HEADER TRANSFERASE 13-AUG-06 2I19
TITLE T. BRUCEI FARNESYL DIPHOSPHATE SYNTHASE COMPLEXED WITH BISPHOSPHONATE
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;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28A+
KEYWDS PROTEIN-BISPHOSPHONATE COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CAO,J.MAO,Y.GAO,H.ROBINSON,S.ODEH,A.GODDARD,E.OLDFIELD
REVDAT 5 30-AUG-23 2I19 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 2I19 1 VERSN
REVDAT 3 12-DEC-06 2I19 1 REMARK
REVDAT 2 21-NOV-06 2I19 1 JRNL
REVDAT 1 17-OCT-06 2I19 0
JRNL AUTH J.MAO,S.MUKHERJEE,Y.ZHANG,R.CAO,J.M.SANDERS,Y.SONG,Y.ZHANG,
JRNL AUTH 2 G.A.MEINTS,Y.G.GAO,D.MUKKAMALA,M.P.HUDOCK,E.OLDFIELD
JRNL TITL SOLID-STATE NMR, CRYSTALLOGRAPHIC, AND COMPUTATIONAL
JRNL TITL 2 INVESTIGATION OF BISPHOSPHONATES AND FARNESYL DIPHOSPHATE
JRNL TITL 3 SYNTHASE-BISPHOSPHONATE COMPLEXES.
JRNL REF J.AM.CHEM.SOC. V. 128 14485 2006
JRNL REFN ISSN 0002-7863
JRNL PMID 17090032
JRNL DOI 10.1021/JA061737C
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.217
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.217
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 0.021
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 770
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 39273
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5832
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 358
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 6234.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 19711
REMARK 3 NUMBER OF RESTRAINTS : 24302
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.019
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.020
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.027
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.030
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.035
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.049
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 4
REMARK 4 2I19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000039010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-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 : NSLS
REMARK 200 BEAMLINE : X12C
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 : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39495
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 91.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 0.1010
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1YHK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPD, 0.1 AMMONIUM ACETATE, PH
REMARK 280 5.75, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 66.60700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.77550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.60700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 59.77550
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: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 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 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 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 OE2 GLU A 297 O HOH A 5317 2.07
REMARK 500 O GLU A 22 O HOH A 5330 2.10
REMARK 500 OE2 GLU B 339 O HOH B 5296 2.12
REMARK 500 OE1 GLN B 155 O HOH B 5300 2.12
REMARK 500 O HOH A 5056 O HOH A 5335 2.14
REMARK 500 OE2 GLU A 335 O HOH A 5356 2.15
REMARK 500 OE2 GLU A 59 O HOH A 5299 2.15
REMARK 500 O GLU B 22 O HOH B 5292 2.16
REMARK 500 OH TYR A 302 O HOH A 5358 2.18
REMARK 500 OD2 ASP A 150 O HOH A 5301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU B 59 O HOH A 5290 4546 2.06
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 SER A 63 -89.31 -74.57
REMARK 500 GLU A 71 156.81 -21.15
REMARK 500 GLU A 72 90.07 -63.28
REMARK 500 ASP A 73 72.76 25.94
REMARK 500 ALA A 76 -37.16 -175.57
REMARK 500 SER A 182 -38.10 -36.80
REMARK 500 LYS A 184 47.58 -86.76
REMARK 500 ILE A 208 36.64 -79.47
REMARK 500 VAL A 209 -44.22 -154.27
REMARK 500 LYS A 269 175.42 174.54
REMARK 500 ASP A 273 -63.58 -23.33
REMARK 500 ASN A 301 -66.42 -128.40
REMARK 500 TYR A 302 137.78 -30.70
REMARK 500 ASP A 306 164.25 177.22
REMARK 500 CYS A 347 -38.34 -138.70
REMARK 500 SER A 348 70.20 -119.21
REMARK 500 SER B 63 6.68 158.35
REMARK 500 ASP B 73 -156.91 156.22
REMARK 500 ASP B 74 -87.96 -137.59
REMARK 500 PRO B 187 -3.14 -54.28
REMARK 500 THR B 213 -56.40 -127.21
REMARK 500 ASP B 236 99.89 -62.96
REMARK 500 LYS B 269 108.42 163.32
REMARK 500 VAL B 270 107.61 -51.25
REMARK 500 SER B 307 -77.04 -86.45
REMARK 500 SER B 348 78.87 -108.63
REMARK 500 LYS B 364 -78.72 -64.61
REMARK 500 ARG B 365 82.98 54.04
REMARK 500 GLN B 366 -79.62 -124.47
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 MG A3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 103 OD1
REMARK 620 2 ASP A 107 OD2 88.8
REMARK 620 3 1BY A3001 O4 91.7 80.8
REMARK 620 4 1BY A3001 O2 93.4 177.5 97.9
REMARK 620 5 HOH A5286 O 73.3 91.4 163.3 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 103 OD2
REMARK 620 2 ASP A 107 OD1 92.6
REMARK 620 3 ASP A 107 OD2 89.4 53.3
REMARK 620 4 1BY A3001 O4 90.2 135.5 82.4
REMARK 620 5 HOH A5036 O 80.3 147.2 156.7 76.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255 OD2
REMARK 620 2 1BY A3001 O6 124.6
REMARK 620 3 1BY A3001 O3 99.0 76.2
REMARK 620 4 HOH A5204 O 174.0 60.9 84.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B4002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 103 OD1
REMARK 620 2 ASP B 107 OD2 73.1
REMARK 620 3 1BY B4001 O2 111.3 168.7
REMARK 620 4 1BY B4001 O4 79.2 76.6 114.1
REMARK 620 5 HOH B5284 O 89.5 82.7 86.9 158.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B4004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 103 OD1
REMARK 620 2 ASP B 103 OD2 44.5
REMARK 620 3 ASP B 107 OD1 85.1 78.8
REMARK 620 4 ASP B 107 OD2 53.0 80.0 47.4
REMARK 620 5 1BY B4001 O4 57.9 96.1 124.1 76.8
REMARK 620 6 HOH B5031 O 98.4 94.6 166.5 143.5 67.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B4003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 1BY B4001 O6
REMARK 620 2 1BY B4001 O3 62.4
REMARK 620 3 HOH B5060 O 136.8 83.6
REMARK 620 4 HOH B5203 O 55.5 64.3 86.9
REMARK 620 N 1 2 3
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 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1BY A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1BY B 4001
DBREF 2I19 A 1 367 UNP Q86C09 Q86C09_9TRYP 1 367
DBREF 2I19 B 1 367 UNP Q86C09 Q86C09_9TRYP 1 367
SEQADV 2I19 MET A -22 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY A -21 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER A -20 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER A -19 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 HIS A -18 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS A -17 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS A -16 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS A -15 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS A -14 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS A -13 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 SER A -12 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER A -11 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY A -10 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 LEU A -9 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 VAL A -8 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 PRO A -7 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 ARG A -6 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY A -5 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER A -4 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 HIS A -3 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 MET A -2 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 ALA A -1 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER A 0 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 MET B -22 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY B -21 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER B -20 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER B -19 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 HIS B -18 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS B -17 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS B -16 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS B -15 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS B -14 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 HIS B -13 UNP Q86C09 EXPRESSION TAG
SEQADV 2I19 SER B -12 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER B -11 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY B -10 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 LEU B -9 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 VAL B -8 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 PRO B -7 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 ARG B -6 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 GLY B -5 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER B -4 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 HIS B -3 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 MET B -2 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 ALA B -1 UNP Q86C09 CLONING ARTIFACT
SEQADV 2I19 SER B 0 UNP Q86C09 CLONING ARTIFACT
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 1BY A3001 17
HET MG B4002 1
HET MG B4003 1
HET MG B4004 1
HET 1BY B4001 17
HETNAM MG MAGNESIUM ION
HETNAM 1BY [2-(PYRIDIN-2-YLAMINO)ETHANE-1,1-DIYL]BIS(PHOSPHONIC
HETNAM 2 1BY ACID)
FORMUL 3 MG 6(MG 2+)
FORMUL 6 1BY 2(C7 H12 N2 O6 P2)
FORMUL 11 HOH *358(H2 O)
HELIX 1 1 MET A 1 PHE A 25 1 25
HELIX 2 2 ASP A 28 LEU A 44 1 17
HELIX 3 3 TYR A 48 LEU A 64 1 17
HELIX 4 4 ALA A 76 ASN A 108 1 33
HELIX 5 5 CYS A 117 HIS A 121 5 5
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 TYR A 211 1 11
HELIX 10 10 THR A 213 TYR A 218 1 6
HELIX 11 11 TYR A 218 GLU A 230 1 13
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 SER A 280 ALA A 290 1 11
HELIX 15 15 SER A 291 TYR A 302 1 12
HELIX 16 16 GLU A 308 ALA A 320 1 13
HELIX 17 17 ASP A 321 LEU A 346 1 26
HELIX 18 18 SER A 348 LYS A 364 1 17
HELIX 19 19 MET B 1 LYS B 24 1 24
HELIX 20 20 ASP B 28 LEU B 44 1 17
HELIX 21 21 TYR B 48 LEU B 62 1 15
HELIX 22 22 GLY B 75 ASN B 108 1 34
HELIX 23 23 TRP B 118 HIS B 121 5 4
HELIX 24 24 THR B 125 ALA B 149 1 25
HELIX 25 25 PHE B 153 THR B 177 1 25
HELIX 26 26 ASP B 181 LEU B 185 5 5
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 SER B 229 GLU B 230 5 2
HELIX 31 31 ALA B 231 VAL B 235 5 5
HELIX 32 32 ASP B 236 THR B 262 1 27
HELIX 33 33 PRO B 263 GLY B 268 1 6
HELIX 34 34 SER B 280 ALA B 290 1 11
HELIX 35 35 SER B 291 TYR B 302 1 12
HELIX 36 36 SER B 307 ALA B 320 1 14
HELIX 37 37 ASP B 321 SER B 348 1 28
HELIX 38 38 SER B 348 LYS B 364 1 17
SHEET 1 A 2 THR B 111 ARG B 112 0
SHEET 2 A 2 LYS B 115 PRO B 116 -1 O LYS B 115 N ARG B 112
LINK OD1 ASP A 103 MG MG A3002 1555 1555 2.41
LINK OD2 ASP A 103 MG MG A3003 1555 1555 2.22
LINK OD2 ASP A 107 MG MG A3002 1555 1555 2.27
LINK OD1 ASP A 107 MG MG A3003 1555 1555 2.71
LINK OD2 ASP A 107 MG MG A3003 1555 1555 2.00
LINK OD2 ASP A 255 MG MG A3004 1555 1555 2.99
LINK O4 1BY A3001 MG MG A3002 1555 1555 2.05
LINK O2 1BY A3001 MG MG A3002 1555 1555 2.06
LINK O4 1BY A3001 MG MG A3003 1555 1555 2.25
LINK O6 1BY A3001 MG MG A3004 1555 1555 2.48
LINK O3 1BY A3001 MG MG A3004 1555 1555 2.42
LINK MG MG A3002 O HOH A5286 1555 1555 1.91
LINK MG MG A3003 O HOH A5036 1555 1555 2.40
LINK MG MG A3004 O HOH A5204 1555 1555 2.94
LINK OD1 ASP B 103 MG MG B4002 1555 1555 1.96
LINK OD1 ASP B 103 MG MG B4004 1555 1555 3.14
LINK OD2 ASP B 103 MG MG B4004 1555 1555 2.16
LINK OD2 ASP B 107 MG MG B4002 1555 1555 2.30
LINK OD1 ASP B 107 MG MG B4004 1555 1555 2.93
LINK OD2 ASP B 107 MG MG B4004 1555 1555 2.39
LINK O2 1BY B4001 MG MG B4002 1555 1555 1.97
LINK O4 1BY B4001 MG MG B4002 1555 1555 2.26
LINK O6 1BY B4001 MG MG B4003 1555 1555 3.03
LINK O3 1BY B4001 MG MG B4003 1555 1555 2.88
LINK O4 1BY B4001 MG MG B4004 1555 1555 2.16
LINK MG MG B4002 O HOH B5284 1555 1555 2.08
LINK MG MG B4003 O HOH B5060 1555 1555 2.72
LINK MG MG B4003 O HOH B5203 1555 1555 2.27
LINK MG MG B4004 O HOH B5031 1555 1555 2.29
SITE 1 AC1 5 ASP A 103 ASP A 107 1BY A3001 MG A3003
SITE 2 AC1 5 HOH A5286
SITE 1 AC2 5 ASP A 103 ASP A 107 1BY A3001 MG A3002
SITE 2 AC2 5 HOH A5036
SITE 1 AC3 4 ASP A 255 ASP A 259 1BY A3001 HOH A5204
SITE 1 AC4 5 ASP B 103 ASP B 107 1BY B4001 MG B4004
SITE 2 AC4 5 HOH B5284
SITE 1 AC5 4 ASP B 255 1BY B4001 HOH B5060 HOH B5203
SITE 1 AC6 6 ASP B 103 ASP B 107 ASP B 175 1BY B4001
SITE 2 AC6 6 MG B4002 HOH B5031
SITE 1 AC7 15 TYR A 99 LEU A 100 ASP A 103 ASP A 107
SITE 2 AC7 15 ARG A 112 THR A 168 GLN A 172 LYS A 212
SITE 3 AC7 15 LYS A 269 MG A3002 MG A3003 MG A3004
SITE 4 AC7 15 HOH A5036 HOH A5204 HOH A5286
SITE 1 AC8 17 TYR B 99 ASP B 103 ASP B 107 ARG B 112
SITE 2 AC8 17 THR B 168 GLN B 172 LYS B 212 MG B4002
SITE 3 AC8 17 MG B4003 MG B4004 HOH B5031 HOH B5065
SITE 4 AC8 17 HOH B5113 HOH B5166 HOH B5203 HOH B5277
SITE 5 AC8 17 HOH B5284
CRYST1 133.214 119.551 62.438 90.00 111.93 90.00 C 1 2 1 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 0.007507 0.000000 0.003022 0.00000
SCALE2 0.000000 0.008365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017265 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
