARK 500 LEU A 286 68.38 61.44
REMARK 500 THR A 373 -68.77 -92.56
REMARK 500 ASP A 466 -167.29 -163.14
REMARK 500 ASN A 474 -62.27 -97.48
REMARK 500 TRP A 476 -131.91 58.78
REMARK 500 TRP A 528 -64.27 -132.73
REMARK 500 SER A 559 -117.00 57.30
REMARK 500 LEU A 586 -5.30 74.88
REMARK 500 ALA A 628 173.76 175.56
REMARK 500 ASP A 706 38.12 39.49
REMARK 500 LEU B 88 -73.76 -100.86
REMARK 500 LEU B 130 -69.52 -123.71
REMARK 500 ASP B 188 -118.15 57.09
REMARK 500 THR B 373 -71.11 -97.68
REMARK 500 ASN B 474 -62.35 -99.96
REMARK 500 TRP B 476 -130.11 59.83
REMARK 500 PRO B 518 -179.03 -67.55
REMARK 500 TRP B 528 -63.39 -132.66
REMARK 500 SER B 559 -116.18 56.34
REMARK 500 LEU B 586 -4.03 78.60
REMARK 500 SER B 608 -168.67 -78.32
REMARK 500 ALA B 628 174.00 174.91
REMARK 500 LEU C 88 -71.17 -87.50
REMARK 500 ASP C 188 -121.72 57.31
REMARK 500 SER C 297 -169.30 -118.22
REMARK 500 LEU C 299 -178.78 -65.84
REMARK 500 SER C 301 -70.98 -73.76
REMARK 500 THR C 361 -64.10 -97.00
REMARK 500 THR C 373 -67.89 -92.13
REMARK 500 ASP C 466 -167.32 -161.96
REMARK 500 ASN C 474 -61.78 -99.50
REMARK 500 TRP C 476 -128.40 60.36
REMARK 500 TRP C 528 -63.64 -133.24
REMARK 500 SER C 559 -116.67 57.59
REMARK 500 LEU C 586 -4.65 77.34
REMARK 500 ALA C 628 176.99 176.46
REMARK 500 LEU D 88 -73.09 -85.48
REMARK 500 LEU D 130 -64.61 -120.93
REMARK 500 ALA D 142 163.88 179.81
REMARK 500 ASP D 188 -121.23 59.45
REMARK 500 THR D 373 -71.24 -98.48
REMARK 500 ASP D 466 -168.56 -162.94
REMARK 500 ASN D 474 -61.81 -101.13
REMARK 500 TRP D 476 -131.82 59.31
REMARK 500 TRP D 528 -63.19 -130.94
REMARK 500 SER D 559 -116.93 57.08
REMARK 500 LEU D 586 -5.29 78.66
REMARK 500 ALA D 628 175.41 175.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JRK RELATED DB: PDB
REMARK 900 5JRK IS THE SEMET-DERIVED FORM OF THIS PROTEIN
REMARK 900 RELATED ID: 5JQF RELATED DB: PDB
REMARK 900 5JQF (SPHINGOPYXIN I) IS THE SUBSTRATE FOR SPI-ISOP
DBREF 5JRL A 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
DBREF 5JRL B 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
DBREF 5JRL C 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
DBREF 5JRL D 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
SEQADV 5JRL MET A -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRL GLY A -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY A -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LEU A -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL VAL A -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO A -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ARG A -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY A -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ALA A 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL TRP A 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER A 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS A 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO A 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLN A 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PHE A 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLU A 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LYS A 736 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL MET B -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRL GLY B -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY B -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LEU B -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL VAL B -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO B -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ARG B -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY B -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ALA B 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL TRP B 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER B 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS B 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO B 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLN B 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PHE B 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLU B 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LYS B 736 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL MET C -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRL GLY C -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY C -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LEU C -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL VAL C -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO C -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ARG C -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY C -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ALA C 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL TRP C 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER C 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS C 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO C 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLN C 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PHE C 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLU C 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LYS C 736 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL MET D -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRL GLY D -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY D -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LEU D -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL VAL D -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO D -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ARG D -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLY D -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL ALA D 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL TRP D 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL SER D 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL HIS D 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PRO D 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLN D 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL PHE D 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL GLU D 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRL LYS D 736 UNP Q1GQ33 EXPRESSION TAG
SEQRES 1 A 756 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 756 LEU VAL PRO ARG GLY SER HIS MET LYS ILE ALA LEU ARG
SEQRES 3 A 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 A 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 A 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 A 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 A 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 A 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 A 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 A 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 A 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 A 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 A 756 VAL PRO VAL GLY LYS ALA ASP MET SER PHE PRO LEU GLY
SEQRES 14 A 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 A 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 A 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 A 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 A 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 A 756 GLY ASP THR THR ARG ILE MET ALA ARG PRO SER THR ASP
SEQRES 20 A 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 A 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 A 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 A 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 A 756 LEU LEU SER MET SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 A 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 A 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 A 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 A 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 A 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 A 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 A 756 SER LEU THR ARG CYS GLY PHE ASP GLY MET LEU ARG SER
SEQRES 32 A 756 ALA ILE CYS VAL GLU GLU GLY MET SER ARG PRO PRO ARG
SEQRES 33 A 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 A 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 A 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 A 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 A 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 A 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 A 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 A 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 A 756 SER LYS ASP LEU MET ASP ALA MET HIS ALA TRP LEU ARG
SEQRES 42 A 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 A 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 A 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 A 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MET VAL
SEQRES 46 A 756 ASN VAL THR VAL THR ASN SER LYS MET PHE ARG ALA ALA
SEQRES 47 A 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 A 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 A 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 A 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 A 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 A 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 A 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 A 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 A 756 MET ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 A 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 A 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 A 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 A 756 GLU LYS
SEQRES 1 B 756 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 756 LEU VAL PRO ARG GLY SER HIS MET LYS ILE ALA LEU ARG
SEQRES 3 B 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 B 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 B 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 B 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 B 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 B 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 B 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 B 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 B 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 B 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 B 756 VAL PRO VAL GLY LYS ALA ASP MET SER PHE PRO LEU GLY
SEQRES 14 B 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 B 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 B 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 B 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 B 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 B 756 GLY ASP THR THR ARG ILE MET ALA ARG PRO SER THR ASP
SEQRES 20 B 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 B 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 B 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 B 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 B 756 LEU LEU SER MET SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 B 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 B 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 B 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 B 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 B 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 B 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 B 756 SER LEU THR ARG CYS GLY PHE ASP GLY MET LEU ARG SER
SEQRES 32 B 756 ALA ILE CYS VAL GLU GLU GLY MET SER ARG PRO PRO ARG
SEQRES 33 B 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 B 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 B 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 B 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 B 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 B 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 B 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 B 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 B 756 SER LYS ASP LEU MET ASP ALA MET HIS ALA TRP LEU ARG
SEQRES 42 B 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 B 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 B 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 B 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MET VAL
SEQRES 46 B 756 ASN VAL THR VAL THR ASN SER LYS MET PHE ARG ALA ALA
SEQRES 47 B 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 B 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 B 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 B 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 B 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 B 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 B 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 B 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 B 756 MET ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 B 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 B 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 B 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 B 756 GLU LYS
SEQRES 1 C 756 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 756 LEU VAL PRO ARG GLY SER HIS MET LYS ILE ALA LEU ARG
SEQRES 3 C 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 C 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 C 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 C 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 C 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 C 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 C 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 C 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 C 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 C 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 C 756 VAL PRO VAL GLY LYS ALA ASP MET SER PHE PRO LEU GLY
SEQRES 14 C 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 C 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 C 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 C 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 C 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 C 756 GLY ASP THR THR ARG ILE MET ALA ARG PRO SER THR ASP
SEQRES 20 C 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 C 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 C 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 C 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 C 756 LEU LEU SER MET SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 C 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 C 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 C 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 C 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 C 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 C 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 C 756 SER LEU THR ARG CYS GLY PHE ASP GLY MET LEU ARG SER
SEQRES 32 C 756 ALA ILE CYS VAL GLU GLU GLY MET SER ARG PRO PRO ARG
SEQRES 33 C 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 C 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 C 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 C 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 C 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 C 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 C 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 C 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 C 756 SER LYS ASP LEU MET ASP ALA MET HIS ALA TRP LEU ARG
SEQRES 42 C 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 C 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 C 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 C 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MET VAL
SEQRES 46 C 756 ASN VAL THR VAL THR ASN SER LYS MET PHE ARG ALA ALA
SEQRES 47 C 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 C 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 C 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 C 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 C 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 C 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 C 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 C 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 C 756 MET ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 C 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 C 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 C 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 C 756 GLU LYS
SEQRES 1 D 756 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 756 LEU VAL PRO ARG GLY SER HIS MET LYS ILE ALA LEU ARG
SEQRES 3 D 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 D 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 D 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 D 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 D 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 D 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 D 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 D 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 D 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 D 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 D 756 VAL PRO VAL GLY LYS ALA ASP MET SER PHE PRO LEU GLY
SEQRES 14 D 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 D 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 D 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 D 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 D 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 D 756 GLY ASP THR THR ARG ILE MET ALA ARG PRO SER THR ASP
SEQRES 20 D 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 D 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 D 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 D 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 D 756 LEU LEU SER MET SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 D 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 D 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 D 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 D 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 D 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 D 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 D 756 SER LEU THR ARG CYS GLY PHE ASP GLY MET LEU ARG SER
SEQRES 32 D 756 ALA ILE CYS VAL GLU GLU GLY MET SER ARG PRO PRO ARG
SEQRES 33 D 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 D 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 D 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 D 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 D 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 D 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 D 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 D 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 D 756 SER LYS ASP LEU MET ASP ALA MET HIS ALA TRP LEU ARG
SEQRES 42 D 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 D 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 D 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 D 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MET VAL
SEQRES 46 D 756 ASN VAL THR VAL THR ASN SER LYS MET PHE ARG ALA ALA
SEQRES 47 D 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 D 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 D 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 D 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 D 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 D 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 D 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 D 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 D 756 MET ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 D 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 D 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 D 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 D 756 GLU LYS
HELIX 1 AA1 THR A 35 VAL A 42 1 8
HELIX 2 AA2 ASP A 188 ALA A 193 1 6
HELIX 3 AA3 ASP A 227 GLY A 233 1 7
HELIX 4 AA4 LEU A 280 SER A 284 5 5
HELIX 5 AA5 SER A 414 GLU A 419 1 6
HELIX 6 AA6 GLU A 471 TRP A 476 1 6
HELIX 7 AA7 PRO A 479 ARG A 486 1 8
HELIX 8 AA8 SER A 497 GLN A 500 5 4
HELIX 9 AA9 SER A 501 GLY A 514 1 14
HELIX 10 AB1 ASP A 519 TRP A 528 1 10
HELIX 11 AB2 TRP A 528 GLU A 545 1 18
HELIX 12 AB3 SER A 559 SER A 572 1 14
HELIX 13 AB4 GLU A 587 TYR A 591 5 5
HELIX 14 AB5 GLY A 594 GLY A 603 1 10
HELIX 15 AB6 ASN A 610 ALA A 618 1 9
HELIX 16 AB7 PRO A 619 VAL A 626 5 8
HELIX 17 AB8 SER A 638 ALA A 651 1 14
HELIX 18 AB9 LEU A 675 ASP A 696 1 22
HELIX 19 AC1 HIS A 707 ASN A 717 1 11
HELIX 20 AC2 THR B 35 VAL B 42 1 8
HELIX 21 AC3 ASP B 188 ALA B 193 1 6
HELIX 22 AC4 ASP B 227 ARG B 232 1 6
HELIX 23 AC5 SER B 414 GLU B 419 1 6
HELIX 24 AC6 GLU B 471 TRP B 476 1 6
HELIX 25 AC7 PRO B 479 ARG B 486 1 8
HELIX 26 AC8 SER B 497 GLN B 500 5 4
HELIX 27 AC9 SER B 501 GLY B 514 1 14
HELIX 28 AD1 ASP B 519 TRP B 528 1 10
HELIX 29 AD2 TRP B 528 GLU B 545 1 18
HELIX 30 AD3 SER B 559 SER B 572 1 14
HELIX 31 AD4 GLU B 587 TYR B 591 5 5
HELIX 32 AD5 GLY B 594 GLY B 603 1 10
HELIX 33 AD6 ASN B 610 ALA B 618 1 9
HELIX 34 AD7 ASN B 622 VAL B 626 5 5
HELIX 35 AD8 SER B 638 ALA B 651 1 14
HELIX 36 AD9 LEU B 675 LEU B 694 1 20
HELIX 37 AE1 ASP B 706 ASN B 717 1 12
HELIX 38 AE2 THR C 35 VAL C 42 1 8
HELIX 39 AE3 ASP C 188 ALA C 193 1 6
HELIX 40 AE4 ASP C 227 ARG C 232 1 6
HELIX 41 AE5 SER C 414 GLU C 419 1 6
HELIX 42 AE6 GLU C 471 TRP C 476 1 6
HELIX 43 AE7 PRO C 479 ARG C 486 1 8
HELIX 44 AE8 SER C 497 GLN C 500 5 4
HELIX 45 AE9 SER C 501 GLY C 514 1 14
HELIX 46 AF1 ASP C 519 TRP C 528 1 10
HELIX 47 AF2 TRP C 528 GLU C 545 1 18
HELIX 48 AF3 SER C 559 SER C 572 1 14
HELIX 49 AF4 GLU C 587 TYR C 591 5 5
HELIX 50 AF5 GLY C 594 GLY C 603 1 10
HELIX 51 AF6 ASN C 610 ALA C 618 1 9
HELIX 52 AF7 ASN C 622 VAL C 626 5 5
HELIX 53 AF8 SER C 638 ALA C 651 1 14
HELIX 54 AF9 LEU C 675 LEU C 694 1 20
HELIX 55 AG1 ASP C 706 ASN C 717 1 12
HELIX 56 AG2 THR D 35 THR D 41 1 7
HELIX 57 AG3 ASP D 188 ALA D 193 1 6
HELIX 58 AG4 ASP D 227 ARG D 232 1 6
HELIX 59 AG5 ARG D 416 ILE D 420 5 5
HELIX 60 AG6 GLU D 471 TRP D 476 1 6
HELIX 61 AG7 PRO D 479 ARG D 486 1 8
HELIX 62 AG8 SER D 497 GLN D 500 5 4
HELIX 63 AG9 SER D 501 GLY D 514 1 14
HELIX 64 AH1 ASP D 519 TRP D 528 1 10
HELIX 65 AH2 TRP D 528 GLU D 545 1 18
HELIX 66 AH3 SER D 559 SER D 572 1 14
HELIX 67 AH4 GLU D 587 ALA D 589 5 3
HELIX 68 AH5 GLY D 590 GLY D 603 1 14
HELIX 69 AH6 ASN D 610 ALA D 618 1 9
HELIX 70 AH7 ASN D 622 VAL D 626 5 5
HELIX 71 AH8 SER D 638 ALA D 651 1 14
HELIX 72 AH9 LEU D 675 ASP D 696 1 22
HELIX 73 AI1 ASP D 706 ASN D 717 1 12
SHEET 1 AA1 4 GLU A 44 LEU A 50 0
SHEET 2 AA1 4 LEU A 56 ASP A 65 -1 O GLU A 62 N GLU A 44
SHEET 3 AA1 4 LYS A 70 ASP A 79 -1 O VAL A 78 N ALA A 57
SHEET 4 AA1 4 THR A 85 VAL A 91 -1 O LEU A 89 N ILE A 75
SHEET 1 AA2 4 THR A 93 SER A 99 0
SHEET 2 AA2 4 TRP A 106 ASP A 111 -1 O LEU A 109 N LYS A 95
SHEET 3 AA2 4 GLN A 116 ILE A 121 -1 O ILE A 121 N TRP A 106
SHEET 4 AA2 4 LEU A 127 ILE A 131 -1 O LEU A 128 N ARG A 120
SHEET 1 AA3 2 VAL A 137 VAL A 139 0
SHEET 2 AA3 2 SER A 155 ILE A 157 -1 O SER A 155 N VAL A 139
SHEET 1 AA4 4 ASP A 161 TRP A 164 0
SHEET 2 AA4 4 LEU A 171 ALA A 178 -1 O SER A 174 N ASP A 161
SHEET 3 AA4 4 VAL A 204 ARG A 211 -1 O GLU A 205 N ARG A 177
SHEET 4 AA4 4 THR A 217 PRO A 224 -1 O ILE A 220 N PHE A 208
SHEET 1 AA5 9 ARG A 186 PHE A 187 0
SHEET 2 AA5 9 ALA C 654 TYR C 659 -1 O TYR C 659 N ARG A 186
SHEET 3 AA5 9 ALA C 629 VAL C 634 1 N GLN C 632 O SER C 658
SHEET 4 AA5 9 ALA C 577 GLY C 581 1 N ALA C 578 O ALA C 629
SHEET 5 AA5 9 ILE C 548 TYR C 558 1 N GLY C 557 O GLY C 581
SHEET 6 AA5 9 HIS C 454 VAL C 459 1 N VAL C 458 O ALA C 556
SHEET 7 AA5 9 VAL C 489 LEU C 493 1 O VAL C 489 N PRO C 455
SHEET 8 AA5 9 GLY C 440 LEU C 443 -1 N TYR C 441 O LEU C 492
SHEET 9 AA5 9 THR C 425 ALA C 427 -1 N ILE C 426 O VAL C 442
SHEET 1 AA6 4 VAL A 237 ARG A 240 0
SHEET 2 AA6 4 GLU A 243 ARG A 247 -1 O GLN A 245 N LEU A 238
SHEET 3 AA6 4 PHE A 261 ASN A 265 -1 O VAL A 262 N PHE A 246
SHEET 4 AA6 4 VAL A 271 ARG A 272 -1 O ARG A 272 N ALA A 263
SHEET 1 AA7 3 GLN A 293 SER A 297 0
SHEET 2 AA7 3 ARG A 303 THR A 308 -1 O ILE A 306 N SER A 295
SHEET 3 AA7 3 PRO A 314 VAL A 320 -1 O TYR A 317 N LEU A 305
SHEET 1 AA8 3 PHE A 322 ILE A 324 0
SHEET 2 AA8 3 VAL A 341 GLY A 347 -1 O ARG A 346 N ASP A 323
SHEET 3 AA8 3 TRP A 332 ARG A 334 -1 N LYS A 333 O VAL A 342
SHEET 1 AA9 4 PHE A 322 ILE A 324 0
SHEET 2 AA9 4 VAL A 341 GLY A 347 -1 O ARG A 346 N ASP A 323
SHEET 3 AA9 4 TYR A 353 ILE A 358 -1 O ILE A 358 N VAL A 341
SHEET 4 AA9 4 VAL A 363 ARG A 364 -1 O ARG A 364 N LEU A 357
SHEET 1 AB1 4 SER A 371 PHE A 377 0
SHEET 2 AB1 4 SER A 383 GLU A 389 -1 O GLU A 389 N SER A 371
SHEET 3 AB1 4 ARG A 396 ASP A 401 -1 O VAL A 400 N ALA A 384
SHEET 4 AB1 4 LYS A 406 PRO A 412 -1 O THR A 408 N ARG A 399
SHEET 1 AB2 9 THR A 425 VAL A 431 0
SHEET 2 AB2 9 TRP A 437 LEU A 443 -1 O VAL A 442 N ILE A 426
SHEET 3 AB2 9 VAL A 489 LEU A 493 -1 O LEU A 492 N TYR A 441
SHEET 4 AB2 9 HIS A 454 VAL A 459 1 N PRO A 455 O VAL A 489
SHEET 5 AB2 9 ILE A 548 TYR A 558 1 O ALA A 556 N VAL A 458
SHEET 6 AB2 9 ALA A 577 GLY A 581 1 O GLY A 581 N GLY A 557
SHEET 7 AB2 9 ALA A 629 VAL A 634 1 O ALA A 629 N ALA A 578
SHEET 8 AB2 9 THR A 655 TYR A 659 1 O SER A 658 N GLN A 632
SHEET 9 AB2 9 ARG C 186 PHE C 187 -1 O ARG C 186 N TYR A 659
SHEET 1 AB3 4 GLU B 44 LEU B 50 0
SHEET 2 AB3 4 LEU B 56 ALA B 64 -1 O GLU B 62 N GLU B 44
SHEET 3 AB3 4 PRO B 71 ASP B 79 -1 O VAL B 78 N ALA B 57
SHEET 4 AB3 4 THR B 85 VAL B 91 -1 O VAL B 91 N SER B 73
SHEET 1 AB4 4 THR B 93 SER B 99 0
SHEET 2 AB4 4 TRP B 106 ASP B 111 -1 O LEU B 109 N LYS B 95
SHEET 3 AB4 4 GLN B 116 ILE B 121 -1 O TYR B 119 N ALA B 108
SHEET 4 AB4 4 LEU B 127 ILE B 131 -1 O LEU B 128 N ARG B 120
SHEET 1 AB5 2 VAL B 137 VAL B 139 0
SHEET 2 AB5 2 SER B 155 ILE B 157 -1 O SER B 155 N VAL B 139
SHEET 1 AB6 4 ASP B 161 TRP B 164 0
SHEET 2 AB6 4 LEU B 171 ALA B 178 -1 O TRP B 172 N ASP B 163
SHEET 3 AB6 4 VAL B 204 ARG B 211 -1 O GLU B 205 N ARG B 177
SHEET 4 AB6 4 THR B 217 ARG B 223 -1 O ILE B 220 N PHE B 208
SHEET 1 AB7 4 LEU B 238 ARG B 240 0
SHEET 2 AB7 4 GLU B 243 ARG B 247 -1 O GLU B 243 N ARG B 240
SHEET 3 AB7 4 PHE B 261 ASN B 265 -1 O TRP B 264 N VAL B 244
SHEET 4 AB7 4 VAL B 271 ARG B 272 -1 O ARG B 272 N ALA B 263
SHEET 1 AB8 3 GLN B 293 SER B 297 0
SHEET 2 AB8 3 ARG B 303 THR B 308 -1 O ILE B 306 N SER B 295
SHEET 3 AB8 3 HIS B 315 VAL B 320 -1 O VAL B 320 N ARG B 303
SHEET 1 AB9 3 PHE B 322 ILE B 324 0
SHEET 2 AB9 3 VAL B 341 GLY B 347 -1 O ARG B 346 N ASP B 323
SHEET 3 AB9 3 TRP B 332 ARG B 334 -1 N LYS B 333 O VAL B 342
SHEET 1 AC1 4 PHE B 322 ILE B 324 0
SHEET 2 AC1 4 VAL B 341 GLY B 347 -1 O ARG B 346 N ASP B 323
SHEET 3 AC1 4 TYR B 353 ILE B 358 -1 O GLY B 354 N THR B 345
SHEET 4 AC1 4 VAL B 363 LEU B 366 -1 O ARG B 364 N LEU B 357
SHEET 1 AC2 4 SER B 371 PHE B 377 0
SHEET 2 AC2 4 SER B 383 GLU B 389 -1 O GLU B 389 N SER B 371
SHEET 3 AC2 4 ARG B 396 ASP B 401 -1 O VAL B 400 N ALA B 384
SHEET 4 AC2 4 LYS B 406 PRO B 412 -1 O THR B 408 N ARG B 399
SHEET 1 AC3 8 THR B 425 VAL B 431 0
SHEET 2 AC3 8 TRP B 437 LEU B 443 -1 O VAL B 442 N ILE B 426
SHEET 3 AC3 8 VAL B 489 LEU B 493 -1 O VAL B 490 N LEU B 443
SHEET 4 AC3 8 HIS B 454 VAL B 459 1 N PRO B 455 O VAL B 489
SHEET 5 AC3 8 ILE B 548 TYR B 558 1 O GLY B 554 N ALA B 456
SHEET 6 AC3 8 ALA B 577 GLY B 581 1 O GLY B 581 N GLY B 557
SHEET 7 AC3 8 ALA B 629 VAL B 634 1 O ALA B 629 N ALA B 578
SHEET 8 AC3 8 THR B 655 TYR B 659 1 O SER B 658 N GLN B 632
SHEET 1 AC4 4 GLU C 44 LEU C 50 0
SHEET 2 AC4 4 LEU C 56 ASP C 65 -1 O GLU C 62 N GLU C 44
SHEET 3 AC4 4 LYS C 70 ASP C 79 -1 O VAL C 78 N ALA C 57
SHEET 4 AC4 4 THR C 85 VAL C 91 -1 O VAL C 91 N SER C 73
SHEET 1 AC5 4 THR C 93 SER C 99 0
SHEET 2 AC5 4 TRP C 106 ASP C 111 -1 O LEU C 109 N LYS C 95
SHEET 3 AC5 4 GLN C 116 ILE C 121 -1 O TYR C 119 N ALA C 108
SHEET 4 AC5 4 LEU C 127 ILE C 131 -1 O LEU C 128 N ARG C 120
SHEET 1 AC6 2 VAL C 137 VAL C 139 0
SHEET 2 AC6 2 SER C 155 ILE C 157 -1 O SER C 155 N VAL C 139
SHEET 1 AC7 4 ASP C 161 TRP C 164 0
SHEET 2 AC7 4 LEU C 171 ALA C 178 -1 O TRP C 172 N ASP C 163
SHEET 3 AC7 4 VAL C 204 ARG C 211 -1 O GLU C 205 N ARG C 177
SHEET 4 AC7 4 THR C 217 PRO C 224 -1 O ILE C 220 N PHE C 208
SHEET 1 AC8 4 LEU C 238 ARG C 240 0
SHEET 2 AC8 4 GLU C 243 ILE C 248 -1 O GLN C 245 N LEU C 238
SHEET 3 AC8 4 GLU C 260 ASN C 265 -1 O GLU C 260 N ILE C 248
SHEET 4 AC8 4 VAL C 271 THR C 273 -1 O ARG C 272 N ALA C 263
SHEET 1 AC9 3 GLN C 293 SER C 297 0
SHEET 2 AC9 3 ARG C 303 THR C 308 -1 O GLU C 304 N SER C 297
SHEET 3 AC9 3 HIS C 315 VAL C 320 -1 O VAL C 320 N ARG C 303
SHEET 1 AD1 3 PHE C 322 ILE C 324 0
SHEET 2 AD1 3 VAL C 341 GLY C 347 -1 O ARG C 346 N ASP C 323
SHEET 3 AD1 3 TRP C 332 ARG C 334 -1 N LYS C 333 O VAL C 342
SHEET 1 AD2 4 PHE C 322 ILE C 324 0
SHEET 2 AD2 4 VAL C 341 GLY C 347 -1 O ARG C 346 N ASP C 323
SHEET 3 AD2 4 TYR C 353 ILE C 358 -1 O GLY C 354 N THR C 345
SHEET 4 AD2 4 VAL C 363 LEU C 366 -1 O ARG C 364 N LEU C 357
SHEET 1 AD3 4 SER C 371 PHE C 377 0
SHEET 2 AD3 4 SER C 383 GLU C 389 -1 O GLU C 389 N SER C 371
SHEET 3 AD3 4 ARG C 396 ASP C 401 -1 O VAL C 400 N ALA C 384
SHEET 4 AD3 4 LYS C 406 PRO C 412 -1 O THR C 408 N ARG C 399
SHEET 1 AD4 2 PHE C 430 VAL C 431 0
SHEET 2 AD4 2 TRP C 437 SER C 438 -1 O SER C 438 N PHE C 430
SHEET 1 AD5 4 GLU D 44 LEU D 50 0
SHEET 2 AD5 4 LEU D 56 ALA D 64 -1 O GLU D 62 N GLU D 44
SHEET 3 AD5 4 PRO D 71 ASP D 79 -1 O VAL D 78 N ALA D 57
SHEET 4 AD5 4 THR D 85 VAL D 91 -1 O LYS D 86 N ILE D 77
SHEET 1 AD6 4 THR D 93 SER D 99 0
SHEET 2 AD6 4 TRP D 106 ASP D 111 -1 O LEU D 109 N LYS D 95
SHEET 3 AD6 4 GLN D 116 ILE D 121 -1 O TYR D 119 N ALA D 108
SHEET 4 AD6 4 LEU D 127 ILE D 131 -1 O LEU D 128 N ARG D 120
SHEET 1 AD7 2 VAL D 137 VAL D 139 0
SHEET 2 AD7 2 SER D 155 ILE D 157 -1 O SER D 155 N VAL D 139
SHEET 1 AD8 4 ASP D 161 TRP D 164 0
SHEET 2 AD8 4 LEU D 171 ALA D 178 -1 O SER D 174 N ASP D 161
SHEET 3 AD8 4 VAL D 204 ARG D 211 -1 O PHE D 209 N TYR D 173
SHEET 4 AD8 4 THR D 217 PRO D 224 -1 O ILE D 220 N PHE D 208
SHEET 1 AD9 4 VAL D 237 ARG D 240 0
SHEET 2 AD9 4 GLU D 243 GLU D 249 -1 O GLN D 245 N LEU D 238
SHEET 3 AD9 4 PHE D 259 ASN D 265 -1 O TRP D 264 N VAL D 244
SHEET 4 AD9 4 VAL D 271 THR D 273 -1 O ARG D 272 N ALA D 263
SHEET 1 AE1 3 GLN D 293 SER D 297 0
SHEET 2 AE1 3 GLU D 304 THR D 308 -1 O ILE D 306 N SER D 295
SHEET 3 AE1 3 HIS D 315 ARG D 319 -1 O TYR D 317 N LEU D 305
SHEET 1 AE2 3 PHE D 322 ILE D 324 0
SHEET 2 AE2 3 VAL D 341 GLY D 347 -1 O ARG D 346 N ASP D 323
SHEET 3 AE2 3 TRP D 332 ARG D 334 -1 N LYS D 333 O VAL D 342
SHEET 1 AE3 4 PHE D 322 ILE D 324 0
SHEET 2 AE3 4 VAL D 341 GLY D 347 -1 O ARG D 346 N ASP D 323
SHEET 3 AE3 4 TYR D 353 ASP D 359 -1 O GLY D 354 N THR D 345
SHEET 4 AE3 4 GLY D 362 GLU D 365 -1 O ARG D 364 N LEU D 357
SHEET 1 AE4 4 SER D 371 PHE D 377 0
SHEET 2 AE4 4 SER D 383 GLU D 389 -1 O GLU D 389 N SER D 371
SHEET 3 AE4 4 ARG D 396 ASP D 401 -1 O VAL D 400 N ALA D 384
SHEET 4 AE4 4 LYS D 406 PRO D 412 -1 O THR D 408 N ARG D 399
SHEET 1 AE5 8 THR D 425 VAL D 431 0
SHEET 2 AE5 8 TRP D 437 LEU D 443 -1 O VAL D 442 N ILE D 426
SHEET 3 AE5 8 VAL D 489 LEU D 493 -1 O LEU D 492 N TYR D 441
SHEET 4 AE5 8 HIS D 454 VAL D 459 1 N PRO D 455 O VAL D 489
SHEET 5 AE5 8 ILE D 548 TYR D 558 1 O ALA D 556 N VAL D 458
SHEET 6 AE5 8 ALA D 577 GLY D 581 1 O GLY D 581 N GLY D 557
SHEET 7 AE5 8 ALA D 629 VAL D 634 1 O ALA D 629 N ALA D 578
SHEET 8 AE5 8 ALA D 654 TYR D 659 1 O SER D 658 N GLN D 632
SSBOND 1 CYS A 375 CYS A 386 1555 1555 2.03
SSBOND 2 CYS B 375 CYS B 386 1555 1555 2.03
SSBOND 3 CYS B 627 CYS B 722 1555 1555 2.03
SSBOND 4 CYS C 375 CYS C 386 1555 1555 2.03
SSBOND 5 CYS D 375 CYS D 386 1555 1555 2.03
SSBOND 6 CYS D 627 CYS D 722 1555 1555 2.03
CISPEP 1 GLY A 516 PRO A 517 0 -2.57
CISPEP 2 PRO A 517 PRO A 518 0 4.52
CISPEP 3 GLY B 516 PRO B 517 0 -0.98
CISPEP 4 PRO B 517 PRO B 518 0 -3.31
CISPEP 5 GLY C 516 PRO C 517 0 -1.21
CISPEP 6 PRO C 517 PRO C 518 0 4.22
CISPEP 7 GLY D 516 PRO D 517 0 -1.05
CISPEP 8 PRO D 517 PRO D 518 0 3.60
CRYST1 108.466 136.586 110.777 90.00 97.62 90.00 P 1 21 1 8
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 0.009219 0.000000 0.001233 0.00000
SCALE2 0.000000 0.007321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009108 0.00000
TER 5266 ARG A 721
TER 10477 CYS B 722
TER 15670 ASP C 720
TER 20896 CYS D 722
MASTER 684 0 0 73 164 0 0 620892 4 12 236
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