HEADER TRANSFERASE 04-MAR-07 2P1C
TITLE T. BRUCEI FARNESYL DIPHOSPHATE SYNTHASE COMPLEXED WITH BISPHOSPHONATE
TITLE 2 BPH-210
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FARNESYL PYROPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-BISPHOSPHONATE COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CAO,Y.GAO,E.OLDFIELD
REVDAT 6 30-AUG-23 2P1C 1 REMARK SEQADV
REVDAT 5 13-JUL-11 2P1C 1 VERSN
REVDAT 4 24-FEB-09 2P1C 1 VERSN
REVDAT 3 16-SEP-08 2P1C 1 JRNL
REVDAT 2 13-MAY-08 2P1C 1 JRNL
REVDAT 1 04-MAR-08 2P1C 0
JRNL AUTH R.CAO,C.K.CHEN,R.T.GUO,A.H.WANG,E.OLDFIELD
JRNL TITL STRUCTURES OF A POTENT PHENYLALKYL BISPHOSPHONATE INHIBITOR
JRNL TITL 2 BOUND TO FARNESYL AND GERANYLGERANYL DIPHOSPHATE SYNTHASES.
JRNL REF PROTEINS V. 73 431 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18442135
JRNL DOI 10.1002/PROT.22066
REMARK 2
REMARK 2 RESOLUTION. 2.45 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 110118.030
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 28696
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) : 0.266
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 859
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2033
REMARK 3 BIN R VALUE (WORKING SET) : 0.4310
REMARK 3 BIN FREE R VALUE : 0.4280
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 55
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.058
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5704
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.21000
REMARK 3 B22 (A**2) : 9.21000
REMARK 3 B33 (A**2) : -18.43000
REMARK 3 B12 (A**2) : 7.64000
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) : 0.41
REMARK 3 ESD FROM SIGMAA (A) : 0.51
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) : 0.56
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 2.770 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.970 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.390 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.620 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 50.49
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 2P1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 123.2
REMARK 200 PH : 5.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34615
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2EWG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPD, 0.1 AMMONIUM ACETATE, PH
REMARK 280 5.75, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.24900
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 118.49800
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 118.49800
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.24900
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 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 -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 VAL A -8
REMARK 465 PRO A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 SER A 0
REMARK 465 LEU A 64
REMARK 465 SER A 65
REMARK 465 PRO A 66
REMARK 465 ASN A 67
REMARK 465 ASN A 68
REMARK 465 ASN A 69
REMARK 465 GLY A 70
REMARK 465 GLU A 71
REMARK 465 GLU A 72
REMARK 465 ASP A 73
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 VAL B -8
REMARK 465 PRO B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 SER B 0
REMARK 465 LEU B 64
REMARK 465 SER B 65
REMARK 465 PRO B 66
REMARK 465 ASN B 67
REMARK 465 ASN B 68
REMARK 465 ASN B 69
REMARK 465 GLY B 70
REMARK 465 GLU B 71
REMARK 465 GLU B 72
REMARK 465 ASP B 73
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 ASP A 123 CG OD1 OD2
REMARK 470 ARG A 266 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 123 CG OD1 OD2
REMARK 470 GLN B 191 CG CD OE1 NE2
REMARK 470 ARG B 266 CG CD NE CZ NH1 NH2
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 LEU A 62 6.80 -67.05
REMARK 500 PRO A 122 -38.34 -33.25
REMARK 500 ASP A 150 64.25 -103.19
REMARK 500 ASP A 181 99.62 -57.86
REMARK 500 ASN B 108 59.40 34.92
REMARK 500 CYS B 117 150.10 -47.58
REMARK 500 ASP B 181 107.43 -58.18
REMARK 500 ASP B 186 112.80 -163.17
REMARK 500 PRO B 187 -25.79 -35.24
REMARK 500 THR B 194 136.58 -33.40
REMARK 500 THR B 213 -65.93 -134.49
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 MG A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 8001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 8003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 8002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GG3 A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GG3 B 8004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 9001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EWG RELATED DB: PDB
REMARK 900 RELATED ID: 2OGC RELATED DB: PDB
REMARK 900 RELATED ID: 2OGD RELATED DB: PDB
REMARK 900 RELATED ID: 2OGL RELATED DB: PDB
DBREF 2P1C A 1 367 UNP Q86C09 Q86C09_9TRYP 1 367
DBREF 2P1C B 1 367 UNP Q86C09 Q86C09_9TRYP 1 367
SEQADV 2P1C MET A -22 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY A -21 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A -20 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A -19 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -18 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -17 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -16 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -15 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -14 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -13 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A -12 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A -11 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY A -10 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C LEU A -9 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C VAL A -8 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C PRO A -7 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C ARG A -6 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY A -5 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A -4 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS A -3 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C MET A -2 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C ALA A -1 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER A 0 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C MET B -22 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY B -21 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B -20 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B -19 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -18 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -17 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -16 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -15 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -14 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -13 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B -12 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B -11 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY B -10 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C LEU B -9 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C VAL B -8 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C PRO B -7 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C ARG B -6 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C GLY B -5 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B -4 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C HIS B -3 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C MET B -2 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C ALA B -1 UNP Q86C09 EXPRESSION TAG
SEQADV 2P1C SER B 0 UNP Q86C09 EXPRESSION TAG
SEQRES 1 A 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 390 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET PRO MET
SEQRES 3 A 390 GLN MET PHE MET GLN VAL TYR ASP GLU ILE GLN MET PHE
SEQRES 4 A 390 LEU LEU GLU GLU LEU GLU LEU LYS PHE ASP MET ASP PRO
SEQRES 5 A 390 ASN ARG VAL ARG TYR LEU ARG LYS MET MET ASP THR THR
SEQRES 6 A 390 CYS LEU GLY GLY LYS TYR ASN ARG GLY LEU THR VAL ILE
SEQRES 7 A 390 ASP VAL ALA GLU SER LEU LEU SER LEU SER PRO ASN ASN
SEQRES 8 A 390 ASN GLY GLU GLU ASP ASP GLY ALA ARG ARG LYS ARG VAL
SEQRES 9 A 390 LEU HIS ASP ALA CYS VAL CYS GLY TRP MET ILE GLU PHE
SEQRES 10 A 390 LEU GLN ALA HIS TYR LEU VAL GLU ASP ASP ILE MET ASP
SEQRES 11 A 390 ASN SER VAL THR ARG ARG GLY LYS PRO CYS TRP TYR ARG
SEQRES 12 A 390 HIS PRO ASP VAL THR VAL GLN CYS ALA ILE ASN ASP GLY
SEQRES 13 A 390 LEU LEU LEU LYS SER TRP THR HIS MET MET ALA MET HIS
SEQRES 14 A 390 PHE PHE ALA ASP ARG PRO PHE LEU GLN ASP LEU LEU CYS
SEQRES 15 A 390 ARG PHE ASN ARG VAL ASP TYR THR THR ALA VAL GLY GLN
SEQRES 16 A 390 LEU TYR ASP VAL THR SER MET PHE ASP SER ASN LYS LEU
SEQRES 17 A 390 ASP PRO ASP VAL SER GLN PRO THR THR THR ASP PHE ALA
SEQRES 18 A 390 GLU PHE THR LEU SER ASN TYR LYS ARG ILE VAL LYS TYR
SEQRES 19 A 390 LYS THR ALA TYR TYR THR TYR LEU LEU PRO LEU VAL MET
SEQRES 20 A 390 GLY LEU ILE VAL SER GLU ALA LEU PRO THR VAL ASP MET
SEQRES 21 A 390 GLY VAL THR GLU GLU LEU ALA MET LEU MET GLY GLU TYR
SEQRES 22 A 390 PHE GLN VAL GLN ASP ASP VAL MET ASP CYS PHE THR PRO
SEQRES 23 A 390 PRO GLU ARG LEU GLY LYS VAL GLY THR ASP ILE GLN ASP
SEQRES 24 A 390 ALA LYS CYS SER TRP LEU ALA VAL THR PHE LEU ALA LYS
SEQRES 25 A 390 ALA SER SER ALA GLN VAL ALA GLU PHE LYS ALA ASN TYR
SEQRES 26 A 390 GLY SER GLY ASP SER GLU LYS VAL ALA THR VAL ARG ARG
SEQRES 27 A 390 LEU TYR GLU GLU ALA ASP LEU GLN GLY ASP TYR VAL ALA
SEQRES 28 A 390 TYR GLU ALA ALA VAL ALA GLU GLN VAL LYS GLU LEU ILE
SEQRES 29 A 390 GLU LYS LEU ARG LEU CYS SER PRO GLY PHE ALA ALA SER
SEQRES 30 A 390 VAL GLU THR LEU TRP GLY LYS THR TYR LYS ARG GLN LYS
SEQRES 1 B 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 390 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET PRO MET
SEQRES 3 B 390 GLN MET PHE MET GLN VAL TYR ASP GLU ILE GLN MET PHE
SEQRES 4 B 390 LEU LEU GLU GLU LEU GLU LEU LYS PHE ASP MET ASP PRO
SEQRES 5 B 390 ASN ARG VAL ARG TYR LEU ARG LYS MET MET ASP THR THR
SEQRES 6 B 390 CYS LEU GLY GLY LYS TYR ASN ARG GLY LEU THR VAL ILE
SEQRES 7 B 390 ASP VAL ALA GLU SER LEU LEU SER LEU SER PRO ASN ASN
SEQRES 8 B 390 ASN GLY GLU GLU ASP ASP GLY ALA ARG ARG LYS ARG VAL
SEQRES 9 B 390 LEU HIS ASP ALA CYS VAL CYS GLY TRP MET ILE GLU PHE
SEQRES 10 B 390 LEU GLN ALA HIS TYR LEU VAL GLU ASP ASP ILE MET ASP
SEQRES 11 B 390 ASN SER VAL THR ARG ARG GLY LYS PRO CYS TRP TYR ARG
SEQRES 12 B 390 HIS PRO ASP VAL THR VAL GLN CYS ALA ILE ASN ASP GLY
SEQRES 13 B 390 LEU LEU LEU LYS SER TRP THR HIS MET MET ALA MET HIS
SEQRES 14 B 390 PHE PHE ALA ASP ARG PRO PHE LEU GLN ASP LEU LEU CYS
SEQRES 15 B 390 ARG PHE ASN ARG VAL ASP TYR THR THR ALA VAL GLY GLN
SEQRES 16 B 390 LEU TYR ASP VAL THR SER MET PHE ASP SER ASN LYS LEU
SEQRES 17 B 390 ASP PRO ASP VAL SER GLN PRO THR THR THR ASP PHE ALA
SEQRES 18 B 390 GLU PHE THR LEU SER ASN TYR LYS ARG ILE VAL LYS TYR
SEQRES 19 B 390 LYS THR ALA TYR TYR THR TYR LEU LEU PRO LEU VAL MET
SEQRES 20 B 390 GLY LEU ILE VAL SER GLU ALA LEU PRO THR VAL ASP MET
SEQRES 21 B 390 GLY VAL THR GLU GLU LEU ALA MET LEU MET GLY GLU TYR
SEQRES 22 B 390 PHE GLN VAL GLN ASP ASP VAL MET ASP CYS PHE THR PRO
SEQRES 23 B 390 PRO GLU ARG LEU GLY LYS VAL GLY THR ASP ILE GLN ASP
SEQRES 24 B 390 ALA LYS CYS SER TRP LEU ALA VAL THR PHE LEU ALA LYS
SEQRES 25 B 390 ALA SER SER ALA GLN VAL ALA GLU PHE LYS ALA ASN TYR
SEQRES 26 B 390 GLY SER GLY ASP SER GLU LYS VAL ALA THR VAL ARG ARG
SEQRES 27 B 390 LEU TYR GLU GLU ALA ASP LEU GLN GLY ASP TYR VAL ALA
SEQRES 28 B 390 TYR GLU ALA ALA VAL ALA GLU GLN VAL LYS GLU LEU ILE
SEQRES 29 B 390 GLU LYS LEU ARG LEU CYS SER PRO GLY PHE ALA ALA SER
SEQRES 30 B 390 VAL GLU THR LEU TRP GLY LYS THR TYR LYS ARG GLN LYS
HET MG A3002 1
HET MG A3003 1
HET MG A3004 1
HET ACT A8001 4
HET ACT A8003 4
HET GG3 A3001 24
HET MG B4001 1
HET MG B4002 1
HET MG B4003 1
HET ACT B8002 4
HET GG3 B8004 24
HET BME B9001 4
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
HETNAM GG3 {1-HYDROXY-3-[METHYL(4-PHENYLBUTYL)AMINO]PROPANE-1,1-
HETNAM 2 GG3 DIYL}BIS(PHOSPHONIC ACID)
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 MG 6(MG 2+)
FORMUL 6 ACT 3(C2 H3 O2 1-)
FORMUL 8 GG3 2(C14 H25 N O7 P2)
FORMUL 14 BME C2 H6 O S
FORMUL 15 HOH *306(H2 O)
HELIX 1 1 MET A 1 LYS A 24 1 24
HELIX 2 2 ASP A 28 LEU A 44 1 17
HELIX 3 3 TYR A 48 LEU A 62 1 15
HELIX 4 4 ASP A 74 ASP A 107 1 34
HELIX 5 5 TRP A 118 HIS A 121 5 4
HELIX 6 6 THR A 125 PHE A 148 1 24
HELIX 7 7 PHE A 153 THR A 177 1 25
HELIX 8 8 ASP A 181 LEU A 185 5 5
HELIX 9 9 THR A 201 THR A 213 1 13
HELIX 10 10 THR A 213 TYR A 218 1 6
HELIX 11 11 TYR A 218 SER A 229 1 12
HELIX 12 12 ALA A 231 VAL A 235 5 5
HELIX 13 13 ASP A 236 THR A 262 1 27
HELIX 14 14 PRO A 263 GLY A 268 1 6
HELIX 15 15 SER A 280 ALA A 290 1 11
HELIX 16 16 SER A 291 ALA A 300 1 10
HELIX 17 17 ASP A 306 ALA A 320 1 15
HELIX 18 18 ASP A 321 SER A 348 1 28
HELIX 19 19 SER A 348 TYR A 363 1 16
HELIX 20 20 MET B 1 LYS B 24 1 24
HELIX 21 21 ASP B 28 LEU B 44 1 17
HELIX 22 22 TYR B 48 LEU B 62 1 15
HELIX 23 23 GLY B 75 ASP B 107 1 33
HELIX 24 24 TRP B 118 HIS B 121 5 4
HELIX 25 25 THR B 125 ALA B 149 1 25
HELIX 26 26 PHE B 153 THR B 177 1 25
HELIX 27 27 THR B 201 THR B 213 1 13
HELIX 28 28 THR B 213 TYR B 218 1 6
HELIX 29 29 TYR B 218 VAL B 228 1 11
HELIX 30 30 ALA B 231 VAL B 235 5 5
HELIX 31 31 ASP B 236 THR B 262 1 27
HELIX 32 32 PRO B 263 GLY B 268 1 6
HELIX 33 33 SER B 280 ALA B 288 1 9
HELIX 34 34 SER B 291 TYR B 302 1 12
HELIX 35 35 ASP B 306 ALA B 320 1 15
HELIX 36 36 LEU B 322 SER B 348 1 27
HELIX 37 37 SER B 348 TYR B 363 1 16
SHEET 1 A 2 THR A 111 ARG A 112 0
SHEET 2 A 2 LYS A 115 PRO A 116 -1 O LYS A 115 N ARG A 112
SHEET 1 B 2 THR B 111 ARG B 112 0
SHEET 2 B 2 LYS B 115 PRO B 116 -1 O LYS B 115 N ARG B 112
SITE 1 AC1 4 ASP A 103 ASP A 107 HOH A8124 HOH A8135
SITE 1 AC2 4 ASP A 255 ASP A 259 ASP A 273 HOH A8112
SITE 1 AC3 6 ASP A 103 ASP A 107 GLN A 172 ASP A 175
SITE 2 AC3 6 LYS A 278 HOH A8115
SITE 1 AC4 4 ASP B 103 ASP B 107 SER B 109 HOH B9150
SITE 1 AC5 5 ASP B 255 ASP B 259 ASP B 273 HOH B9103
SITE 2 AC5 5 HOH B9131
SITE 1 AC6 3 ASP B 103 ASP B 107 ASP B 175
SITE 1 AC7 3 GLN A 96 ARG A 113 HOH A8019
SITE 1 AC8 6 GLY A 46 LYS A 47 ASN A 49 HOH A8019
SITE 2 AC8 6 HOH A8033 HOH A8043
SITE 1 AC9 4 GLN B 96 ARG B 113 HOH B9025 HOH B9124
SITE 1 BC1 19 TYR A 99 ASP A 103 MET A 106 ASP A 107
SITE 2 BC1 19 ARG A 112 THR A 168 ALA A 169 GLN A 172
SITE 3 BC1 19 LYS A 212 THR A 213 TYR A 216 GLN A 252
SITE 4 BC1 19 ASP A 255 LYS A 269 HOH A8112 HOH A8115
SITE 5 BC1 19 HOH A8133 ASN B 131 LEU B 134
SITE 1 BC2 17 ASN A 131 LEU A 134 TYR B 99 ASP B 103
SITE 2 BC2 17 ASP B 107 ARG B 112 THR B 168 GLN B 172
SITE 3 BC2 17 LYS B 212 THR B 213 TYR B 216 ASP B 255
SITE 4 BC2 17 LYS B 269 HOH B9103 HOH B9123 HOH B9131
SITE 5 BC2 17 HOH B9150
SITE 1 BC3 4 ASP B 156 CYS B 159 ARG B 160 ARG B 163
CRYST1 92.124 92.124 177.747 90.00 90.00 120.00 P 31 2 1 12
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 0.010855 0.006267 0.000000 0.00000
SCALE2 0.000000 0.012534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005626 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
