HEADER METAL BINDING PROTEIN 17-NOV-00 1G8L
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS MOLYBDENUM COFACTOR BIOSYNTHESIS, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XIANG,J.NICHOLS,K.V.RAJAGOPALAN,H.SCHINDELIN
REVDAT 5 07-FEB-24 1G8L 1 REMARK
REVDAT 4 13-JUL-11 1G8L 1 VERSN
REVDAT 3 24-FEB-09 1G8L 1 VERSN
REVDAT 2 01-APR-03 1G8L 1 JRNL
REVDAT 1 02-MAY-01 1G8L 0
JRNL AUTH S.XIANG,J.NICHOLS,K.V.RAJAGOPALAN,H.SCHINDELIN
JRNL TITL THE CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA AND ITS
JRNL TITL 2 RELATIONSHIP TO THE MULTIFUNCTIONAL PROTEIN GEPHYRIN.
JRNL REF STRUCTURE V. 9 299 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11525167
JRNL DOI 10.1016/S0969-2126(01)00588-3
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 54423
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) : 0.228
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2892
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 : 6080
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 593
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : -0.96000
REMARK 3 B33 (A**2) : 0.57000
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) : 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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.379
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.113 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.214 ; 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 1G8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-99; 01-JAN-00
REMARK 200 TEMPERATURE (KELVIN) : 95.0; NULL
REMARK 200 PH : 6.5; 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 5
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X26C; X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1; 0.98
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66845
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.15
REMARK 200 R MERGE FOR SHELL (I) : 0.67400
REMARK 200 R SYM FOR SHELL (I) : 0.67400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CALCIUM ACETATE, CACODYLAIC
REMARK 280 ACID, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K.
REMARK 280 PEG 6000, CALCIUM ACETATE, CACODYLAIC ACID, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 44.16150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.36950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.70700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.36950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.16150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.70700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 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 PHE A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 410
REMARK 465 LEU A 411
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 PHE B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 410
REMARK 465 LEU B 411
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 82 -80.06 -44.55
REMARK 500 GLN A 84 86.42 -169.79
REMARK 500 ASP A 198 -94.35 -50.59
REMARK 500 ASP A 228 73.55 -60.20
REMARK 500 ASP A 259 -176.07 -175.91
REMARK 500 LYS A 282 -54.36 175.53
REMARK 500 LEU A 311 -54.55 -120.37
REMARK 500 PRO A 328 146.90 -29.55
REMARK 500 ASP A 358 21.17 -73.65
REMARK 500 SER B 70 -17.43 -47.09
REMARK 500 PRO B 73 101.46 -49.86
REMARK 500 TRP B 90 72.36 51.06
REMARK 500 ALA B 92 -75.72 -44.93
REMARK 500 GLN B 114 11.16 -69.85
REMARK 500 ALA B 128 -154.81 -99.62
REMARK 500 GLN B 134 126.13 -36.42
REMARK 500 ASN B 135 18.00 52.72
REMARK 500 ASP B 198 -76.86 -29.82
REMARK 500 ASP B 228 65.37 -69.26
REMARK 500 LYS B 282 -59.27 166.98
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 GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 715
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 716
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 717
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 718
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G8R RELATED DB: PDB
REMARK 900 1G8R CONTAINS THE SAME PROTEIN
DBREF 1G8L A 1 411 UNP P12281 MOEA_ECOLI 1 411
DBREF 1G8L B 1 411 UNP P12281 MOEA_ECOLI 1 411
SEQRES 1 A 411 MET GLU PHE THR THR GLY LEU MET SER LEU ASP THR ALA
SEQRES 2 A 411 LEU ASN GLU MET LEU SER ARG VAL THR PRO LEU THR ALA
SEQRES 3 A 411 GLN GLU THR LEU PRO LEU VAL GLN CYS PHE GLY ARG ILE
SEQRES 4 A 411 LEU ALA SER ASP VAL VAL SER PRO LEU ASP VAL PRO GLY
SEQRES 5 A 411 PHE ASP ASN SER ALA MET ASP GLY TYR ALA VAL ARG LEU
SEQRES 6 A 411 ALA ASP ILE ALA SER GLY GLN PRO LEU PRO VAL ALA GLY
SEQRES 7 A 411 LYS SER PHE ALA GLY GLN PRO TYR HIS GLY GLU TRP PRO
SEQRES 8 A 411 ALA GLY THR CYS ILE ARG ILE MET THR GLY ALA PRO VAL
SEQRES 9 A 411 PRO GLU GLY CYS GLU ALA VAL VAL MET GLN GLU GLN THR
SEQRES 10 A 411 GLU GLN MET ASP ASN GLY VAL ARG PHE THR ALA GLU VAL
SEQRES 11 A 411 ARG SER GLY GLN ASN ILE ARG ARG ARG GLY GLU ASP ILE
SEQRES 12 A 411 SER ALA GLY ALA VAL VAL PHE PRO ALA GLY THR ARG LEU
SEQRES 13 A 411 THR THR ALA GLU LEU PRO VAL ILE ALA SER LEU GLY ILE
SEQRES 14 A 411 ALA GLU VAL PRO VAL ILE ARG LYS VAL ARG VAL ALA LEU
SEQRES 15 A 411 PHE SER THR GLY ASP GLU LEU GLN LEU PRO GLY GLN PRO
SEQRES 16 A 411 LEU GLY ASP GLY GLN ILE TYR ASP THR ASN ARG LEU ALA
SEQRES 17 A 411 VAL HIS LEU MET LEU GLU GLN LEU GLY CYS GLU VAL ILE
SEQRES 18 A 411 ASN LEU GLY ILE ILE ARG ASP ASP PRO HIS ALA LEU ARG
SEQRES 19 A 411 ALA ALA PHE ILE GLU ALA ASP SER GLN ALA ASP VAL VAL
SEQRES 20 A 411 ILE SER SER GLY GLY VAL SER VAL GLY GLU ALA ASP TYR
SEQRES 21 A 411 THR LYS THR ILE LEU GLU GLU LEU GLY GLU ILE ALA PHE
SEQRES 22 A 411 TRP LYS LEU ALA ILE LYS PRO GLY LYS PRO PHE ALA PHE
SEQRES 23 A 411 GLY LYS LEU SER ASN SER TRP PHE CYS GLY LEU PRO GLY
SEQRES 24 A 411 ASN PRO VAL SER ALA THR LEU THR PHE TYR GLN LEU VAL
SEQRES 25 A 411 GLN PRO LEU LEU ALA LYS LEU SER GLY ASN THR ALA SER
SEQRES 26 A 411 GLY LEU PRO ALA ARG GLN ARG VAL ARG THR ALA SER ARG
SEQRES 27 A 411 LEU LYS LYS THR PRO GLY ARG LEU ASP PHE GLN ARG GLY
SEQRES 28 A 411 VAL LEU GLN ARG ASN ALA ASP GLY GLU LEU GLU VAL THR
SEQRES 29 A 411 THR THR GLY HIS GLN GLY SER HIS ILE PHE SER SER PHE
SEQRES 30 A 411 SER LEU GLY ASN CYS PHE ILE VAL LEU GLU ARG ASP ARG
SEQRES 31 A 411 GLY ASN VAL GLU VAL GLY GLU TRP VAL GLU VAL GLU PRO
SEQRES 32 A 411 PHE ASN ALA LEU PHE GLY GLY LEU
SEQRES 1 B 411 MET GLU PHE THR THR GLY LEU MET SER LEU ASP THR ALA
SEQRES 2 B 411 LEU ASN GLU MET LEU SER ARG VAL THR PRO LEU THR ALA
SEQRES 3 B 411 GLN GLU THR LEU PRO LEU VAL GLN CYS PHE GLY ARG ILE
SEQRES 4 B 411 LEU ALA SER ASP VAL VAL SER PRO LEU ASP VAL PRO GLY
SEQRES 5 B 411 PHE ASP ASN SER ALA MET ASP GLY TYR ALA VAL ARG LEU
SEQRES 6 B 411 ALA ASP ILE ALA SER GLY GLN PRO LEU PRO VAL ALA GLY
SEQRES 7 B 411 LYS SER PHE ALA GLY GLN PRO TYR HIS GLY GLU TRP PRO
SEQRES 8 B 411 ALA GLY THR CYS ILE ARG ILE MET THR GLY ALA PRO VAL
SEQRES 9 B 411 PRO GLU GLY CYS GLU ALA VAL VAL MET GLN GLU GLN THR
SEQRES 10 B 411 GLU GLN MET ASP ASN GLY VAL ARG PHE THR ALA GLU VAL
SEQRES 11 B 411 ARG SER GLY GLN ASN ILE ARG ARG ARG GLY GLU ASP ILE
SEQRES 12 B 411 SER ALA GLY ALA VAL VAL PHE PRO ALA GLY THR ARG LEU
SEQRES 13 B 411 THR THR ALA GLU LEU PRO VAL ILE ALA SER LEU GLY ILE
SEQRES 14 B 411 ALA GLU VAL PRO VAL ILE ARG LYS VAL ARG VAL ALA LEU
SEQRES 15 B 411 PHE SER THR GLY ASP GLU LEU GLN LEU PRO GLY GLN PRO
SEQRES 16 B 411 LEU GLY ASP GLY GLN ILE TYR ASP THR ASN ARG LEU ALA
SEQRES 17 B 411 VAL HIS LEU MET LEU GLU GLN LEU GLY CYS GLU VAL ILE
SEQRES 18 B 411 ASN LEU GLY ILE ILE ARG ASP ASP PRO HIS ALA LEU ARG
SEQRES 19 B 411 ALA ALA PHE ILE GLU ALA ASP SER GLN ALA ASP VAL VAL
SEQRES 20 B 411 ILE SER SER GLY GLY VAL SER VAL GLY GLU ALA ASP TYR
SEQRES 21 B 411 THR LYS THR ILE LEU GLU GLU LEU GLY GLU ILE ALA PHE
SEQRES 22 B 411 TRP LYS LEU ALA ILE LYS PRO GLY LYS PRO PHE ALA PHE
SEQRES 23 B 411 GLY LYS LEU SER ASN SER TRP PHE CYS GLY LEU PRO GLY
SEQRES 24 B 411 ASN PRO VAL SER ALA THR LEU THR PHE TYR GLN LEU VAL
SEQRES 25 B 411 GLN PRO LEU LEU ALA LYS LEU SER GLY ASN THR ALA SER
SEQRES 26 B 411 GLY LEU PRO ALA ARG GLN ARG VAL ARG THR ALA SER ARG
SEQRES 27 B 411 LEU LYS LYS THR PRO GLY ARG LEU ASP PHE GLN ARG GLY
SEQRES 28 B 411 VAL LEU GLN ARG ASN ALA ASP GLY GLU LEU GLU VAL THR
SEQRES 29 B 411 THR THR GLY HIS GLN GLY SER HIS ILE PHE SER SER PHE
SEQRES 30 B 411 SER LEU GLY ASN CYS PHE ILE VAL LEU GLU ARG ASP ARG
SEQRES 31 B 411 GLY ASN VAL GLU VAL GLY GLU TRP VAL GLU VAL GLU PRO
SEQRES 32 B 411 PHE ASN ALA LEU PHE GLY GLY LEU
HET GOL A 701 6
HET GOL A 704 6
HET GOL A 706 6
HET GOL A 709 6
HET GOL A 714 6
HET GOL A 715 6
HET GOL A 717 6
HET GOL B 702 6
HET GOL B 703 6
HET GOL B 705 6
HET GOL B 707 6
HET GOL B 708 6
HET GOL B 710 6
HET GOL B 711 6
HET GOL B 712 6
HET GOL B 713 6
HET GOL B 716 6
HET GOL B 718 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 18(C3 H8 O3)
FORMUL 21 HOH *593(H2 O)
HELIX 1 1 SER A 9 VAL A 21 1 13
HELIX 2 2 VAL A 33 CYS A 35 5 3
HELIX 3 3 ARG A 64 GLY A 71 1 8
HELIX 4 4 GLU A 160 LEU A 167 1 8
HELIX 5 5 THR A 204 LEU A 216 1 13
HELIX 6 6 ASP A 229 ALA A 244 1 16
HELIX 7 7 ASP A 259 GLY A 269 1 11
HELIX 8 8 ASN A 300 LEU A 311 1 12
HELIX 9 9 LEU A 311 GLY A 321 1 11
HELIX 10 10 SER A 375 GLY A 380 1 6
HELIX 11 11 ASN A 405 GLY A 409 5 5
HELIX 12 12 SER B 9 VAL B 21 1 13
HELIX 13 13 VAL B 33 CYS B 35 5 3
HELIX 14 14 ARG B 64 SER B 70 1 7
HELIX 15 15 GLU B 160 SER B 166 1 7
HELIX 16 16 THR B 204 LEU B 216 1 13
HELIX 17 17 ASP B 229 ALA B 244 1 16
HELIX 18 18 ASP B 259 GLY B 269 1 11
HELIX 19 19 ASN B 300 LEU B 311 1 12
HELIX 20 20 LEU B 311 SER B 320 1 10
HELIX 21 21 PHE B 374 GLY B 380 1 7
HELIX 22 22 ASN B 405 GLY B 409 5 5
SHEET 1 A 2 GLN A 27 PRO A 31 0
SHEET 2 A 2 GLU A 171 ILE A 175 -1 O VAL A 172 N LEU A 30
SHEET 1 B 2 VAL A 44 VAL A 45 0
SHEET 2 B 2 VAL A 148 PHE A 150 -1 N VAL A 149 O VAL A 44
SHEET 1 C 2 ASN A 55 SER A 56 0
SHEET 2 C 2 ILE A 136 ARG A 137 -1 N ARG A 137 O ASN A 55
SHEET 1 D 4 VAL A 76 SER A 80 0
SHEET 2 D 4 CYS A 95 ILE A 98 1 O CYS A 95 N ALA A 77
SHEET 3 D 4 GLY A 60 VAL A 63 -1 O GLY A 60 N ILE A 98
SHEET 4 D 4 ALA A 110 MET A 113 -1 O ALA A 110 N VAL A 63
SHEET 1 E 2 THR A 117 MET A 120 0
SHEET 2 E 2 GLY A 123 PHE A 126 -1 O GLY A 123 N MET A 120
SHEET 1 F 6 GLU A 219 ILE A 226 0
SHEET 2 F 6 ARG A 179 THR A 185 1 N VAL A 180 O GLU A 219
SHEET 3 F 6 VAL A 246 SER A 249 1 O VAL A 246 N ALA A 181
SHEET 4 F 6 TRP A 293 GLY A 296 1 O TRP A 293 N VAL A 247
SHEET 5 F 6 PRO A 283 LYS A 288 -1 O ALA A 285 N GLY A 296
SHEET 6 F 6 GLU A 270 LYS A 275 -1 N GLU A 270 O LYS A 288
SHEET 1 G 2 LEU A 189 GLN A 190 0
SHEET 2 G 2 ILE A 201 TYR A 202 1 O ILE A 201 N GLN A 190
SHEET 1 H 6 ILE A 278 LYS A 279 0
SHEET 2 H 6 LEU A 346 ARG A 355 1 O LEU A 346 N LYS A 279
SHEET 3 H 6 CYS A 382 LEU A 386 -1 O CYS A 382 N GLY A 351
SHEET 4 H 6 TRP A 398 PRO A 403 -1 O GLU A 400 N VAL A 385
SHEET 5 H 6 GLN A 331 THR A 335 -1 O GLN A 331 N VAL A 401
SHEET 6 H 6 LEU A 361 THR A 365 1 O LEU A 361 N ARG A 334
SHEET 1 I 2 GLN B 27 PRO B 31 0
SHEET 2 I 2 GLU B 171 ILE B 175 -1 O VAL B 172 N LEU B 30
SHEET 1 J 2 VAL B 44 VAL B 45 0
SHEET 2 J 2 VAL B 148 PHE B 150 -1 N VAL B 149 O VAL B 44
SHEET 1 K 2 ASN B 55 SER B 56 0
SHEET 2 K 2 ILE B 136 ARG B 137 -1 N ARG B 137 O ASN B 55
SHEET 1 L 4 VAL B 76 SER B 80 0
SHEET 2 L 4 CYS B 95 ILE B 98 1 O CYS B 95 N ALA B 77
SHEET 3 L 4 GLY B 60 VAL B 63 -1 O GLY B 60 N ILE B 98
SHEET 4 L 4 ALA B 110 MET B 113 -1 O ALA B 110 N VAL B 63
SHEET 1 M 2 THR B 117 MET B 120 0
SHEET 2 M 2 GLY B 123 PHE B 126 -1 O GLY B 123 N MET B 120
SHEET 1 N 6 GLU B 219 ILE B 226 0
SHEET 2 N 6 ARG B 179 THR B 185 1 N VAL B 180 O GLU B 219
SHEET 3 N 6 VAL B 246 GLY B 251 1 O VAL B 246 N ALA B 181
SHEET 4 N 6 TRP B 293 GLY B 296 1 O TRP B 293 N VAL B 247
SHEET 5 N 6 PRO B 283 LYS B 288 -1 O ALA B 285 N GLY B 296
SHEET 6 N 6 GLU B 270 LYS B 275 -1 N GLU B 270 O LYS B 288
SHEET 1 0 2 LEU B 189 GLN B 190 0
SHEET 2 0 2 ILE B 201 TYR B 202 1 O ILE B 201 N GLN B 190
SHEET 1 P 6 ILE B 278 LYS B 279 0
SHEET 2 P 6 LEU B 346 ARG B 355 1 O LEU B 346 N LYS B 279
SHEET 3 P 6 LEU B 361 THR B 365 -1 O GLU B 362 N GLN B 354
SHEET 4 P 6 GLN B 331 THR B 335 1 O ARG B 334 N VAL B 363
SHEET 5 P 6 TRP B 398 PRO B 403 -1 N VAL B 399 O VAL B 333
SHEET 6 P 6 CYS B 382 LEU B 386 -1 N PHE B 383 O GLU B 402
CISPEP 1 VAL A 50 PRO A 51 0 -0.15
CISPEP 2 LYS A 279 PRO A 280 0 -1.76
CISPEP 3 VAL B 50 PRO B 51 0 0.98
CISPEP 4 LYS B 279 PRO B 280 0 -1.82
SITE 1 AC1 9 PHE A 374 SER A 375 SER A 378 HOH A 765
SITE 2 AC1 9 HOH A 865 HOH A 934 ILE B 143 PHE B 150
SITE 3 AC1 9 VAL B 163
SITE 1 AC2 7 THR A 157 GLU A 160 HOH A 855 SER B 378
SITE 2 AC2 7 GLY B 380 PHE B 408 HOH B 829
SITE 1 AC3 6 ILE A 143 VAL A 163 PHE B 374 SER B 375
SITE 2 AC3 6 HOH B 837 HOH B 864
SITE 1 AC4 6 SER A 378 PHE A 408 HOH A 723 HOH A 866
SITE 2 AC4 6 GLU B 160 HOH B 800
SITE 1 AC5 8 GLY B 37 ILE B 39 LYS B 177 VAL B 178
SITE 2 AC5 8 LEU B 216 GLY B 217 HOH B 721 HOH B 724
SITE 1 AC6 8 GLY A 37 ARG A 176 LYS A 177 VAL A 178
SITE 2 AC6 8 GLY A 217 SER A 320 HOH A 755 HOH A 881
SITE 1 AC7 7 GLU B 188 ASP B 228 GLY B 252 SER B 254
SITE 2 AC7 7 ASP B 259 HOH B 802 HOH B 862
SITE 1 AC8 7 GLY B 186 ASP B 187 LEU B 189 ILE B 225
SITE 2 AC8 7 ARG B 227 HOH B 812 HOH B 823
SITE 1 AC9 7 PRO A 230 HIS A 231 GOL A 717 HOH A 774
SITE 2 AC9 7 ARG B 179 GLU B 219 ILE B 221
SITE 1 BC1 6 VAL B 255 PRO B 283 PRO B 298 GLY B 299
SITE 2 BC1 6 HOH B 845 HOH B 920
SITE 1 BC2 3 GLY B 281 ARG B 345 HOH B 848
SITE 1 BC3 4 ALA A 145 HOH A 883 GLU B 387 ARG B 390
SITE 1 BC4 4 LEU B 10 ASP B 11 ARG B 330 LEU B 346
SITE 1 BC5 4 SER A 19 VAL A 21 THR A 22 LYS A 318
SITE 1 BC6 5 LYS A 79 GLN A 84 PRO A 85 TYR A 86
SITE 2 BC6 5 HIS A 87
SITE 1 BC7 8 ARG B 176 ARG B 179 ASP B 241 SER B 242
SITE 2 BC7 8 GLN B 243 ALA B 244 ASP B 245 ASN B 291
SITE 1 BC8 4 ASP A 228 ASP A 229 PRO A 230 GOL A 709
SITE 1 BC9 3 THR B 364 THR B 365 GLY B 367
CRYST1 88.323 97.414 98.739 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 0.011322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010265 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010128 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
