HEADER TRANSFERASE 26-NOV-03 1V5V
TITLE CRYSTAL STRUCTURE OF A COMPONENT OF GLYCINE CLEAVAGE SYSTEM: T-PROTEIN
TITLE 2 FROM PYROCOCCUS HORIKOSHII OT3 AT 1.5 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOMETHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLYCINE CLEAVAGE SYSTEM T PROTEIN;
COMPND 5 EC: 2.1.2.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 GENE: GCS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS GLYCINE-CLEAVAGE SYTEM, AMINOMETHYL TRANSFERASE, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.K.LOKANATH,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 5 27-DEC-23 1V5V 1 REMARK
REVDAT 4 13-JUL-11 1V5V 1 VERSN
REVDAT 3 24-FEB-09 1V5V 1 VERSN
REVDAT 2 08-FEB-05 1V5V 1 KEYWDS AUTHOR JRNL
REVDAT 1 26-OCT-04 1V5V 0
JRNL AUTH N.K.LOKANATH,C.KUROISHI,N.OKAZAKI,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF A COMPONENT OF GLYCINE CLEAVAGE SYSTEM:
JRNL TITL 2 T-PROTEIN FROM PYROCOCCUS HORIKOSHII OT3 AT 1.5 A RESOLUTION
JRNL REF PROTEINS V. 58 769 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 15609340
JRNL DOI 10.1002/PROT.20345
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2140110.830
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 141020
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) : 0.197
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 7136
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 21560
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1151
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 547
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 1.81000
REMARK 3 B33 (A**2) : -1.86000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 44.56
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 1V5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.0, 0.91971, 0.92001, 0.92540
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141020
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.04900
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) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, MES, PH 5.9, MICROBATCH,
REMARK 280 TEMPERATURE 295K
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 39.74800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.30250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.04950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.30250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.74800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.04950
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE
REMARK 300 MONOMER USING SYMMETRY OPERATIONS. TWO MOLECULES IN THE ASYMMETRIC
REMARK 300 UNIT OF THE CRYSTAL FORM AS WELL AS IN SOLUTION
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: 4320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ILE A 2
REMARK 465 MET B 1
REMARK 465 ILE B 2
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 OD1 ASP B 301 O HOH B 1724 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 126 NE1 TRP A 126 CE2 0.114
REMARK 500 ARG A 162 CG ARG A 162 CD 0.322
REMARK 500 ARG A 162 CG ARG A 162 CD 0.258
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 ARG A 162 CD - NE - CZ ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 162 NE - CZ - NH1 ANGL. DEV. = -4.8 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 ILE A 10 38.34 -97.42
REMARK 500 SER A 34 -67.08 -102.44
REMARK 500 ALA A 46 -101.77 -137.00
REMARK 500 ASP A 99 156.78 178.51
REMARK 500 PHE A 179 1.59 83.93
REMARK 500 ASN A 265 -68.88 -108.81
REMARK 500 LYS A 268 171.01 179.71
REMARK 500 ASN A 352 34.84 70.76
REMARK 500 ILE B 10 37.40 -97.57
REMARK 500 SER B 34 -70.22 -105.31
REMARK 500 ALA B 46 -101.52 -137.21
REMARK 500 ASP B 99 156.04 178.39
REMARK 500 PHE B 179 -0.40 85.56
REMARK 500 ASN B 265 -72.11 -111.57
REMARK 500 LYS B 268 171.49 179.12
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PHO001001146 RELATED DB: TARGETDB
DBREF 1V5V A 1 401 UNP O58888 GCST_PYRHO 1 401
DBREF 1V5V B 1 401 UNP O58888 GCST_PYRHO 1 401
SEQRES 1 A 401 MET ILE GLN MET VAL LYS ARG VAL HIS ILE PHE ASP TRP
SEQRES 2 A 401 HIS LYS GLU HIS ALA ARG LYS ILE GLU GLU PHE ALA GLY
SEQRES 3 A 401 TRP GLU MET PRO ILE TRP TYR SER SER ILE LYS GLU GLU
SEQRES 4 A 401 HIS LEU ALA VAL ARG ASN ALA VAL GLY ILE PHE ASP VAL
SEQRES 5 A 401 SER HIS MET GLY GLU ILE VAL PHE ARG GLY LYS ASP ALA
SEQRES 6 A 401 LEU LYS PHE LEU GLN TYR VAL THR THR ASN ASP ILE SER
SEQRES 7 A 401 LYS PRO PRO ALA ILE SER GLY THR TYR THR LEU VAL LEU
SEQRES 8 A 401 ASN GLU ARG GLY ALA ILE LYS ASP GLU THR LEU VAL PHE
SEQRES 9 A 401 ASN MET GLY ASN ASN GLU TYR LEU MET ILE CYS ASP SER
SEQRES 10 A 401 ASP ALA PHE GLU LYS LEU TYR ALA TRP PHE THR TYR LEU
SEQRES 11 A 401 LYS ARG THR ILE GLU GLN PHE THR LYS LEU ASP LEU GLU
SEQRES 12 A 401 ILE GLU LEU LYS THR TYR ASP ILE ALA MET PHE ALA VAL
SEQRES 13 A 401 GLN GLY PRO LYS ALA ARG ASP LEU ALA LYS ASP LEU PHE
SEQRES 14 A 401 GLY ILE ASP ILE ASN GLU MET TRP TRP PHE GLN ALA ARG
SEQRES 15 A 401 TRP VAL GLU LEU ASP GLY ILE LYS MET LEU LEU SER ARG
SEQRES 16 A 401 SER GLY TYR THR GLY GLU ASN GLY PHE GLU VAL TYR ILE
SEQRES 17 A 401 GLU ASP ALA ASN PRO TYR HIS PRO ASP GLU SER LYS ARG
SEQRES 18 A 401 GLY GLU PRO GLU LYS ALA LEU HIS VAL TRP GLU ARG ILE
SEQRES 19 A 401 LEU GLU GLU GLY LYS LYS TYR GLY ILE LYS PRO CYS GLY
SEQRES 20 A 401 LEU GLY ALA ARG ASP THR LEU ARG LEU GLU ALA GLY TYR
SEQRES 21 A 401 THR LEU TYR GLY ASN GLU THR LYS GLU LEU GLN LEU LEU
SEQRES 22 A 401 SER THR ASP ILE ASP GLU VAL THR PRO LEU GLN ALA ASN
SEQRES 23 A 401 LEU GLU PHE ALA ILE TYR TRP ASP LYS ASP PHE ILE GLY
SEQRES 24 A 401 LYS ASP ALA LEU LEU LYS GLN LYS GLU ARG GLY VAL GLY
SEQRES 25 A 401 ARG LYS LEU VAL HIS PHE LYS MET ILE ASP LYS GLY ILE
SEQRES 26 A 401 PRO ARG GLU GLY TYR LYS VAL TYR ALA ASN GLY GLU MET
SEQRES 27 A 401 ILE GLY GLU VAL THR SER GLY THR LEU SER PRO LEU LEU
SEQRES 28 A 401 ASN VAL GLY ILE GLY ILE ALA PHE VAL LYS GLU GLU TYR
SEQRES 29 A 401 ALA LYS PRO GLY ILE GLU ILE GLU VAL GLU ILE ARG GLY
SEQRES 30 A 401 GLN ARG LYS LYS ALA VAL THR VAL THR PRO PRO PHE TYR
SEQRES 31 A 401 ASP PRO LYS LYS TYR GLY LEU PHE ARG GLU THR
SEQRES 1 B 401 MET ILE GLN MET VAL LYS ARG VAL HIS ILE PHE ASP TRP
SEQRES 2 B 401 HIS LYS GLU HIS ALA ARG LYS ILE GLU GLU PHE ALA GLY
SEQRES 3 B 401 TRP GLU MET PRO ILE TRP TYR SER SER ILE LYS GLU GLU
SEQRES 4 B 401 HIS LEU ALA VAL ARG ASN ALA VAL GLY ILE PHE ASP VAL
SEQRES 5 B 401 SER HIS MET GLY GLU ILE VAL PHE ARG GLY LYS ASP ALA
SEQRES 6 B 401 LEU LYS PHE LEU GLN TYR VAL THR THR ASN ASP ILE SER
SEQRES 7 B 401 LYS PRO PRO ALA ILE SER GLY THR TYR THR LEU VAL LEU
SEQRES 8 B 401 ASN GLU ARG GLY ALA ILE LYS ASP GLU THR LEU VAL PHE
SEQRES 9 B 401 ASN MET GLY ASN ASN GLU TYR LEU MET ILE CYS ASP SER
SEQRES 10 B 401 ASP ALA PHE GLU LYS LEU TYR ALA TRP PHE THR TYR LEU
SEQRES 11 B 401 LYS ARG THR ILE GLU GLN PHE THR LYS LEU ASP LEU GLU
SEQRES 12 B 401 ILE GLU LEU LYS THR TYR ASP ILE ALA MET PHE ALA VAL
SEQRES 13 B 401 GLN GLY PRO LYS ALA ARG ASP LEU ALA LYS ASP LEU PHE
SEQRES 14 B 401 GLY ILE ASP ILE ASN GLU MET TRP TRP PHE GLN ALA ARG
SEQRES 15 B 401 TRP VAL GLU LEU ASP GLY ILE LYS MET LEU LEU SER ARG
SEQRES 16 B 401 SER GLY TYR THR GLY GLU ASN GLY PHE GLU VAL TYR ILE
SEQRES 17 B 401 GLU ASP ALA ASN PRO TYR HIS PRO ASP GLU SER LYS ARG
SEQRES 18 B 401 GLY GLU PRO GLU LYS ALA LEU HIS VAL TRP GLU ARG ILE
SEQRES 19 B 401 LEU GLU GLU GLY LYS LYS TYR GLY ILE LYS PRO CYS GLY
SEQRES 20 B 401 LEU GLY ALA ARG ASP THR LEU ARG LEU GLU ALA GLY TYR
SEQRES 21 B 401 THR LEU TYR GLY ASN GLU THR LYS GLU LEU GLN LEU LEU
SEQRES 22 B 401 SER THR ASP ILE ASP GLU VAL THR PRO LEU GLN ALA ASN
SEQRES 23 B 401 LEU GLU PHE ALA ILE TYR TRP ASP LYS ASP PHE ILE GLY
SEQRES 24 B 401 LYS ASP ALA LEU LEU LYS GLN LYS GLU ARG GLY VAL GLY
SEQRES 25 B 401 ARG LYS LEU VAL HIS PHE LYS MET ILE ASP LYS GLY ILE
SEQRES 26 B 401 PRO ARG GLU GLY TYR LYS VAL TYR ALA ASN GLY GLU MET
SEQRES 27 B 401 ILE GLY GLU VAL THR SER GLY THR LEU SER PRO LEU LEU
SEQRES 28 B 401 ASN VAL GLY ILE GLY ILE ALA PHE VAL LYS GLU GLU TYR
SEQRES 29 B 401 ALA LYS PRO GLY ILE GLU ILE GLU VAL GLU ILE ARG GLY
SEQRES 30 B 401 GLN ARG LYS LYS ALA VAL THR VAL THR PRO PRO PHE TYR
SEQRES 31 B 401 ASP PRO LYS LYS TYR GLY LEU PHE ARG GLU THR
HET GOL A 901 6
HET GOL B 902 6
HET PEG B1503 7
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 HOH *547(H2 O)
HELIX 1 1 ILE A 10 ALA A 18 1 9
HELIX 2 2 SER A 35 ALA A 46 1 12
HELIX 3 3 ASP A 64 THR A 73 1 10
HELIX 4 4 ALA A 119 GLN A 136 1 18
HELIX 5 5 LYS A 160 GLY A 170 1 11
HELIX 6 6 ASP A 172 MET A 176 5 5
HELIX 7 7 ASP A 217 ARG A 221 5 5
HELIX 8 8 PRO A 224 LYS A 239 1 16
HELIX 9 9 LYS A 240 GLY A 242 5 3
HELIX 10 10 GLY A 247 GLY A 259 1 13
HELIX 11 11 LEU A 287 ILE A 291 5 5
HELIX 12 12 GLY A 299 GLY A 310 1 12
HELIX 13 13 GLU A 363 ALA A 365 5 3
HELIX 14 14 ILE B 10 ALA B 18 1 9
HELIX 15 15 SER B 35 ALA B 46 1 12
HELIX 16 16 ASP B 64 THR B 73 1 10
HELIX 17 17 ALA B 119 GLU B 135 1 17
HELIX 18 18 LYS B 160 GLY B 170 1 11
HELIX 19 19 ASP B 172 MET B 176 5 5
HELIX 20 20 ASP B 217 ARG B 221 5 5
HELIX 21 21 PRO B 224 LYS B 239 1 16
HELIX 22 22 LYS B 240 GLY B 242 5 3
HELIX 23 23 GLY B 247 GLY B 259 1 13
HELIX 24 24 LEU B 287 ILE B 291 5 5
HELIX 25 25 GLY B 299 GLY B 310 1 12
HELIX 26 26 GLU B 363 ALA B 365 5 3
SHEET 1 A 2 LYS A 20 PHE A 24 0
SHEET 2 A 2 TRP A 27 TRP A 32 -1 O TRP A 27 N PHE A 24
SHEET 1 B 6 ALA A 181 LEU A 186 0
SHEET 2 B 6 ILE A 189 SER A 194 -1 O MET A 191 N VAL A 184
SHEET 3 B 6 GLY A 203 GLU A 209 -1 O GLU A 205 N SER A 194
SHEET 4 B 6 ILE A 151 GLN A 157 -1 N ALA A 152 O ILE A 208
SHEET 5 B 6 GLY A 48 ASP A 51 -1 N PHE A 50 O ALA A 155
SHEET 6 B 6 LYS A 244 CYS A 246 1 O CYS A 246 N ILE A 49
SHEET 1 C 5 SER A 84 LEU A 91 0
SHEET 2 C 5 ILE A 97 GLY A 107 -1 O LYS A 98 N VAL A 90
SHEET 3 C 5 GLU A 110 CYS A 115 -1 O LEU A 112 N PHE A 104
SHEET 4 C 5 GLY A 56 ARG A 61 -1 N ILE A 58 O MET A 113
SHEET 5 C 5 GLU A 143 LEU A 146 -1 O GLU A 145 N VAL A 59
SHEET 1 D 7 ARG A 313 MET A 320 0
SHEET 2 D 7 GLY A 354 LYS A 361 -1 O VAL A 360 N LYS A 314
SHEET 3 D 7 GLU A 337 LEU A 347 -1 N THR A 346 O ILE A 355
SHEET 4 D 7 LYS A 331 ALA A 334 -1 N VAL A 332 O GLY A 340
SHEET 5 D 7 GLU A 370 ILE A 375 -1 O GLU A 372 N TYR A 333
SHEET 6 D 7 GLN A 378 VAL A 385 -1 O GLN A 378 N ILE A 375
SHEET 7 D 7 ARG A 313 MET A 320 -1 N LYS A 319 O VAL A 383
SHEET 1 E 2 LYS B 20 PHE B 24 0
SHEET 2 E 2 TRP B 27 TRP B 32 -1 O TRP B 27 N PHE B 24
SHEET 1 F 6 ALA B 181 LEU B 186 0
SHEET 2 F 6 ILE B 189 SER B 194 -1 O MET B 191 N VAL B 184
SHEET 3 F 6 GLY B 203 GLU B 209 -1 O GLU B 205 N SER B 194
SHEET 4 F 6 ILE B 151 GLN B 157 -1 N ALA B 152 O ILE B 208
SHEET 5 F 6 GLY B 48 ASP B 51 -1 N PHE B 50 O ALA B 155
SHEET 6 F 6 LYS B 244 CYS B 246 1 O CYS B 246 N ILE B 49
SHEET 1 G 5 SER B 84 LEU B 91 0
SHEET 2 G 5 ILE B 97 ASN B 105 -1 O LYS B 98 N VAL B 90
SHEET 3 G 5 GLU B 110 CYS B 115 -1 O LEU B 112 N PHE B 104
SHEET 4 G 5 GLY B 56 ARG B 61 -1 N ILE B 58 O MET B 113
SHEET 5 G 5 GLU B 143 LEU B 146 -1 O GLU B 143 N ARG B 61
SHEET 1 H 7 ARG B 313 MET B 320 0
SHEET 2 H 7 GLY B 354 LYS B 361 -1 O VAL B 360 N LYS B 314
SHEET 3 H 7 GLU B 337 LEU B 347 -1 N GLU B 341 O PHE B 359
SHEET 4 H 7 LYS B 331 ALA B 334 -1 N VAL B 332 O ILE B 339
SHEET 5 H 7 GLU B 370 ILE B 375 -1 O GLU B 372 N TYR B 333
SHEET 6 H 7 GLN B 378 VAL B 385 -1 O GLN B 378 N ILE B 375
SHEET 7 H 7 ARG B 313 MET B 320 -1 N HIS B 317 O VAL B 385
CISPEP 1 ALA A 82 ILE A 83 0 -0.34
CISPEP 2 GLU A 279 VAL A 280 0 1.13
CISPEP 3 PRO A 387 PRO A 388 0 -0.10
CISPEP 4 ALA B 82 ILE B 83 0 -0.72
CISPEP 5 GLU B 279 VAL B 280 0 0.66
CISPEP 6 PRO B 387 PRO B 388 0 0.05
SITE 1 AC1 8 VAL A 316 HIS A 317 ALA A 365 PRO A 367
SITE 2 AC1 8 VAL A 385 HOH A1070 HOH A1110 HOH A1113
SITE 1 AC2 7 VAL B 316 HIS B 317 ALA B 365 LYS B 366
SITE 2 AC2 7 PRO B 367 VAL B 385 HOH B1728
SITE 1 AC3 3 PHE A 398 LYS B 79 TRP B 177
CRYST1 79.496 96.099 118.605 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 0.012579 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010406 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008431 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
