HEADER TRANSFERASE 31-AUG-09 3IVA
TITLE STRUCTURE OF THE B12-DEPENDENT METHIONINE SYNTHASE (METH) C-TEMINAL
TITLE 2 HALF WITH ADOHCY BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL ACTIVATION COMPLEX (UNP RESIDUES 649-1227);
COMPND 5 SYNONYM: 5-METHYLTETRAHYDROFOLATE--HOMOCYSTEINE METHYLTRANSFERASE,
COMPND 6 METHIONINE SYNTHASE, VITAMIN-B12-DEPENDENT, MS;
COMPND 7 EC: 2.1.1.13;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: B4019, JW3979, METH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PVB8
KEYWDS METH, TRANSFERASE, REACTIVATION CONFORMATION, H759, COBALAMIN,
KEYWDS 2 INTERMODULAR INTERACTIONS, AMINO-ACID BIOSYNTHESIS, COBALT, METAL-
KEYWDS 3 BINDING, METHIONINE BIOSYNTHESIS, METHYLTRANSFERASE, S-ADENOSYL-L-
KEYWDS 4 METHIONINE, S-ADENOSYL-HOMOCYSTEINE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.PATTRIDGE,M.KOUTMOS,J.L.SMITH
REVDAT 2 24-OCT-12 3IVA 1 FORMUL VERSN
REVDAT 1 24-NOV-09 3IVA 0
JRNL AUTH M.KOUTMOS,S.DATTA,K.A.PATTRIDGE,J.L.SMITH,R.G.MATTHEWS
JRNL TITL INSIGHTS INTO THE REACTIVATION OF COBALAMIN-DEPENDENT
JRNL TITL 2 METHIONINE SYNTHASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 18527 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19846791
JRNL DOI 10.1073/PNAS.0906132106
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3333675.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23159
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1130
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3588
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 169
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4563
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 133
REMARK 3 SOLVENT ATOMS : 26
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.58000
REMARK 3 B22 (A**2) : -6.58000
REMARK 3 B33 (A**2) : 13.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.31
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.32
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.980 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 60.99
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PARAM12CNS.KAP
REMARK 3 PARAMETER FILE 5 : LIGANDS.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : TOPCNS.COB3
REMARK 3 TOPOLOGY FILE 5 : LIGANDS.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3IVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB054908.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.400
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 22.40
REMARK 200 R MERGE FOR SHELL (I) : 0.20400
REMARK 200 R SYM FOR SHELL (I) : 0.62200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: INDIVIDUAL DOMAINS OF PDB ENTRY 3BUL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM NITRATE, 18 % (W/V)
REMARK 280 PEG3350, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 302K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.59250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.50300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.50300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 105.88875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.50300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.50300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.29625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.50300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.50300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 105.88875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.50300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.50300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.29625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.59250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 649
REMARK 465 GLN A 650
REMARK 465 ASP A 1227
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 ALA A 652 -8.49 162.12
REMARK 500 GLU A 653 -57.53 72.85
REMARK 500 GLN A 677 48.15 -79.03
REMARK 500 ASP A 678 -22.85 -154.67
REMARK 500 SER A 739 27.30 -151.97
REMARK 500 LYS A 740 -168.67 47.49
REMARK 500 GLU A 741 126.70 77.42
REMARK 500 CYS A 743 133.09 56.57
REMARK 500 VAL A 754 153.71 -35.84
REMARK 500 ASN A 774 -4.96 67.09
REMARK 500 ASN A 797 96.74 24.06
REMARK 500 SER A 872 -168.09 -100.59
REMARK 500 GLN A 875 -31.50 -139.53
REMARK 500 ARG A 896 -152.35 -120.40
REMARK 500 LYS A 898 131.85 -1.46
REMARK 500 PRO A 899 86.86 -50.98
REMARK 500 ARG A 900 107.23 -58.65
REMARK 500 THR A 901 71.61 161.25
REMARK 500 PRO A 902 120.75 -39.52
REMARK 500 HIS A1028 143.38 62.91
REMARK 500 GLN A1032 68.96 -118.63
REMARK 500 LEU A1051 39.93 -74.38
REMARK 500 GLN A1079 28.11 -69.87
REMARK 500 VAL A1110 -75.86 -116.30
REMARK 500 ALA A1115 50.42 -141.15
REMARK 500 CYS A1142 68.12 -154.58
REMARK 500 GLU A1144 94.33 -52.15
REMARK 500 GLU A1147 -9.00 -59.14
REMARK 500 ALA A1193 -147.07 57.47
REMARK 500
REMARK 500 REMARK: NULL
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 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K7Y RELATED DB: PDB
REMARK 900 SAME FRAGMENT WITH H759G MUTATION AND NO ADOHCY
REMARK 900 RELATED ID: 3BUL RELATED DB: PDB
REMARK 900 SAME FRAGMENT WITH NO ADOHCY
REMARK 900 RELATED ID: 3IV9 RELATED DB: PDB
DBREF 3IVA A 649 1227 UNP P13009 METH_ECOLI 649 1227
SEQADV 3IVA CYS A 690 UNP P13009 ILE 690 ENGINEERED
SEQADV 3IVA CYS A 743 UNP P13009 GLY 743 ENGINEERED
SEQRES 1 A 579 ALA GLN GLN ALA GLU TRP ARG SER TRP GLU VAL ASN LYS
SEQRES 2 A 579 ARG LEU GLU TYR SER LEU VAL LYS GLY ILE THR GLU PHE
SEQRES 3 A 579 ILE GLU GLN ASP THR GLU GLU ALA ARG GLN GLN ALA THR
SEQRES 4 A 579 ARG PRO CYS GLU VAL ILE GLU GLY PRO LEU MET ASP GLY
SEQRES 5 A 579 MET ASN VAL VAL GLY ASP LEU PHE GLY GLU GLY LYS MET
SEQRES 6 A 579 PHE LEU PRO GLN VAL VAL LYS SER ALA ARG VAL MET LYS
SEQRES 7 A 579 GLN ALA VAL ALA TYR LEU GLU PRO PHE ILE GLU ALA SER
SEQRES 8 A 579 LYS GLU GLN CYS LYS THR ASN GLY LYS MET VAL ILE ALA
SEQRES 9 A 579 THR VAL LYS GLY ASP VAL HIS ASP ILE GLY LYS ASN ILE
SEQRES 10 A 579 VAL GLY VAL VAL LEU GLN CYS ASN ASN TYR GLU ILE VAL
SEQRES 11 A 579 ASP LEU GLY VAL MET VAL PRO ALA GLU LYS ILE LEU ARG
SEQRES 12 A 579 THR ALA LYS GLU VAL ASN ALA ASP LEU ILE GLY LEU SER
SEQRES 13 A 579 GLY LEU ILE THR PRO SER LEU ASP GLU MET VAL ASN VAL
SEQRES 14 A 579 ALA LYS GLU MET GLU ARG GLN GLY PHE THR ILE PRO LEU
SEQRES 15 A 579 LEU ILE GLY GLY ALA THR THR SER LYS ALA HIS THR ALA
SEQRES 16 A 579 VAL LYS ILE GLU GLN ASN TYR SER GLY PRO THR VAL TYR
SEQRES 17 A 579 VAL GLN ASN ALA SER ARG THR VAL GLY VAL VAL ALA ALA
SEQRES 18 A 579 LEU LEU SER ASP THR GLN ARG ASP ASP PHE VAL ALA ARG
SEQRES 19 A 579 THR ARG LYS GLU TYR GLU THR VAL ARG ILE GLN HIS GLY
SEQRES 20 A 579 ARG LYS LYS PRO ARG THR PRO PRO VAL THR LEU GLU ALA
SEQRES 21 A 579 ALA ARG ASP ASN ASP PHE ALA PHE ASP TRP GLN ALA TYR
SEQRES 22 A 579 THR PRO PRO VAL ALA HIS ARG LEU GLY VAL GLN GLU VAL
SEQRES 23 A 579 GLU ALA SER ILE GLU THR LEU ARG ASN TYR ILE ASP TRP
SEQRES 24 A 579 THR PRO PHE PHE MET THR TRP SER LEU ALA GLY LYS TYR
SEQRES 25 A 579 PRO ARG ILE LEU GLU ASP GLU VAL VAL GLY VAL GLU ALA
SEQRES 26 A 579 GLN ARG LEU PHE LYS ASP ALA ASN ASP MET LEU ASP LYS
SEQRES 27 A 579 LEU SER ALA GLU LYS THR LEU ASN PRO ARG GLY VAL VAL
SEQRES 28 A 579 GLY LEU PHE PRO ALA ASN ARG VAL GLY ASP ASP ILE GLU
SEQRES 29 A 579 ILE TYR ARG ASP GLU THR ARG THR HIS VAL ILE ASN VAL
SEQRES 30 A 579 SER HIS HIS LEU ARG GLN GLN THR GLU LYS THR GLY PHE
SEQRES 31 A 579 ALA ASN TYR CYS LEU ALA ASP PHE VAL ALA PRO LYS LEU
SEQRES 32 A 579 SER GLY LYS ALA ASP TYR ILE GLY ALA PHE ALA VAL THR
SEQRES 33 A 579 GLY GLY LEU GLU GLU ASP ALA LEU ALA ASP ALA PHE GLU
SEQRES 34 A 579 ALA GLN HIS ASP ASP TYR ASN LYS ILE MET VAL LYS ALA
SEQRES 35 A 579 LEU ALA ASP ARG LEU ALA GLU ALA PHE ALA GLU TYR LEU
SEQRES 36 A 579 HIS GLU ARG VAL ARG LYS VAL TYR TRP GLY TYR ALA PRO
SEQRES 37 A 579 ASN GLU ASN LEU SER ASN GLU GLU LEU ILE ARG GLU ASN
SEQRES 38 A 579 TYR GLN GLY ILE ARG PRO ALA PRO GLY TYR PRO ALA CYS
SEQRES 39 A 579 PRO GLU HIS THR GLU LYS ALA THR ILE TRP GLU LEU LEU
SEQRES 40 A 579 GLU VAL GLU LYS HIS THR GLY MET LYS LEU THR GLU SER
SEQRES 41 A 579 PHE ALA MET TRP PRO GLY ALA SER VAL SER GLY TRP TYR
SEQRES 42 A 579 PHE SER HIS PRO ASP SER LYS TYR TYR ALA VAL ALA GLN
SEQRES 43 A 579 ILE GLN ARG ASP GLN VAL GLU ASP TYR ALA ARG ARG LYS
SEQRES 44 A 579 GLY MET SER VAL THR GLU VAL GLU ARG TRP LEU ALA PRO
SEQRES 45 A 579 ASN LEU GLY TYR ASP ALA ASP
HET B12 A1301 91
HET SAH A1401 26
HET NO3 A1303 4
HET NO3 A1304 4
HET NO3 A1305 4
HET NO3 A1306 4
HETNAM B12 COBALAMIN
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM NO3 NITRATE ION
FORMUL 2 B12 C62 H89 CO N13 O14 P 2+
FORMUL 3 SAH C14 H20 N6 O5 S
FORMUL 4 NO3 4(N O3 1-)
FORMUL 8 HOH *26(H2 O)
HELIX 1 1 GLU A 653 TRP A 657 5 5
HELIX 2 2 GLU A 658 GLY A 670 1 13
HELIX 3 3 ILE A 675 ALA A 686 1 12
HELIX 4 4 PRO A 689 GLY A 695 1 7
HELIX 5 5 GLY A 695 GLU A 710 1 16
HELIX 6 6 PHE A 714 LEU A 732 1 19
HELIX 7 7 LEU A 732 ALA A 738 1 7
HELIX 8 8 ASP A 760 CYS A 772 1 13
HELIX 9 9 PRO A 785 VAL A 796 1 12
HELIX 10 10 ILE A 807 GLN A 824 1 18
HELIX 11 11 SER A 838 LYS A 845 1 8
HELIX 12 12 ILE A 846 TYR A 850 5 5
HELIX 13 13 SER A 861 LEU A 870 1 10
HELIX 14 14 GLN A 875 VAL A 890 1 16
HELIX 15 15 VAL A 890 ARG A 896 1 7
HELIX 16 16 THR A 905 ASN A 912 1 8
HELIX 17 17 SER A 937 ARG A 942 1 6
HELIX 18 18 ASN A 943 ILE A 945 5 3
HELIX 19 19 TRP A 947 TRP A 954 1 8
HELIX 20 20 PRO A 961 ASP A 966 5 6
HELIX 21 21 VAL A 969 GLU A 990 1 22
HELIX 22 22 CYS A 1042 VAL A 1047 5 6
HELIX 23 23 PRO A 1049 GLY A 1053 5 5
HELIX 24 24 GLU A 1068 GLN A 1079 1 12
HELIX 25 25 ASP A 1081 VAL A 1110 1 30
HELIX 26 26 SER A 1121 ARG A 1127 1 7
HELIX 27 27 GLU A 1144 THR A 1146 5 3
HELIX 28 28 GLU A 1147 LEU A 1155 1 9
HELIX 29 29 GLU A 1156 GLY A 1162 1 7
HELIX 30 30 GLN A 1196 GLY A 1208 1 13
HELIX 31 31 SER A 1210 LEU A 1218 1 9
HELIX 32 32 ALA A 1219 LEU A 1222 5 4
SHEET 1 A 5 GLU A 776 ASP A 779 0
SHEET 2 A 5 LYS A 748 THR A 753 1 N MET A 749 O VAL A 778
SHEET 3 A 5 LEU A 800 SER A 804 1 O GLY A 802 N VAL A 750
SHEET 4 A 5 LEU A 830 GLY A 833 1 O GLY A 833 N LEU A 803
SHEET 5 A 5 THR A 854 TYR A 856 1 O VAL A 855 N LEU A 830
SHEET 1 B 4 GLY A 930 GLU A 935 0
SHEET 2 B 4 ARG A 996 VAL A1007 -1 O VAL A 999 N GLN A 932
SHEET 3 B 4 ASP A1010 TYR A1014 -1 O GLU A1012 N ASN A1005
SHEET 4 B 4 VAL A1022 SER A1026 -1 O SER A1026 N ILE A1011
SHEET 1 C 4 GLY A 930 GLU A 935 0
SHEET 2 C 4 ARG A 996 VAL A1007 -1 O VAL A 999 N GLN A 932
SHEET 3 C 4 ASP A1056 THR A1064 -1 O ALA A1060 N GLY A1000
SHEET 4 C 4 SER A1176 TYR A1181 -1 O VAL A1177 N VAL A1063
SHEET 1 D 2 LYS A1164 LEU A1165 0
SHEET 2 D 2 MET A1171 TRP A1172 -1 O TRP A1172 N LYS A1164
SSBOND 1 CYS A 690 CYS A 743 1555 1555 2.03
CISPEP 1 TYR A 960 PRO A 961 0 0.27
CISPEP 2 TRP A 1172 PRO A 1173 0 0.00
SITE 1 AC1 38 ILE A 751 VAL A 758 HIS A 759 GLY A 762
SITE 2 AC1 38 VAL A 766 GLY A 802 LEU A 803 SER A 804
SITE 3 AC1 38 LEU A 806 ILE A 807 THR A 808 LEU A 831
SITE 4 AC1 38 GLY A 833 GLY A 834 ALA A 835 VAL A 857
SITE 5 AC1 38 GLN A 858 ASN A 859 ALA A 860 THR A 953
SITE 6 AC1 38 ASP A1093 ARG A1094 GLU A1097 ALA A1136
SITE 7 AC1 38 PRO A1137 GLY A1138 TYR A1139 PRO A1140
SITE 8 AC1 38 HIS A1145 LYS A1148 ALA A1170 MET A1171
SITE 9 AC1 38 PRO A1173 GLY A1174 SER A1176 VAL A1177
SITE 10 AC1 38 SER A1178 SAH A1401
SITE 1 AC2 14 ARG A 823 ASP A 946 ARG A1094 GLU A1097
SITE 2 AC2 14 GLU A1128 ARG A1134 PRO A1135 ALA A1136
SITE 3 AC2 14 TYR A1139 PRO A1140 ALA A1141 TYR A1189
SITE 4 AC2 14 TYR A1190 B12 A1301
SITE 1 AC3 4 ASN A1024 VAL A1025 THR A1150 GLU A1153
SITE 1 AC4 4 TYR A 944 GLU A1105 LEU A1120 ASN A1122
SITE 1 AC5 3 TYR A1130 GLY A1132 SER A1187
SITE 1 AC6 2 ASP A 911 ASP A 913
CRYST1 107.006 107.006 141.185 90.00 90.00 90.00 P 43 21 2 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 0.009345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
