HEADER METHYLTRANSFERASE 02-SEP-94 1BMT
TITLE HOW A PROTEIN BINDS B12: A 3.O ANGSTROM X-RAY STRUCTURE OF THE B12-
TITLE 2 BINDING DOMAINS OF METHIONINE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METHYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.DRENNAN,S.HUANG,J.T.DRUMMOND,R.G.MATTHEWS,M.L.LUDWIG
REVDAT 5 07-FEB-24 1BMT 1 REMARK
REVDAT 4 27-APR-22 1BMT 1 SOURCE JRNL REMARK
REVDAT 3 24-FEB-09 1BMT 1 VERSN
REVDAT 2 01-APR-03 1BMT 1 JRNL
REVDAT 1 03-JUN-95 1BMT 0
JRNL AUTH C.L.DRENNAN,S.HUANG,J.T.DRUMMOND,R.G.MATTHEWS,M.L.LUDWIG
JRNL TITL HOW A PROTEIN BINDS B12: A 3.0 A X-RAY STRUCTURE OF
JRNL TITL 2 B12-BINDING DOMAINS OF METHIONINE SYNTHASE.
JRNL REF SCIENCE V. 266 1669 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 7992050
JRNL DOI 10.1126/SCIENCE.7992050
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.L.DRENNAN,R.G.MATTHEWS,M.L.LUDWIG
REMARK 1 TITL COBALAMIN-DEPENDENT METHIONINE SYNTHASE: THE STRUCTURE OF A
REMARK 1 TITL 2 METHYLCOBALAMIN-BINDING FRAGMENT AND IMPLICATIONS FOR OTHER
REMARK 1 TITL 3 B12-DEPENDENT ENZYMES
REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 4 919 1994
REMARK 1 REFN ISSN 0959-440X
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 9019
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3814
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 184
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.610
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 48.35000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE SECONDARY STRUCTURAL ELEMENTS WERE IDENTIFIED BY
REMARK 400 HYDROGEN BONDING PATTERNS AND THE METHOD OF KABSCH AND
REMARK 400 SANDER, 1983.
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 B 785 C - N - CA ANGL. DEV. = 10.3 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 ALA A 652 -166.07 -176.44
REMARK 500 ARG A 655 21.46 -66.61
REMARK 500 LYS A 740 142.18 -170.08
REMARK 500 GLU A 741 -3.76 -146.12
REMARK 500 GLN A 742 -96.55 35.59
REMARK 500 VAL A 754 161.71 -44.25
REMARK 500 ASP A 760 -1.82 -151.39
REMARK 500 ASN A 774 71.88 68.94
REMARK 500 THR A 827 -8.57 -144.80
REMARK 500 GLN A 848 -31.75 -31.29
REMARK 500 ARG A 876 -79.65 -31.74
REMARK 500 HIS A 894 24.37 -70.39
REMARK 500 ARG B 655 7.52 -59.90
REMARK 500 TRP B 657 -173.23 -66.45
REMARK 500 LYS B 740 80.19 167.84
REMARK 500 GLN B 742 -135.71 38.83
REMARK 500 LYS B 744 -109.18 -119.55
REMARK 500 ASP B 760 -11.46 -146.11
REMARK 500 CYS B 772 5.87 -64.55
REMARK 500 ASN B 774 78.04 64.06
REMARK 500 ILE B 846 -63.85 -104.60
REMARK 500 ARG B 876 -77.28 -28.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 823 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 COB A 122 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 759 NE2
REMARK 620 2 COB A 122 N21 99.5
REMARK 620 3 COB A 122 N22 83.4 88.8
REMARK 620 4 COB A 122 N23 87.6 172.9 92.2
REMARK 620 5 COB A 122 N24 96.9 89.0 177.8 90.0
REMARK 620 6 COB A 122 C1A 167.4 90.8 89.6 82.2 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 COB B 122 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 759 NE2
REMARK 620 2 COB B 122 N21 110.4
REMARK 620 3 COB B 122 N22 95.9 98.5
REMARK 620 4 COB B 122 N23 85.2 162.9 86.2
REMARK 620 5 COB B 122 N24 103.7 79.3 159.8 90.7
REMARK 620 6 COB B 122 C1A 168.5 81.1 82.4 83.3 77.4
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 COB A 122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COB B 122
DBREF 1BMT A 651 896 UNP P13009 METH_ECOLI 650 895
DBREF 1BMT B 651 896 UNP P13009 METH_ECOLI 650 895
SEQRES 1 A 246 GLN ALA GLU TRP ARG SER TRP GLU VAL ASN LYS ARG LEU
SEQRES 2 A 246 GLU TYR SER LEU VAL LYS GLY ILE THR GLU PHE ILE GLU
SEQRES 3 A 246 GLN ASP THR GLU GLU ALA ARG GLN GLN ALA THR ARG PRO
SEQRES 4 A 246 ILE GLU VAL ILE GLU GLY PRO LEU MET ASP GLY MET ASN
SEQRES 5 A 246 VAL VAL GLY ASP LEU PHE GLY GLU GLY LYS MET PHE LEU
SEQRES 6 A 246 PRO GLN VAL VAL LYS SER ALA ARG VAL MET LYS GLN ALA
SEQRES 7 A 246 VAL ALA TYR LEU GLU PRO PHE ILE GLU ALA SER LYS GLU
SEQRES 8 A 246 GLN GLY LYS THR ASN GLY LYS MET VAL ILE ALA THR VAL
SEQRES 9 A 246 LYS GLY ASP VAL HIS ASP ILE GLY LYS ASN ILE VAL GLY
SEQRES 10 A 246 VAL VAL LEU GLN CYS ASN ASN TYR GLU ILE VAL ASP LEU
SEQRES 11 A 246 GLY VAL MET VAL PRO ALA GLU LYS ILE LEU ARG THR ALA
SEQRES 12 A 246 LYS GLU VAL ASN ALA ASP LEU ILE GLY LEU SER GLY LEU
SEQRES 13 A 246 ILE THR PRO SER LEU ASP GLU MET VAL ASN VAL ALA LYS
SEQRES 14 A 246 GLU MET GLU ARG GLN GLY PHE THR ILE PRO LEU LEU ILE
SEQRES 15 A 246 GLY GLY ALA THR THR SER LYS ALA HIS THR ALA VAL LYS
SEQRES 16 A 246 ILE GLU GLN ASN TYR SER GLY PRO THR VAL TYR VAL GLN
SEQRES 17 A 246 ASN ALA SER ARG THR VAL GLY VAL VAL ALA ALA LEU LEU
SEQRES 18 A 246 SER ASP THR GLN ARG ASP ASP PHE VAL ALA ARG THR ARG
SEQRES 19 A 246 LYS GLU TYR GLU THR VAL ARG ILE GLN HIS GLY ARG
SEQRES 1 B 246 GLN ALA GLU TRP ARG SER TRP GLU VAL ASN LYS ARG LEU
SEQRES 2 B 246 GLU TYR SER LEU VAL LYS GLY ILE THR GLU PHE ILE GLU
SEQRES 3 B 246 GLN ASP THR GLU GLU ALA ARG GLN GLN ALA THR ARG PRO
SEQRES 4 B 246 ILE GLU VAL ILE GLU GLY PRO LEU MET ASP GLY MET ASN
SEQRES 5 B 246 VAL VAL GLY ASP LEU PHE GLY GLU GLY LYS MET PHE LEU
SEQRES 6 B 246 PRO GLN VAL VAL LYS SER ALA ARG VAL MET LYS GLN ALA
SEQRES 7 B 246 VAL ALA TYR LEU GLU PRO PHE ILE GLU ALA SER LYS GLU
SEQRES 8 B 246 GLN GLY LYS THR ASN GLY LYS MET VAL ILE ALA THR VAL
SEQRES 9 B 246 LYS GLY ASP VAL HIS ASP ILE GLY LYS ASN ILE VAL GLY
SEQRES 10 B 246 VAL VAL LEU GLN CYS ASN ASN TYR GLU ILE VAL ASP LEU
SEQRES 11 B 246 GLY VAL MET VAL PRO ALA GLU LYS ILE LEU ARG THR ALA
SEQRES 12 B 246 LYS GLU VAL ASN ALA ASP LEU ILE GLY LEU SER GLY LEU
SEQRES 13 B 246 ILE THR PRO SER LEU ASP GLU MET VAL ASN VAL ALA LYS
SEQRES 14 B 246 GLU MET GLU ARG GLN GLY PHE THR ILE PRO LEU LEU ILE
SEQRES 15 B 246 GLY GLY ALA THR THR SER LYS ALA HIS THR ALA VAL LYS
SEQRES 16 B 246 ILE GLU GLN ASN TYR SER GLY PRO THR VAL TYR VAL GLN
SEQRES 17 B 246 ASN ALA SER ARG THR VAL GLY VAL VAL ALA ALA LEU LEU
SEQRES 18 B 246 SER ASP THR GLN ARG ASP ASP PHE VAL ALA ARG THR ARG
SEQRES 19 B 246 LYS GLU TYR GLU THR VAL ARG ILE GLN HIS GLY ARG
HET COB A 122 92
HET COB B 122 92
HETNAM COB CO-METHYLCOBALAMIN
FORMUL 3 COB 2(C63 H91 CO N13 O14 P 1+)
FORMUL 5 HOH *2(H2 O)
HELIX 1 A1 TRP A 654 SER A 656 5 3
HELIX 2 A2 VAL A 659 GLY A 670 1 12
HELIX 3 A3 PHE A 674 GLN A 684 1 11
HELIX 4 A4 PRO A 689 GLU A 710 1 22
HELIX 5 A5 PHE A 714 ALA A 738 1 25
HELIX 6 A6 ILE A 761 ASN A 773 1 13
HELIX 7 A7 PRO A 785 VAL A 796 1 12
HELIX 8 A8 ILE A 807 GLN A 824 1 18
HELIX 9 A9 SER A 838 VAL A 844 1 7
HELIX 10 A10 GLU A 847 ASN A 849 5 3
HELIX 11 A11 ALA A 860 LEU A 871 1 12
HELIX 12 A12 GLN A 875 GLN A 893 1 19
HELIX 13 B1 TRP B 654 SER B 656 5 3
HELIX 14 B2 VAL B 659 GLY B 670 1 12
HELIX 15 B3 PHE B 674 GLN B 684 1 11
HELIX 16 B4 PRO B 689 GLU B 710 1 22
HELIX 17 B5 PHE B 714 ALA B 738 1 25
HELIX 18 B6 ILE B 761 ASN B 773 1 13
HELIX 19 B7 PRO B 785 VAL B 796 1 12
HELIX 20 B8 ILE B 807 GLN B 824 1 18
HELIX 21 B9 SER B 838 VAL B 844 1 7
HELIX 22 B10 GLU B 847 ASN B 849 5 3
HELIX 23 B11 ALA B 860 LEU B 871 1 12
HELIX 24 B12 GLN B 875 GLN B 893 1 19
SHEET 1 B1A 5 GLU A 776 GLY A 781 0
SHEET 2 B1A 5 LYS A 748 VAL A 754 1 N MET A 749 O GLU A 776
SHEET 3 B1A 5 ASP A 799 GLY A 805 1 N LEU A 800 O LYS A 748
SHEET 4 B1A 5 PRO A 829 GLY A 833 1 O PRO A 829 N ILE A 801
SHEET 5 B1A 5 PRO A 853 VAL A 857 1 O PRO A 853 N LEU A 830
SHEET 1 B1B 5 GLU B 776 GLY B 781 0
SHEET 2 B1B 5 LYS B 748 VAL B 754 1 N MET B 749 O GLU B 776
SHEET 3 B1B 5 ASP B 799 GLY B 805 1 N LEU B 800 O LYS B 748
SHEET 4 B1B 5 PRO B 829 GLY B 833 1 O PRO B 829 N ILE B 801
SHEET 5 B1B 5 PRO B 853 VAL B 857 1 O PRO B 853 N LEU B 830
LINK CO COB A 122 NE2 HIS A 759 1555 1555 2.24
LINK CO COB B 122 NE2 HIS B 759 1555 1555 2.14
SITE 1 AC1 33 GLU A 694 MET A 698 MET A 701 GLY A 705
SITE 2 AC1 33 LEU A 715 VAL A 718 GLY A 756 ASP A 757
SITE 3 AC1 33 VAL A 758 HIS A 759 ASP A 760 ILE A 761
SITE 4 AC1 33 GLY A 762 ILE A 765 GLY A 802 LEU A 803
SITE 5 AC1 33 SER A 804 LEU A 806 ILE A 807 THR A 808
SITE 6 AC1 33 LEU A 831 GLY A 834 ALA A 835 VAL A 857
SITE 7 AC1 33 GLN A 858 ASN A 859 ALA A 860 THR A 863
SITE 8 AC1 33 GLN B 677 GLU B 680 ARG B 683 TYR B 731
SITE 9 AC1 33 PHE B 735
SITE 1 AC2 31 ALA A 738 GLU A 741 GLU B 694 MET B 698
SITE 2 AC2 31 MET B 701 VAL B 704 GLY B 705 LEU B 715
SITE 3 AC2 31 VAL B 718 MET B 725 ILE B 751 GLY B 756
SITE 4 AC2 31 ASP B 757 VAL B 758 HIS B 759 ASP B 760
SITE 5 AC2 31 ILE B 761 GLY B 762 ILE B 765 GLY B 802
SITE 6 AC2 31 LEU B 803 SER B 804 LEU B 806 ILE B 807
SITE 7 AC2 31 THR B 808 GLY B 834 ALA B 835 GLN B 858
SITE 8 AC2 31 ASN B 859 ALA B 860 THR B 863
CRYST1 96.700 55.300 103.800 90.00 90.00 90.00 P 21 21 21 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 0.010341 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009634 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
