HEADER METAL BINDING PROTEIN 14-NOV-09 3KOY
TITLE CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH
TITLE 2 ORNITHINE (AEROBIC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ORNITHINE AMINOMUTASE E COMPONENT;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: D-ORNITHINE AMINOMUTASE S COMPONENT;
COMPND 7 CHAIN: E, F, G, H;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM STICKLANDII;
SOURCE 3 ORGANISM_TAXID: 1511;
SOURCE 4 GENE: ORAE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE STRATAGENE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: CLOSTRIDIUM STICKLANDII;
SOURCE 12 ORGANISM_TAXID: 1511;
SOURCE 13 GENE: ORAS;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE STRATAGENE;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET23D
KEYWDS D-ORNITHINE 4, 5 AMINOMUTASE (OAM), ORNITHINE COMPLEX, AEROBIC, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.WOLTHERS,C.W.LEVY,N.S.SCRUTTON,D.LEYS
REVDAT 5 21-FEB-24 3KOY 1 REMARK SEQADV LINK
REVDAT 4 17-JUL-19 3KOY 1 REMARK
REVDAT 3 24-OCT-12 3KOY 1 FORMUL VERSN
REVDAT 2 12-MAY-10 3KOY 1 JRNL
REVDAT 1 26-JAN-10 3KOY 0
JRNL AUTH K.R.WOLTHERS,C.LEVY,N.S.SCRUTTON,D.LEYS
JRNL TITL LARGE-SCALE DOMAIN DYNAMICS AND ADENOSYLCOBALAMIN
JRNL TITL 2 REORIENTATION ORCHESTRATE RADICAL CATALYSIS IN ORNITHINE
JRNL TITL 3 4,5-AMINOMUTASE.
JRNL REF J.BIOL.CHEM. V. 285 13942 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20106986
JRNL DOI 10.1074/JBC.M109.068908
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 84502
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 4264
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 60.3867 - 8.6919 0.97 2826 155 0.1474 0.1813
REMARK 3 2 8.6919 - 6.9022 1.00 2866 141 0.1357 0.1808
REMARK 3 3 6.9022 - 6.0306 0.97 2758 148 0.1556 0.2283
REMARK 3 4 6.0306 - 5.4796 0.98 2809 157 0.1680 0.2433
REMARK 3 5 5.4796 - 5.0871 0.98 2827 140 0.1572 0.2711
REMARK 3 6 5.0871 - 4.7873 0.99 2809 161 0.1505 0.2034
REMARK 3 7 4.7873 - 4.5476 0.98 2818 144 0.1364 0.2302
REMARK 3 8 4.5476 - 4.3497 0.98 2791 162 0.1365 0.1930
REMARK 3 9 4.3497 - 4.1823 0.99 2794 150 0.1415 0.2005
REMARK 3 10 4.1823 - 4.0380 0.97 2796 160 0.1499 0.2482
REMARK 3 11 4.0380 - 3.9118 0.98 2754 154 0.1527 0.2458
REMARK 3 12 3.9118 - 3.8000 0.97 2774 162 0.1612 0.2352
REMARK 3 13 3.8000 - 3.7000 0.97 2741 145 0.1583 0.2449
REMARK 3 14 3.7000 - 3.6097 0.95 2735 141 0.1644 0.2511
REMARK 3 15 3.6097 - 3.5277 0.96 2704 132 0.1676 0.2660
REMARK 3 16 3.5277 - 3.4526 0.94 2708 150 0.1832 0.2982
REMARK 3 17 3.4526 - 3.3835 0.95 2719 155 0.1917 0.2966
REMARK 3 18 3.3835 - 3.3197 0.93 2602 137 0.2077 0.3087
REMARK 3 19 3.3197 - 3.2604 0.91 2641 142 0.2111 0.3323
REMARK 3 20 3.2604 - 3.2052 0.93 2656 140 0.2187 0.3210
REMARK 3 21 3.2052 - 3.1535 0.90 2543 127 0.2217 0.3031
REMARK 3 22 3.1535 - 3.1049 0.90 2592 120 0.2253 0.3506
REMARK 3 23 3.1049 - 3.0593 0.90 2597 130 0.2280 0.3264
REMARK 3 24 3.0593 - 3.0162 0.89 2468 131 0.2301 0.3038
REMARK 3 25 3.0162 - 2.9754 0.87 2551 107 0.2281 0.3707
REMARK 3 26 2.9754 - 2.9368 0.89 2527 123 0.2380 0.3157
REMARK 3 27 2.9368 - 2.9001 0.88 2457 140 0.2562 0.3794
REMARK 3 28 2.9001 - 2.8651 0.84 2414 146 0.2441 0.3589
REMARK 3 29 2.8651 - 2.8318 0.87 2509 139 0.2571 0.3333
REMARK 3 30 2.8318 - 2.8000 0.88 2452 125 0.2367 0.3278
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 16.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.87000
REMARK 3 B22 (A**2) : 1.92000
REMARK 3 B33 (A**2) : -4.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.57000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.012 27116
REMARK 3 ANGLE : 1.418 36789
REMARK 3 CHIRALITY : 0.115 4116
REMARK 3 PLANARITY : 0.006 4753
REMARK 3 DIHEDRAL : 20.832 10207
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
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) : 1.072
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 120.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: A PROTEIN SOLUTION (8 MG/ML 4,5-OAM, 5
REMARK 280 MM 2-MERCAPTOETHANOL, 10 MM TRIS HCL PH 8.0, 2 MM PLP, AND 2 MM
REMARK 280 ADOCBL) WAS MIXED IN A 1:1 RATIO WITH PRECIPITANT SOLUTION [(0.1
REMARK 280 M TRIS HCL, PH 8.0, 0.2 M MGCL2, 25 % (WT/VOL) POLYETHYLENE
REMARK 280 GLYCOL 2000 MONO-METHYLETHER] UNDER RED LIGHT AT ROOM
REMARK 280 TEMPERATURE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
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 116.61000
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, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, C, G
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -182.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 LYS A 3
REMARK 465 ASP A 4
REMARK 465 HIS A 507
REMARK 465 SER A 508
REMARK 465 GLU A 588
REMARK 465 PRO A 589
REMARK 465 GLU A 590
REMARK 465 GLU A 741
REMARK 465 GLY A 742
REMARK 465 LYS A 743
REMARK 465 SER A 744
REMARK 465 GLU A 745
REMARK 465 ASP A 746
REMARK 465 PRO A 747
REMARK 465 ASN A 748
REMARK 465 SER A 749
REMARK 465 SER A 750
REMARK 465 SER A 751
REMARK 465 VAL A 752
REMARK 465 ASP A 753
REMARK 465 LYS A 754
REMARK 465 LEU A 755
REMARK 465 ALA A 756
REMARK 465 ALA A 757
REMARK 465 ALA A 758
REMARK 465 LEU A 759
REMARK 465 GLU A 760
REMARK 465 HIS A 761
REMARK 465 HIS A 762
REMARK 465 HIS A 763
REMARK 465 HIS A 764
REMARK 465 HIS A 765
REMARK 465 HIS A 766
REMARK 465 MET E 1
REMARK 465 LYS E 2
REMARK 465 ARG E 3
REMARK 465 ALA E 4
REMARK 465 ILE E 115
REMARK 465 PHE E 116
REMARK 465 LYS E 117
REMARK 465 GLY E 118
REMARK 465 GLY E 119
REMARK 465 VAL E 120
REMARK 465 LYS E 121
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 HIS B 507
REMARK 465 SER B 508
REMARK 465 GLU B 588
REMARK 465 PRO B 589
REMARK 465 GLU B 590
REMARK 465 GLU B 741
REMARK 465 GLY B 742
REMARK 465 LYS B 743
REMARK 465 SER B 744
REMARK 465 GLU B 745
REMARK 465 ASP B 746
REMARK 465 PRO B 747
REMARK 465 ASN B 748
REMARK 465 SER B 749
REMARK 465 SER B 750
REMARK 465 SER B 751
REMARK 465 VAL B 752
REMARK 465 ASP B 753
REMARK 465 LYS B 754
REMARK 465 LEU B 755
REMARK 465 ALA B 756
REMARK 465 ALA B 757
REMARK 465 ALA B 758
REMARK 465 LEU B 759
REMARK 465 GLU B 760
REMARK 465 HIS B 761
REMARK 465 HIS B 762
REMARK 465 HIS B 763
REMARK 465 HIS B 764
REMARK 465 HIS B 765
REMARK 465 HIS B 766
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 ARG F 3
REMARK 465 ALA F 4
REMARK 465 ILE F 115
REMARK 465 PHE F 116
REMARK 465 LYS F 117
REMARK 465 GLY F 118
REMARK 465 GLY F 119
REMARK 465 VAL F 120
REMARK 465 LYS F 121
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 LYS C 3
REMARK 465 ASP C 4
REMARK 465 HIS C 507
REMARK 465 SER C 508
REMARK 465 GLU C 588
REMARK 465 PRO C 589
REMARK 465 GLU C 590
REMARK 465 GLU C 741
REMARK 465 GLY C 742
REMARK 465 LYS C 743
REMARK 465 SER C 744
REMARK 465 GLU C 745
REMARK 465 ASP C 746
REMARK 465 PRO C 747
REMARK 465 ASN C 748
REMARK 465 SER C 749
REMARK 465 SER C 750
REMARK 465 SER C 751
REMARK 465 VAL C 752
REMARK 465 ASP C 753
REMARK 465 LYS C 754
REMARK 465 LEU C 755
REMARK 465 ALA C 756
REMARK 465 ALA C 757
REMARK 465 ALA C 758
REMARK 465 LEU C 759
REMARK 465 GLU C 760
REMARK 465 HIS C 761
REMARK 465 HIS C 762
REMARK 465 HIS C 763
REMARK 465 HIS C 764
REMARK 465 HIS C 765
REMARK 465 HIS C 766
REMARK 465 MET G 1
REMARK 465 LYS G 2
REMARK 465 ARG G 3
REMARK 465 ALA G 4
REMARK 465 ILE G 115
REMARK 465 PHE G 116
REMARK 465 LYS G 117
REMARK 465 GLY G 118
REMARK 465 GLY G 119
REMARK 465 VAL G 120
REMARK 465 LYS G 121
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 LYS D 3
REMARK 465 ASP D 4
REMARK 465 HIS D 507
REMARK 465 SER D 508
REMARK 465 GLU D 588
REMARK 465 PRO D 589
REMARK 465 GLU D 590
REMARK 465 GLU D 741
REMARK 465 GLY D 742
REMARK 465 LYS D 743
REMARK 465 SER D 744
REMARK 465 GLU D 745
REMARK 465 ASP D 746
REMARK 465 PRO D 747
REMARK 465 ASN D 748
REMARK 465 SER D 749
REMARK 465 SER D 750
REMARK 465 SER D 751
REMARK 465 VAL D 752
REMARK 465 ASP D 753
REMARK 465 LYS D 754
REMARK 465 LEU D 755
REMARK 465 ALA D 756
REMARK 465 ALA D 757
REMARK 465 ALA D 758
REMARK 465 LEU D 759
REMARK 465 GLU D 760
REMARK 465 HIS D 761
REMARK 465 HIS D 762
REMARK 465 HIS D 763
REMARK 465 HIS D 764
REMARK 465 HIS D 765
REMARK 465 HIS D 766
REMARK 465 MET H 1
REMARK 465 LYS H 2
REMARK 465 ARG H 3
REMARK 465 ALA H 4
REMARK 465 ILE H 115
REMARK 465 PHE H 116
REMARK 465 LYS H 117
REMARK 465 GLY H 118
REMARK 465 GLY H 119
REMARK 465 VAL H 120
REMARK 465 LYS H 121
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 GLU A 39 CG CD OE1 OE2
REMARK 470 LEU A 75 CG CD1 CD2
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 GLU A 504 CG CD OE1 OE2
REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 594 CG CD OE1 OE2
REMARK 470 GLU A 596 CG CD OE1 OE2
REMARK 470 GLU A 599 CG CD OE1 OE2
REMARK 470 LYS A 603 CG CD CE NZ
REMARK 470 LYS A 651 CG CD CE NZ
REMARK 470 GLU A 658 CG CD OE1 OE2
REMARK 470 LEU A 659 CG CD1 CD2
REMARK 470 LYS A 660 CG CD CE NZ
REMARK 470 ILE A 692 CG1 CG2 CD1
REMARK 470 LYS A 695 CG CD CE NZ
REMARK 470 LYS A 712 CG CD CE NZ
REMARK 470 MET A 739 CG SD CE
REMARK 470 ARG A 740 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 5 CG OD1 OD2
REMARK 470 LYS E 87 CG CD CE NZ
REMARK 470 ASP E 110 CG OD1 OD2
REMARK 470 GLN B 6 CG CD OE1 NE2
REMARK 470 ILE B 127 CG1 CG2 CD1
REMARK 470 GLU B 374 CG CD OE1 OE2
REMARK 470 GLU B 462 CG CD OE1 OE2
REMARK 470 GLU B 491 CG CD OE1 OE2
REMARK 470 LYS B 503 CG CD CE NZ
REMARK 470 GLU B 504 CG CD OE1 OE2
REMARK 470 GLU B 594 CG CD OE1 OE2
REMARK 470 GLU B 596 CG CD OE1 OE2
REMARK 470 GLU B 599 CG CD OE1 OE2
REMARK 470 ARG B 740 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 5 CG OD1 OD2
REMARK 470 LYS F 87 CG CD CE NZ
REMARK 470 GLU C 149 CG CD OE1 OE2
REMARK 470 GLU C 292 CG CD OE1 OE2
REMARK 470 GLU C 374 CG CD OE1 OE2
REMARK 470 GLU C 442 CG CD OE1 OE2
REMARK 470 GLU C 491 CG CD OE1 OE2
REMARK 470 GLU C 501 CG CD OE1 OE2
REMARK 470 LYS C 503 CG CD CE NZ
REMARK 470 GLU C 504 CG CD OE1 OE2
REMARK 470 GLU C 594 CG CD OE1 OE2
REMARK 470 GLU C 596 CG CD OE1 OE2
REMARK 470 GLU C 599 CG CD OE1 OE2
REMARK 470 ARG C 682 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 740 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 5 CG OD1 OD2
REMARK 470 LYS G 87 CG CD CE NZ
REMARK 470 ASP G 110 CG OD1 OD2
REMARK 470 LYS D 503 CG CD CE NZ
REMARK 470 GLU D 504 CG CD OE1 OE2
REMARK 470 GLU D 550 CG CD OE1 OE2
REMARK 470 GLU D 551 CG CD OE1 OE2
REMARK 470 GLU D 594 CG CD OE1 OE2
REMARK 470 GLU D 596 CG CD OE1 OE2
REMARK 470 GLU D 599 CG CD OE1 OE2
REMARK 470 GLU D 602 CG CD OE1 OE2
REMARK 470 GLU D 658 CG CD OE1 OE2
REMARK 470 GLU D 738 CG CD OE1 OE2
REMARK 470 ARG D 740 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 5 CG OD1 OD2
REMARK 470 LYS H 87 CG CD CE NZ
REMARK 470 ASP H 110 CG OD1 OD2
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 N23 B12 A 1801 C5' 5AD C 1500 2.04
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 PRO C 586 C - N - CA ANGL. DEV. = 9.9 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 GLN A 6 -177.16 117.38
REMARK 500 LEU A 7 99.37 78.97
REMARK 500 LYS A 12 166.56 -46.91
REMARK 500 ASP A 69 43.91 33.65
REMARK 500 ALA A 83 99.46 -174.50
REMARK 500 ASP A 117 49.58 -75.47
REMARK 500 ASN A 193 51.96 35.11
REMARK 500 ALA A 213 1.55 -68.24
REMARK 500 GLU A 306 -153.42 -146.62
REMARK 500 THR A 326 -105.87 -118.95
REMARK 500 ARG A 340 -31.42 -135.64
REMARK 500 PRO A 447 42.42 -84.12
REMARK 500 ASP A 461 103.52 175.87
REMARK 500 PRO A 468 -11.25 -48.79
REMARK 500 LEU A 471 -26.39 -37.43
REMARK 500 ASP A 493 54.88 -95.40
REMARK 500 THR A 502 34.28 -150.12
REMARK 500 GLU A 516 -48.97 -139.40
REMARK 500 PRO A 530 39.44 -63.56
REMARK 500 LYS A 546 -9.31 -58.56
REMARK 500 SER A 577 -151.63 -104.88
REMARK 500 ILE A 578 140.19 -172.35
REMARK 500 ILE A 601 37.06 -76.99
REMARK 500 GLU A 602 -55.56 -134.75
REMARK 500 GLU A 615 39.28 -98.43
REMARK 500 ILE A 633 -29.80 -39.78
REMARK 500 SER A 646 3.17 57.72
REMARK 500 VAL A 649 -57.67 -26.97
REMARK 500 GLU A 658 -9.04 -54.53
REMARK 500 ALA A 663 140.08 178.09
REMARK 500 HIS A 672 133.82 -38.53
REMARK 500 HIS A 676 -72.20 -75.48
REMARK 500 ARG A 693 47.52 -83.75
REMARK 500 ASP A 694 -7.52 -165.18
REMARK 500 PRO A 707 -7.23 -56.29
REMARK 500 VAL A 709 11.75 -66.91
REMARK 500 LYS A 712 38.00 -86.06
REMARK 500 GLN A 713 -2.50 -143.36
REMARK 500 GLU A 738 -62.85 -106.70
REMARK 500 ASP E 6 -71.88 34.18
REMARK 500 ILE E 94 -161.68 -110.73
REMARK 500 TYR E 108 -6.81 90.58
REMARK 500 GLN B 6 -171.23 -176.92
REMARK 500 LEU B 7 105.59 84.95
REMARK 500 ASN B 40 58.14 30.58
REMARK 500 ASP B 69 23.45 48.14
REMARK 500 ALA B 83 104.45 -178.59
REMARK 500 THR B 123 53.68 -158.66
REMARK 500 ASP B 168 -71.23 -37.21
REMARK 500 PRO B 275 76.11 -63.66
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
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 B12 A1801 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 618 NE2
REMARK 620 2 B12 A1801 N21 82.0
REMARK 620 3 B12 A1801 N22 75.7 86.0
REMARK 620 4 B12 A1801 N23 99.1 177.5 96.5
REMARK 620 5 B12 A1801 N24 88.5 85.4 162.9 92.3
REMARK 620 6 5AD C1500 C5' 159.3 118.6 101.4 60.5 95.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 B12 C1801 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 5AD A1500 C5'
REMARK 620 2 B12 C1801 N21 100.5
REMARK 620 3 B12 C1801 N22 106.9 87.8
REMARK 620 4 B12 C1801 N23 79.6 175.2 96.8
REMARK 620 5 B12 C1801 N24 90.9 83.4 161.3 91.8
REMARK 620 6 HIS C 618 NE2 170.0 81.3 83.0 97.8 79.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 B12 B1801 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 618 NE2
REMARK 620 2 B12 B1801 N21 87.7
REMARK 620 3 B12 B1801 N22 79.4 87.0
REMARK 620 4 B12 B1801 N23 95.7 175.6 96.2
REMARK 620 5 B12 B1801 N24 83.9 85.2 161.9 92.6
REMARK 620 6 5AD D1500 C5' 160.6 99.2 118.8 76.6 78.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 B12 D1801 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 5AD B1500 C5'
REMARK 620 2 B12 D1801 N21 104.9
REMARK 620 3 B12 D1801 N22 116.8 85.7
REMARK 620 4 B12 D1801 N23 73.6 177.2 97.1
REMARK 620 5 B12 D1801 N24 81.4 85.1 161.3 92.3
REMARK 620 6 HIS D 618 NE2 163.9 87.2 74.0 93.8 89.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD C 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z97 C 767
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 D 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z97 A 767
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 C 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z97 B 767
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD D 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z97 D 767
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KOW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE BACKSOAKED COMPLEX
REMARK 900 RELATED ID: 3KOX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH 2,4-
REMARK 900 DIAMINOBUTYRATE (ANAEROBIC)
REMARK 900 RELATED ID: 3KOZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH
REMARK 900 ORNITHINE (ANAEROBIC)
REMARK 900 RELATED ID: 3KP0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH 2,4-
REMARK 900 DIAMINOBUTYRATE (DAB) (AEROBIC)
REMARK 900 RELATED ID: 3KP1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE (RESTING STATE)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRUCTURE DOES NOT CONTAIN RESIDUES GLY220 TO ASP222 OF ORAE
REMARK 999 PRESENT IN THE UNP SEQUENCE. WE DO NOT FIND ANY EVIDENCE FOR THESE
REMARK 999 RESIDUES FROM CLOSTRIDIUM STICKLANDII GENOMIC DNA SEQUENCING OR BY
REMARK 999 ALIGNMENT BETWEEN THE ORAE PROTEIN SEQUENCES FROM CLOSTRIDIUM
REMARK 999 STICKLANDII AND CLOSTRIDIUM DIFFICILE (ACCESSION NUMBER ZP_05349629;
REMARK 999 79% SEQUENCE IDENTITY) WHICH ALSO SHOWS THAT THE CORRESPONDING
REMARK 999 ORAE CODING SEQUENCE FROM THE LATTER ORGANISM ALSO DOES NOT CONTAIN
REMARK 999 THE THREE AMINO ACID GID INSERT (A SIMILAR CONCLUSION CAN BE
REMARK 999 REACHED BY ALIGNMENT WITH VARIOUS THERMOANAEROBACTER SP)
DBREF 3KOY A 1 743 UNP Q8VPJ5 Q8VPJ5_CLOST 1 743
DBREF 3KOY E 1 121 UNP Q8VPJ6 Q8VPJ6_CLOST 1 121
DBREF 3KOY B 1 743 UNP Q8VPJ5 Q8VPJ5_CLOST 1 743
DBREF 3KOY F 1 121 UNP Q8VPJ6 Q8VPJ6_CLOST 1 121
DBREF 3KOY C 1 743 UNP Q8VPJ5 Q8VPJ5_CLOST 1 743
DBREF 3KOY G 1 121 UNP Q8VPJ6 Q8VPJ6_CLOST 1 121
DBREF 3KOY D 1 743 UNP Q8VPJ5 Q8VPJ5_CLOST 1 743
DBREF 3KOY H 1 121 UNP Q8VPJ6 Q8VPJ6_CLOST 1 121
SEQADV 3KOY A UNP Q8VPJ5 ILE 218 SEE REMARK 999
SEQADV 3KOY A UNP Q8VPJ5 ASP 219 SEE REMARK 999
SEQADV 3KOY A UNP Q8VPJ5 GLY 220 SEE REMARK 999
SEQADV 3KOY SER A 744 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU A 745 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP A 746 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY PRO A 747 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASN A 748 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER A 749 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER A 750 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER A 751 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY VAL A 752 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP A 753 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LYS A 754 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU A 755 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA A 756 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA A 757 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA A 758 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU A 759 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU A 760 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 761 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 762 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 763 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 764 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 765 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS A 766 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY B UNP Q8VPJ5 ILE 218 SEE REMARK 999
SEQADV 3KOY B UNP Q8VPJ5 ASP 219 SEE REMARK 999
SEQADV 3KOY B UNP Q8VPJ5 GLY 220 SEE REMARK 999
SEQADV 3KOY SER B 744 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU B 745 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP B 746 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY PRO B 747 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASN B 748 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER B 749 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER B 750 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER B 751 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY VAL B 752 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP B 753 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LYS B 754 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU B 755 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA B 756 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA B 757 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA B 758 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU B 759 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU B 760 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 761 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 762 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 763 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 764 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 765 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS B 766 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY C UNP Q8VPJ5 ILE 218 SEE REMARK 999
SEQADV 3KOY C UNP Q8VPJ5 ASP 219 SEE REMARK 999
SEQADV 3KOY C UNP Q8VPJ5 GLY 220 SEE REMARK 999
SEQADV 3KOY SER C 744 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU C 745 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP C 746 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY PRO C 747 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASN C 748 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER C 749 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER C 750 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER C 751 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY VAL C 752 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP C 753 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LYS C 754 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU C 755 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA C 756 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA C 757 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA C 758 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU C 759 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU C 760 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 761 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 762 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 763 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 764 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 765 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS C 766 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY D UNP Q8VPJ5 ILE 218 SEE REMARK 999
SEQADV 3KOY D UNP Q8VPJ5 ASP 219 SEE REMARK 999
SEQADV 3KOY D UNP Q8VPJ5 GLY 220 SEE REMARK 999
SEQADV 3KOY SER D 744 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU D 745 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP D 746 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY PRO D 747 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASN D 748 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER D 749 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER D 750 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY SER D 751 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY VAL D 752 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ASP D 753 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LYS D 754 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU D 755 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA D 756 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA D 757 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY ALA D 758 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY LEU D 759 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY GLU D 760 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 761 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 762 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 763 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 764 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 765 UNP Q8VPJ5 EXPRESSION TAG
SEQADV 3KOY HIS D 766 UNP Q8VPJ5 EXPRESSION TAG
SEQRES 1 A 763 MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU
SEQRES 2 A 763 ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR
SEQRES 3 A 763 PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU
SEQRES 4 A 763 ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER
SEQRES 5 A 763 THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS
SEQRES 6 A 763 TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE
SEQRES 7 A 763 THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE
SEQRES 8 A 763 ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS
SEQRES 9 A 763 ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP
SEQRES 10 A 763 GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL
SEQRES 11 A 763 PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA
SEQRES 12 A 763 LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN
SEQRES 13 A 763 TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE
SEQRES 14 A 763 ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS
SEQRES 15 A 763 GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN
SEQRES 16 A 763 MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR
SEQRES 17 A 763 ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA
SEQRES 18 A 763 HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL
SEQRES 19 A 763 MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE
SEQRES 20 A 763 PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS
SEQRES 21 A 763 LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER
SEQRES 22 A 763 MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU
SEQRES 23 A 763 MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR
SEQRES 24 A 763 LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR
SEQRES 25 A 763 HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA
SEQRES 26 A 763 ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN
SEQRES 27 A 763 VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR
SEQRES 28 A 763 ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP
SEQRES 29 A 763 MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR
SEQRES 30 A 763 VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU
SEQRES 31 A 763 GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU
SEQRES 32 A 763 GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG
SEQRES 33 A 763 ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE
SEQRES 34 A 763 GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET
SEQRES 35 A 763 ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS
SEQRES 36 A 763 GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU
SEQRES 37 A 763 ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL
SEQRES 38 A 763 TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL
SEQRES 39 A 763 ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET
SEQRES 40 A 763 ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL
SEQRES 41 A 763 LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA
SEQRES 42 A 763 GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU
SEQRES 43 A 763 GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU
SEQRES 44 A 763 ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO
SEQRES 45 A 763 PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU
SEQRES 46 A 763 PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE
SEQRES 47 A 763 GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY
SEQRES 48 A 763 GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP
SEQRES 49 A 763 ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL
SEQRES 50 A 763 HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL
SEQRES 51 A 763 ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA
SEQRES 52 A 763 SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN
SEQRES 53 A 763 MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE
SEQRES 54 A 763 ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL
SEQRES 55 A 763 THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY
SEQRES 56 A 763 PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE
SEQRES 57 A 763 LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER
SEQRES 58 A 763 GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA
SEQRES 59 A 763 ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 121 MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS
SEQRES 2 E 121 LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE
SEQRES 3 E 121 TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP
SEQRES 4 E 121 LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER
SEQRES 5 E 121 VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS
SEQRES 6 E 121 ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY
SEQRES 7 E 121 LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU
SEQRES 8 E 121 LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER
SEQRES 9 E 121 GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS
SEQRES 10 E 121 GLY GLY VAL LYS
SEQRES 1 B 763 MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU
SEQRES 2 B 763 ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR
SEQRES 3 B 763 PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU
SEQRES 4 B 763 ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER
SEQRES 5 B 763 THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS
SEQRES 6 B 763 TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE
SEQRES 7 B 763 THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE
SEQRES 8 B 763 ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS
SEQRES 9 B 763 ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP
SEQRES 10 B 763 GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL
SEQRES 11 B 763 PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA
SEQRES 12 B 763 LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN
SEQRES 13 B 763 TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE
SEQRES 14 B 763 ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS
SEQRES 15 B 763 GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN
SEQRES 16 B 763 MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR
SEQRES 17 B 763 ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA
SEQRES 18 B 763 HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL
SEQRES 19 B 763 MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE
SEQRES 20 B 763 PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS
SEQRES 21 B 763 LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER
SEQRES 22 B 763 MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU
SEQRES 23 B 763 MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR
SEQRES 24 B 763 LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR
SEQRES 25 B 763 HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA
SEQRES 26 B 763 ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN
SEQRES 27 B 763 VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR
SEQRES 28 B 763 ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP
SEQRES 29 B 763 MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR
SEQRES 30 B 763 VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU
SEQRES 31 B 763 GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU
SEQRES 32 B 763 GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG
SEQRES 33 B 763 ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE
SEQRES 34 B 763 GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET
SEQRES 35 B 763 ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS
SEQRES 36 B 763 GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU
SEQRES 37 B 763 ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL
SEQRES 38 B 763 TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL
SEQRES 39 B 763 ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET
SEQRES 40 B 763 ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL
SEQRES 41 B 763 LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA
SEQRES 42 B 763 GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU
SEQRES 43 B 763 GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU
SEQRES 44 B 763 ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO
SEQRES 45 B 763 PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU
SEQRES 46 B 763 PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE
SEQRES 47 B 763 GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY
SEQRES 48 B 763 GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP
SEQRES 49 B 763 ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL
SEQRES 50 B 763 HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL
SEQRES 51 B 763 ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA
SEQRES 52 B 763 SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN
SEQRES 53 B 763 MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE
SEQRES 54 B 763 ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL
SEQRES 55 B 763 THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY
SEQRES 56 B 763 PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE
SEQRES 57 B 763 LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER
SEQRES 58 B 763 GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA
SEQRES 59 B 763 ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 121 MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS
SEQRES 2 F 121 LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE
SEQRES 3 F 121 TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP
SEQRES 4 F 121 LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER
SEQRES 5 F 121 VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS
SEQRES 6 F 121 ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY
SEQRES 7 F 121 LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU
SEQRES 8 F 121 LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER
SEQRES 9 F 121 GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS
SEQRES 10 F 121 GLY GLY VAL LYS
SEQRES 1 C 763 MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU
SEQRES 2 C 763 ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR
SEQRES 3 C 763 PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU
SEQRES 4 C 763 ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER
SEQRES 5 C 763 THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS
SEQRES 6 C 763 TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE
SEQRES 7 C 763 THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE
SEQRES 8 C 763 ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS
SEQRES 9 C 763 ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP
SEQRES 10 C 763 GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL
SEQRES 11 C 763 PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA
SEQRES 12 C 763 LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN
SEQRES 13 C 763 TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE
SEQRES 14 C 763 ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS
SEQRES 15 C 763 GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN
SEQRES 16 C 763 MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR
SEQRES 17 C 763 ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA
SEQRES 18 C 763 HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL
SEQRES 19 C 763 MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE
SEQRES 20 C 763 PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS
SEQRES 21 C 763 LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER
SEQRES 22 C 763 MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU
SEQRES 23 C 763 MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR
SEQRES 24 C 763 LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR
SEQRES 25 C 763 HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA
SEQRES 26 C 763 ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN
SEQRES 27 C 763 VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR
SEQRES 28 C 763 ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP
SEQRES 29 C 763 MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR
SEQRES 30 C 763 VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU
SEQRES 31 C 763 GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU
SEQRES 32 C 763 GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG
SEQRES 33 C 763 ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE
SEQRES 34 C 763 GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET
SEQRES 35 C 763 ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS
SEQRES 36 C 763 GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU
SEQRES 37 C 763 ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL
SEQRES 38 C 763 TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL
SEQRES 39 C 763 ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET
SEQRES 40 C 763 ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL
SEQRES 41 C 763 LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA
SEQRES 42 C 763 GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU
SEQRES 43 C 763 GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU
SEQRES 44 C 763 ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO
SEQRES 45 C 763 PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU
SEQRES 46 C 763 PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE
SEQRES 47 C 763 GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY
SEQRES 48 C 763 GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP
SEQRES 49 C 763 ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL
SEQRES 50 C 763 HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL
SEQRES 51 C 763 ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA
SEQRES 52 C 763 SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN
SEQRES 53 C 763 MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE
SEQRES 54 C 763 ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL
SEQRES 55 C 763 THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY
SEQRES 56 C 763 PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE
SEQRES 57 C 763 LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER
SEQRES 58 C 763 GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA
SEQRES 59 C 763 ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 121 MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS
SEQRES 2 G 121 LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE
SEQRES 3 G 121 TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP
SEQRES 4 G 121 LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER
SEQRES 5 G 121 VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS
SEQRES 6 G 121 ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY
SEQRES 7 G 121 LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU
SEQRES 8 G 121 LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER
SEQRES 9 G 121 GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS
SEQRES 10 G 121 GLY GLY VAL LYS
SEQRES 1 D 763 MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU
SEQRES 2 D 763 ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR
SEQRES 3 D 763 PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU
SEQRES 4 D 763 ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER
SEQRES 5 D 763 THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS
SEQRES 6 D 763 TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE
SEQRES 7 D 763 THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE
SEQRES 8 D 763 ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS
SEQRES 9 D 763 ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP
SEQRES 10 D 763 GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL
SEQRES 11 D 763 PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA
SEQRES 12 D 763 LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN
SEQRES 13 D 763 TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE
SEQRES 14 D 763 ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS
SEQRES 15 D 763 GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN
SEQRES 16 D 763 MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR
SEQRES 17 D 763 ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA
SEQRES 18 D 763 HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL
SEQRES 19 D 763 MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE
SEQRES 20 D 763 PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS
SEQRES 21 D 763 LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER
SEQRES 22 D 763 MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU
SEQRES 23 D 763 MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR
SEQRES 24 D 763 LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR
SEQRES 25 D 763 HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA
SEQRES 26 D 763 ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN
SEQRES 27 D 763 VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR
SEQRES 28 D 763 ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP
SEQRES 29 D 763 MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR
SEQRES 30 D 763 VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU
SEQRES 31 D 763 GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU
SEQRES 32 D 763 GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG
SEQRES 33 D 763 ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE
SEQRES 34 D 763 GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET
SEQRES 35 D 763 ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS
SEQRES 36 D 763 GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU
SEQRES 37 D 763 ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL
SEQRES 38 D 763 TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL
SEQRES 39 D 763 ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET
SEQRES 40 D 763 ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL
SEQRES 41 D 763 LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA
SEQRES 42 D 763 GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU
SEQRES 43 D 763 GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU
SEQRES 44 D 763 ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO
SEQRES 45 D 763 PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU
SEQRES 46 D 763 PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE
SEQRES 47 D 763 GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY
SEQRES 48 D 763 GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP
SEQRES 49 D 763 ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL
SEQRES 50 D 763 HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL
SEQRES 51 D 763 ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA
SEQRES 52 D 763 SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN
SEQRES 53 D 763 MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE
SEQRES 54 D 763 ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL
SEQRES 55 D 763 THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY
SEQRES 56 D 763 PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE
SEQRES 57 D 763 LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER
SEQRES 58 D 763 GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA
SEQRES 59 D 763 ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 121 MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS
SEQRES 2 H 121 LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE
SEQRES 3 H 121 TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP
SEQRES 4 H 121 LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER
SEQRES 5 H 121 VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS
SEQRES 6 H 121 ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY
SEQRES 7 H 121 LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU
SEQRES 8 H 121 LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER
SEQRES 9 H 121 GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS
SEQRES 10 H 121 GLY GLY VAL LYS
HET B12 A1801 91
HET Z97 A 767 24
HET 5AD A1500 18
HET 5AD B1500 18
HET Z97 B 767 24
HET B12 B1801 91
HET 5AD C1500 18
HET Z97 C 767 24
HET B12 C1801 91
HET B12 D1801 91
HET 5AD D1500 18
HET Z97 D 767 24
HETNAM B12 COBALAMIN
HETNAM Z97 (E)-N~5~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 Z97 METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-ORNITHINE
HETNAM 5AD 5'-DEOXYADENOSINE
FORMUL 9 B12 4(C62 H89 CO N13 O14 P 2+)
FORMUL 10 Z97 4(C13 H20 N3 O7 P)
FORMUL 11 5AD 4(C10 H13 N5 O3)
HELIX 1 1 ASP A 14 LEU A 19 1 6
HELIX 2 2 LYS A 20 TYR A 25 5 6
HELIX 3 3 LEU A 61 GLY A 68 5 8
HELIX 4 4 ARG A 86 HIS A 100 1 15
HELIX 5 5 GLY A 112 TYR A 116 5 5
HELIX 6 6 THR A 133 GLY A 152 1 20
HELIX 7 7 ALA A 165 GLU A 176 1 12
HELIX 8 8 ASP A 184 ASN A 193 1 10
HELIX 9 9 ASN A 195 ALA A 213 1 19
HELIX 10 10 ALA A 224 THR A 230 1 7
HELIX 11 11 GLU A 233 LYS A 236 5 4
HELIX 12 12 VAL A 237 GLY A 256 1 20
HELIX 13 13 PRO A 275 PHE A 291 1 17
HELIX 14 14 SER A 308 THR A 326 1 19
HELIX 15 15 TRP A 344 MET A 362 1 19
HELIX 16 16 GLY A 364 ASP A 367 5 4
HELIX 17 17 GLY A 375 ALA A 398 1 24
HELIX 18 18 GLY A 400 GLN A 407 1 8
HELIX 19 19 ASP A 461 VAL A 465 5 5
HELIX 20 20 SER A 469 ASP A 473 5 5
HELIX 21 21 VAL A 479 ILE A 483 5 5
HELIX 22 22 ASN A 494 GLU A 501 1 8
HELIX 23 23 THR A 502 ARG A 506 5 5
HELIX 24 24 SER A 532 LYS A 546 1 15
HELIX 25 25 SER A 593 THR A 604 1 12
HELIX 26 26 SER A 619 VAL A 625 1 7
HELIX 27 27 ILE A 626 GLY A 631 5 6
HELIX 28 28 GLY A 632 GLY A 637 5 6
HELIX 29 29 PRO A 648 LYS A 660 1 13
HELIX 30 30 SER A 671 ASP A 673 5 3
HELIX 31 31 ASP A 674 GLU A 689 1 16
HELIX 32 32 PRO A 707 LYS A 712 1 6
HELIX 33 33 LYS A 724 LYS A 735 1 12
HELIX 34 34 LYS A 735 ARG A 740 1 6
HELIX 35 35 ASP E 6 ALA E 12 1 7
HELIX 36 36 SER E 18 LYS E 43 1 26
HELIX 37 37 THR E 46 MET E 57 1 12
HELIX 38 38 SER E 60 ARG E 74 1 15
HELIX 39 39 LEU E 76 LYS E 79 5 4
HELIX 40 40 GLY E 80 LYS E 92 1 13
HELIX 41 41 SER E 95 SER E 104 1 10
HELIX 42 42 TYR E 108 ILE E 113 1 6
HELIX 43 43 ASP B 14 LEU B 19 1 6
HELIX 44 44 ASP B 21 TYR B 25 5 5
HELIX 45 45 LEU B 61 GLY B 68 5 8
HELIX 46 46 ARG B 86 GLY B 101 1 16
HELIX 47 47 GLY B 112 TYR B 116 5 5
HELIX 48 48 THR B 133 GLY B 152 1 20
HELIX 49 49 ALA B 165 GLU B 176 1 12
HELIX 50 50 ASP B 184 TYR B 191 1 8
HELIX 51 51 ASN B 195 ALA B 213 1 19
HELIX 52 52 HIS B 225 ALA B 231 1 7
HELIX 53 53 GLU B 233 LYS B 236 5 4
HELIX 54 54 VAL B 237 GLY B 256 1 20
HELIX 55 55 LYS B 258 SER B 260 5 3
HELIX 56 56 PRO B 275 PHE B 291 1 17
HELIX 57 57 SER B 308 THR B 326 1 19
HELIX 58 58 TRP B 344 MET B 362 1 19
HELIX 59 59 GLY B 364 ASP B 367 5 4
HELIX 60 60 GLY B 375 ALA B 398 1 24
HELIX 61 61 GLY B 400 GLN B 407 1 8
HELIX 62 62 SER B 469 ASP B 473 5 5
HELIX 63 63 VAL B 479 ILE B 483 5 5
HELIX 64 64 ASN B 494 GLU B 501 1 8
HELIX 65 65 THR B 502 ARG B 506 5 5
HELIX 66 66 SER B 532 LYS B 546 1 15
HELIX 67 67 ASN B 581 LEU B 583 5 3
HELIX 68 68 SER B 593 THR B 604 1 12
HELIX 69 69 SER B 619 VAL B 625 1 7
HELIX 70 70 ILE B 626 GLY B 631 5 6
HELIX 71 71 GLY B 632 GLY B 637 5 6
HELIX 72 72 PRO B 648 LEU B 659 1 12
HELIX 73 73 ASP B 674 GLU B 689 1 16
HELIX 74 74 LYS B 724 GLU B 738 1 15
HELIX 75 75 ASP F 6 ARG F 11 1 6
HELIX 76 76 ALA F 12 LEU F 14 5 3
HELIX 77 77 SER F 18 LYS F 43 1 26
HELIX 78 78 THR F 46 MET F 57 1 12
HELIX 79 79 SER F 60 ARG F 74 1 15
HELIX 80 80 LEU F 76 LYS F 79 5 4
HELIX 81 81 GLY F 80 ASN F 93 1 14
HELIX 82 82 SER F 95 SER F 104 1 10
HELIX 83 83 TYR F 108 ILE F 113 1 6
HELIX 84 84 ASP C 14 LYS C 20 1 7
HELIX 85 85 ASP C 21 TYR C 25 5 5
HELIX 86 86 LEU C 61 GLY C 68 5 8
HELIX 87 87 ARG C 86 HIS C 100 1 15
HELIX 88 88 GLY C 112 TYR C 116 5 5
HELIX 89 89 THR C 133 GLY C 152 1 20
HELIX 90 90 ALA C 165 GLU C 176 1 12
HELIX 91 91 ASP C 184 ASN C 193 1 10
HELIX 92 92 ASN C 195 ALA C 213 1 19
HELIX 93 93 ALA C 224 ALA C 231 1 8
HELIX 94 94 VAL C 237 GLY C 256 1 20
HELIX 95 95 PRO C 275 PHE C 291 1 17
HELIX 96 96 SER C 308 THR C 326 1 19
HELIX 97 97 TRP C 344 MET C 362 1 19
HELIX 98 98 ASP C 363 ASP C 367 5 5
HELIX 99 99 GLY C 375 ALA C 398 1 24
HELIX 100 100 GLY C 400 GLN C 407 1 8
HELIX 101 101 ASP C 461 VAL C 465 5 5
HELIX 102 102 SER C 469 ASP C 473 5 5
HELIX 103 103 VAL C 479 ILE C 483 5 5
HELIX 104 104 ASN C 494 GLU C 501 1 8
HELIX 105 105 SER C 532 LYS C 546 1 15
HELIX 106 106 ASN C 581 LEU C 583 5 3
HELIX 107 107 SER C 593 THR C 604 1 12
HELIX 108 108 SER C 619 VAL C 625 1 7
HELIX 109 109 ILE C 626 GLY C 631 5 6
HELIX 110 110 GLY C 632 GLY C 637 5 6
HELIX 111 111 PRO C 648 LEU C 659 1 12
HELIX 112 112 SER C 671 ASP C 673 5 3
HELIX 113 113 ASP C 674 GLU C 689 1 16
HELIX 114 114 ILE C 692 ILE C 696 5 5
HELIX 115 115 THR C 706 GLN C 713 1 8
HELIX 116 116 LYS C 724 ARG C 740 1 17
HELIX 117 117 ASP G 6 ARG G 11 1 6
HELIX 118 118 ALA G 12 ALA G 15 5 4
HELIX 119 119 SER G 18 LYS G 43 1 26
HELIX 120 120 THR G 46 ARG G 56 1 11
HELIX 121 121 SER G 60 ARG G 74 1 15
HELIX 122 122 GLY G 75 LYS G 79 5 5
HELIX 123 123 GLY G 80 GLU G 91 1 12
HELIX 124 124 SER G 95 GLU G 105 1 11
HELIX 125 125 TYR G 108 ILE G 113 1 6
HELIX 126 126 ASP D 14 LEU D 19 1 6
HELIX 127 127 LEU D 61 GLY D 68 5 8
HELIX 128 128 ARG D 86 HIS D 100 1 15
HELIX 129 129 GLY D 112 TYR D 116 5 5
HELIX 130 130 THR D 133 GLY D 152 1 20
HELIX 131 131 ALA D 165 GLU D 176 1 12
HELIX 132 132 ASP D 184 ASN D 193 1 10
HELIX 133 133 ASN D 195 ALA D 213 1 19
HELIX 134 134 HIS D 225 THR D 230 1 6
HELIX 135 135 GLU D 233 LYS D 236 5 4
HELIX 136 136 VAL D 237 GLY D 256 1 20
HELIX 137 137 LYS D 258 SER D 260 5 3
HELIX 138 138 PRO D 275 PHE D 291 1 17
HELIX 139 139 SER D 308 THR D 326 1 19
HELIX 140 140 TRP D 344 MET D 362 1 19
HELIX 141 141 GLY D 364 ASP D 367 5 4
HELIX 142 142 GLY D 375 ALA D 398 1 24
HELIX 143 143 GLY D 400 GLN D 407 1 8
HELIX 144 144 ASP D 461 VAL D 465 5 5
HELIX 145 145 GLU D 467 ASP D 473 5 7
HELIX 146 146 VAL D 479 ILE D 483 5 5
HELIX 147 147 ASN D 494 GLU D 500 1 7
HELIX 148 148 GLU D 501 ARG D 506 5 6
HELIX 149 149 SER D 532 MET D 547 1 16
HELIX 150 150 ASN D 581 LEU D 583 5 3
HELIX 151 151 ASP D 595 THR D 604 1 10
HELIX 152 152 SER D 619 ASP D 627 1 9
HELIX 153 153 GLY D 632 GLY D 637 5 6
HELIX 154 154 GLU D 650 LEU D 652 5 3
HELIX 155 155 VAL D 653 LEU D 659 1 7
HELIX 156 156 SER D 671 ASP D 673 5 3
HELIX 157 157 ASP D 674 LYS D 690 1 17
HELIX 158 158 THR D 706 VAL D 711 1 6
HELIX 159 159 LYS D 724 ARG D 736 1 13
HELIX 160 160 ASP H 6 ALA H 12 1 7
HELIX 161 161 HIS H 13 ALA H 15 5 3
HELIX 162 162 SER H 18 LYS H 43 1 26
HELIX 163 163 THR H 46 GLY H 58 1 13
HELIX 164 164 SER H 60 ARG H 74 1 15
HELIX 165 165 LEU H 76 LYS H 79 5 4
HELIX 166 166 GLY H 80 LYS H 92 1 13
HELIX 167 167 SER H 95 SER H 104 1 10
HELIX 168 168 TYR H 108 ILE H 113 1 6
SHEET 1 A 2 LEU A 41 MET A 43 0
SHEET 2 A 2 PHE A 46 TYR A 48 -1 O PHE A 46 N MET A 43
SHEET 1 B 2 ALA A 51 SER A 52 0
SHEET 2 B 2 GLN A 73 PRO A 74 -1 O GLN A 73 N SER A 52
SHEET 1 C 9 VAL A 77 GLU A 81 0
SHEET 2 C 9 HIS A 104 MET A 106 1 O MET A 106 N THR A 80
SHEET 3 C 9 ASN A 156 TYR A 160 1 O ASN A 156 N ILE A 105
SHEET 4 C 9 GLY A 180 HIS A 182 1 O GLY A 180 N TYR A 157
SHEET 5 C 9 ALA A 216 ILE A 218 1 O ALA A 216 N ALA A 181
SHEET 6 C 9 ILE A 262 THR A 266 1 O CYS A 263 N GLN A 217
SHEET 7 C 9 ARG A 295 ALA A 298 1 O ARG A 297 N LEU A 264
SHEET 8 C 9 ILE A 330 GLN A 331 1 O ILE A 330 N ALA A 298
SHEET 9 C 9 VAL A 77 GLU A 81 1 N VAL A 77 O GLN A 331
SHEET 1 D 2 VAL A 369 LEU A 371 0
SHEET 2 D 2 VAL C 369 LEU C 371 -1 O GLN C 370 N GLN A 370
SHEET 1 E 2 PHE A 438 GLU A 439 0
SHEET 2 E 2 ASN E 44 THR E 45 -1 O THR E 45 N PHE A 438
SHEET 1 F 6 GLU A 550 GLN A 561 0
SHEET 2 F 6 GLY A 565 ARG A 573 -1 O ARG A 573 N GLU A 550
SHEET 3 F 6 THR A 522 LEU A 529 -1 N LEU A 525 O LEU A 570
SHEET 4 F 6 THR C 522 LEU C 529 -1 O THR C 526 N LEU A 524
SHEET 5 F 6 GLY C 565 ARG C 573 -1 O LEU C 570 N LEU C 525
SHEET 6 F 6 GLU C 550 GLN C 561 -1 N GLU C 553 O LYS C 571
SHEET 1 G 5 GLU A 639 TYR A 642 0
SHEET 2 G 5 LYS A 607 THR A 612 1 N ILE A 608 O GLU A 639
SHEET 3 G 5 ALA A 663 SER A 667 1 O LEU A 665 N VAL A 609
SHEET 4 G 5 MET A 697 GLY A 701 1 O GLY A 699 N ILE A 664
SHEET 5 G 5 ALA A 717 PHE A 719 1 O ALA A 717 N CYS A 700
SHEET 1 H 3 PRO B 37 ALA B 38 0
SHEET 2 H 3 ALA B 51 SER B 52 -1 O ALA B 51 N ALA B 38
SHEET 3 H 3 GLN B 73 PRO B 74 -1 O GLN B 73 N SER B 52
SHEET 1 I 2 LEU B 41 MET B 43 0
SHEET 2 I 2 PHE B 46 TYR B 48 -1 O PHE B 46 N MET B 43
SHEET 1 J 9 VAL B 77 GLU B 81 0
SHEET 2 J 9 HIS B 104 MET B 106 1 O MET B 106 N THR B 80
SHEET 3 J 9 ASN B 156 TYR B 160 1 O ASN B 156 N ILE B 105
SHEET 4 J 9 GLY B 180 HIS B 182 1 O GLY B 180 N TYR B 157
SHEET 5 J 9 ALA B 216 ILE B 218 1 O ALA B 216 N ALA B 181
SHEET 6 J 9 ILE B 262 THR B 266 1 O CYS B 263 N GLN B 217
SHEET 7 J 9 ARG B 295 ALA B 298 1 O ARG B 295 N ILE B 262
SHEET 8 J 9 ILE B 330 GLN B 331 1 O ILE B 330 N MET B 296
SHEET 9 J 9 VAL B 77 GLU B 81 1 N VAL B 77 O GLN B 331
SHEET 1 K 2 VAL B 369 LEU B 371 0
SHEET 2 K 2 VAL D 369 LEU D 371 -1 O GLN D 370 N GLN B 370
SHEET 1 L 2 PHE B 438 GLU B 439 0
SHEET 2 L 2 ASN F 44 THR F 45 -1 O THR F 45 N PHE B 438
SHEET 1 M 2 MET B 510 ILE B 511 0
SHEET 2 M 2 ILE B 578 ASP B 579 -1 O ILE B 578 N ILE B 511
SHEET 1 N 6 GLU B 550 GLN B 561 0
SHEET 2 N 6 GLY B 565 ARG B 573 -1 O LYS B 571 N GLU B 553
SHEET 3 N 6 THR B 522 LEU B 529 -1 N LEU B 529 O THR B 566
SHEET 4 N 6 THR D 522 LEU D 529 -1 O THR D 526 N LEU B 524
SHEET 5 N 6 GLY D 565 ARG D 573 -1 O LEU D 570 N LEU D 525
SHEET 6 N 6 GLU D 550 GLN D 561 -1 N GLU D 550 O ARG D 573
SHEET 1 O 5 GLU B 639 TYR B 642 0
SHEET 2 O 5 LYS B 607 THR B 612 1 N ILE B 608 O GLU B 639
SHEET 3 O 5 ALA B 663 SER B 667 1 O SER B 667 N ALA B 611
SHEET 4 O 5 MET B 697 GLY B 701 1 O MET B 697 N ILE B 664
SHEET 5 O 5 ALA B 717 PHE B 719 1 O ALA B 717 N CYS B 700
SHEET 1 P 2 LEU C 41 MET C 43 0
SHEET 2 P 2 PHE C 46 TYR C 48 -1 O TYR C 48 N LEU C 41
SHEET 1 Q 2 ALA C 51 SER C 52 0
SHEET 2 Q 2 GLN C 73 PRO C 74 -1 O GLN C 73 N SER C 52
SHEET 1 R 9 VAL C 77 GLU C 81 0
SHEET 2 R 9 HIS C 104 MET C 106 1 O MET C 106 N THR C 80
SHEET 3 R 9 ASN C 156 TYR C 160 1 O HIS C 158 N ILE C 105
SHEET 4 R 9 GLY C 180 HIS C 182 1 O GLY C 180 N TYR C 157
SHEET 5 R 9 ALA C 216 ILE C 218 1 O ALA C 216 N ALA C 181
SHEET 6 R 9 ILE C 262 THR C 266 1 O CYS C 263 N GLN C 217
SHEET 7 R 9 ARG C 295 ALA C 298 1 O ARG C 297 N THR C 266
SHEET 8 R 9 ILE C 330 SER C 332 1 O ILE C 330 N ALA C 298
SHEET 9 R 9 VAL C 77 GLU C 81 1 N VAL C 77 O GLN C 331
SHEET 1 S 2 PHE C 438 GLU C 439 0
SHEET 2 S 2 ASN G 44 THR G 45 -1 O THR G 45 N PHE C 438
SHEET 1 T 2 MET C 510 ILE C 511 0
SHEET 2 T 2 ILE C 578 ASP C 579 -1 O ILE C 578 N ILE C 511
SHEET 1 U 5 GLU C 639 TYR C 642 0
SHEET 2 U 5 LYS C 607 THR C 612 1 N ILE C 608 O GLU C 639
SHEET 3 U 5 ALA C 663 SER C 667 1 O SER C 667 N ALA C 611
SHEET 4 U 5 MET C 697 GLY C 701 1 O MET C 697 N ILE C 664
SHEET 5 U 5 ALA C 717 PHE C 719 1 O ALA C 717 N CYS C 700
SHEET 1 V 2 LEU D 41 MET D 43 0
SHEET 2 V 2 PHE D 46 TYR D 48 -1 O TYR D 48 N LEU D 41
SHEET 1 W 2 ALA D 51 SER D 52 0
SHEET 2 W 2 GLN D 73 PRO D 74 -1 O GLN D 73 N SER D 52
SHEET 1 X 9 VAL D 77 GLU D 81 0
SHEET 2 X 9 HIS D 104 MET D 106 1 O MET D 106 N THR D 80
SHEET 3 X 9 ASN D 156 TYR D 160 1 O ASN D 156 N ILE D 105
SHEET 4 X 9 GLY D 180 HIS D 182 1 O HIS D 182 N SER D 159
SHEET 5 X 9 ALA D 216 ILE D 218 1 O ALA D 216 N ALA D 181
SHEET 6 X 9 ILE D 262 THR D 266 1 O CYS D 263 N GLN D 217
SHEET 7 X 9 ARG D 295 ALA D 298 1 O ARG D 297 N LEU D 264
SHEET 8 X 9 ILE D 330 SER D 332 1 O SER D 332 N ALA D 298
SHEET 9 X 9 VAL D 77 GLU D 81 1 N VAL D 77 O GLN D 331
SHEET 1 Y 2 PHE D 438 GLU D 439 0
SHEET 2 Y 2 ASN H 44 THR H 45 -1 O THR H 45 N PHE D 438
SHEET 1 Z 2 MET D 510 ILE D 511 0
SHEET 2 Z 2 ILE D 578 ASP D 579 -1 O ILE D 578 N ILE D 511
SHEET 1 AA 5 GLU D 639 VAL D 647 0
SHEET 2 AA 5 LYS D 607 VAL D 613 1 N ILE D 608 O HIS D 641
SHEET 3 AA 5 ALA D 663 SER D 667 1 O LEU D 665 N VAL D 609
SHEET 4 AA 5 ILE D 698 GLY D 701 1 O GLY D 699 N ILE D 664
SHEET 5 AA 5 ALA D 717 PHE D 719 1 O PHE D 719 N CYS D 700
LINK NE2 HIS A 618 CO B12 A1801 1555 1555 2.69
LINK C5' 5AD A1500 CO B12 C1801 1555 1555 2.09
LINK CO B12 A1801 C5' 5AD C1500 1555 1555 2.11
LINK NE2 HIS B 618 CO B12 B1801 1555 1555 2.29
LINK C5' 5AD B1500 CO B12 D1801 1555 1555 2.11
LINK CO B12 B1801 C5' 5AD D1500 1555 1555 2.10
LINK NE2 HIS C 618 CO B12 C1801 1555 1555 2.26
LINK NE2 HIS D 618 CO B12 D1801 1555 1555 2.40
CISPEP 1 PRO A 272 PRO A 273 0 13.72
CISPEP 2 TYR A 416 PRO A 417 0 15.37
CISPEP 3 ASP E 5 ASP E 6 0 18.13
CISPEP 4 PRO B 272 PRO B 273 0 10.33
CISPEP 5 TYR B 416 PRO B 417 0 8.69
CISPEP 6 ASP F 5 ASP F 6 0 11.10
CISPEP 7 PRO C 272 PRO C 273 0 3.43
CISPEP 8 TYR C 416 PRO C 417 0 0.83
CISPEP 9 ASP G 5 ASP G 6 0 15.44
CISPEP 10 PRO D 272 PRO D 273 0 8.73
CISPEP 11 TYR D 416 PRO D 417 0 14.00
CISPEP 12 ASP H 5 ASP H 6 0 0.71
SITE 1 AC1 22 GLU A 615 GLU A 617 HIS A 618 SER A 619
SITE 2 AC1 22 VAL A 620 GLY A 621 VAL A 625 SER A 667
SITE 3 AC1 22 ILE A 669 ILE A 670 SER A 671 HIS A 672
SITE 4 AC1 22 GLY A 701 GLY A 702 THR A 703 PHE A 719
SITE 5 AC1 22 GLY A 722 SER A 723 VAL A 728 TYR C 116
SITE 6 AC1 22 ASP C 490 5AD C1500
SITE 1 AC2 2 B12 A1801 LEU C 489
SITE 1 AC3 14 LYS A 629 GLU C 81 ARG C 109 GLN C 113
SITE 2 AC3 14 SER C 114 TYR C 160 SER C 162 HIS C 182
SITE 3 AC3 14 TYR C 187 ARG C 192 HIS C 225 ASN C 226
SITE 4 AC3 14 ARG C 297 GLN C 299
SITE 1 AC4 24 TYR B 116 5AD B1500 GLU D 617 HIS D 618
SITE 2 AC4 24 SER D 619 VAL D 620 GLY D 621 LEU D 622
SITE 3 AC4 24 GLU D 624 VAL D 625 ALA D 666 SER D 667
SITE 4 AC4 24 ILE D 669 ILE D 670 SER D 671 HIS D 672
SITE 5 AC4 24 GLY D 701 GLY D 702 THR D 703 PHE D 719
SITE 6 AC4 24 GLY D 720 GLY D 722 SER D 723 VAL D 728
SITE 1 AC5 3 LEU B 489 ASP B 490 B12 D1801
SITE 1 AC6 15 GLU A 81 ARG A 109 GLY A 112 GLN A 113
SITE 2 AC6 15 SER A 114 TYR A 160 SER A 162 HIS A 182
SITE 3 AC6 15 TYR A 187 ARG A 192 HIS A 225 ASN A 226
SITE 4 AC6 15 ARG A 297 GLN A 299 LYS C 629
SITE 1 AC7 23 TYR A 116 ASP A 490 5AD A1500 GLU C 615
SITE 2 AC7 23 GLU C 617 HIS C 618 SER C 619 VAL C 620
SITE 3 AC7 23 GLY C 621 LEU C 622 SER C 667 ILE C 669
SITE 4 AC7 23 ILE C 670 SER C 671 HIS C 672 GLY C 701
SITE 5 AC7 23 GLY C 702 THR C 703 PHE C 719 GLY C 720
SITE 6 AC7 23 GLY C 722 SER C 723 VAL C 728
SITE 1 AC8 3 LEU A 489 ASP A 490 B12 C1801
SITE 1 AC9 16 GLU B 81 ILE B 108 ARG B 109 GLN B 113
SITE 2 AC9 16 SER B 114 TYR B 160 SER B 162 HIS B 182
SITE 3 AC9 16 TYR B 187 ARG B 192 GLY B 223 HIS B 225
SITE 4 AC9 16 ASN B 226 ARG B 297 GLN B 299 LYS D 629
SITE 1 BC1 23 GLU B 615 ASP B 616 GLU B 617 HIS B 618
SITE 2 BC1 23 SER B 619 VAL B 620 GLY B 621 LEU B 665
SITE 3 BC1 23 ALA B 666 SER B 667 ILE B 669 ILE B 670
SITE 4 BC1 23 SER B 671 HIS B 672 GLY B 701 GLY B 702
SITE 5 BC1 23 THR B 703 PHE B 719 GLY B 720 SER B 723
SITE 6 BC1 23 TYR D 116 ASP D 490 5AD D1500
SITE 1 BC2 2 B12 B1801 LEU D 489
SITE 1 BC3 15 LYS B 629 GLU D 81 ARG D 109 GLY D 112
SITE 2 BC3 15 GLN D 113 SER D 114 TYR D 160 SER D 162
SITE 3 BC3 15 HIS D 182 TYR D 187 ARG D 192 HIS D 225
SITE 4 BC3 15 ASN D 226 ARG D 297 GLN D 299
CRYST1 66.520 233.220 124.140 90.00 103.43 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 0.015033 0.000000 0.003590 0.00000
SCALE2 0.000000 0.004288 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008282 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
