HEADER TRANSFERASE 10-FEB-03 1NXE
TITLE A NOVEL NADH ALLOSTERIC REGULATOR SITE IS FOUND ON THE SURFACE OF THE
TITLE 2 HEXAMERIC TYPE II PHE383ALA VARIANT OF CITRATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CITRATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.3.3.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GLTA OR GLUT OR ICDB OR B0720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CITRATE SYNTHASE, NADH, ALLOSTERIC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MAURUS,N.T.NGUYEN,D.J.STOKELL,A.AYED,P.G.HULTIN,H.W.DUCKWORTH,
AUTHOR 2 G.D.BRAYER
REVDAT 6 16-AUG-23 1NXE 1 REMARK
REVDAT 5 27-OCT-21 1NXE 1 REMARK SEQADV
REVDAT 4 26-MAY-10 1NXE 1 COMPND HEADER KEYWDS
REVDAT 3 24-FEB-09 1NXE 1 VERSN
REVDAT 2 04-NOV-03 1NXE 1 JRNL
REVDAT 1 08-APR-03 1NXE 0
JRNL AUTH R.MAURUS,N.T.NGUYEN,D.J.STOKELL,A.AYED,P.G.HULTIN,
JRNL AUTH 2 H.W.DUCKWORTH,G.D.BRAYER
JRNL TITL INSIGHTS INTO THE EVOLUTION OF ALLOSTERIC PROPERTIES. THE
JRNL TITL 2 NADH BINDING SITE OF HEXAMERIC TYPE II CITRATE SYNTHASES.
JRNL REF BIOCHEMISTRY V. 42 5555 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12741811
JRNL DOI 10.1021/BI020622S
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 77.0
REMARK 3 NUMBER OF REFLECTIONS : 53934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6719
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 726
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1NXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018314.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54292
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1K3P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 82.62150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.70155
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.51900
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 82.62150
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 47.70155
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.51900
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 82.62150
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 47.70155
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.51900
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 95.40309
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 105.03800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 95.40309
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 105.03800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 95.40309
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 105.03800
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: HEXAMERIC
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 165.24300
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 82.62150
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 143.10464
REMARK 350 BIOMT3 3 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 0
REMARK 465 MET B 1000
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 O HOH A 2007 O HOH B 251 2.12
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 LYS A 4 27.63 -67.50
REMARK 500 ASP A 12 -12.49 -146.09
REMARK 500 LYS A 37 30.01 -70.43
REMARK 500 ASP A 60 84.11 -153.96
REMARK 500 TYR A 145 65.45 -104.40
REMARK 500 SER A 148 51.95 -107.36
REMARK 500 HIS A 229 54.88 -148.47
REMARK 500 GLU A 230 -145.41 57.40
REMARK 500 ASN A 232 -174.68 -67.79
REMARK 500 ALA A 246 135.84 -23.00
REMARK 500 ALA A 267 155.99 155.19
REMARK 500 ASN A 268 -6.70 -59.23
REMARK 500 GLU A 269 37.19 -153.74
REMARK 500 ALA A 270 -71.08 -57.74
REMARK 500 GLU A 277 30.32 -96.65
REMARK 500 PRO A 285 29.04 -56.71
REMARK 500 GLU A 286 -62.18 -168.02
REMARK 500 PHE A 287 3.98 -67.42
REMARK 500 ARG A 289 -95.75 -106.95
REMARK 500 ARG A 290 46.32 -69.52
REMARK 500 ALA A 291 -3.19 -161.74
REMARK 500 LYS A 292 -10.70 -141.14
REMARK 500 ASP A 293 -73.97 -58.02
REMARK 500 LYS A 294 93.83 -47.50
REMARK 500 SER A 297 155.98 -31.70
REMARK 500 THR A 331 50.05 -66.63
REMARK 500 LYS A 332 -8.01 -150.23
REMARK 500 LEU A 357 45.91 -94.16
REMARK 500 TYR A 415 159.41 -49.57
REMARK 500 SER A 422 121.17 -33.60
REMARK 500 ASP B1002 -95.10 -106.52
REMARK 500 LYS B1004 1.95 -60.43
REMARK 500 ALA B1005 -74.42 -86.89
REMARK 500 ASP B1012 10.41 -163.61
REMARK 500 SER B1036 41.62 -79.72
REMARK 500 LYS B1037 2.05 -159.58
REMARK 500 ASP B1043 73.45 -153.04
REMARK 500 SER B1080 -154.33 -111.26
REMARK 500 PHE B1144 -81.64 -107.50
REMARK 500 TYR B1145 68.24 -62.76
REMARK 500 SER B1148 44.81 -157.68
REMARK 500 HIS B1229 50.21 -158.78
REMARK 500 GLU B1230 -150.11 56.99
REMARK 500 ALA B1267 155.66 154.97
REMARK 500 ASN B1268 -9.39 -47.30
REMARK 500 GLU B1269 35.70 -158.77
REMARK 500 GLU B1277 30.31 -90.01
REMARK 500 PRO B1285 29.62 -55.96
REMARK 500 GLU B1286 -62.31 -166.49
REMARK 500 PHE B1287 3.91 -68.00
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 SO4 B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K3P RELATED DB: PDB
DBREF 1NXE A 0 426 UNP P0ABH7 CISY_ECOLI 1 427
DBREF 1NXE B 1000 1426 UNP P0ABH7 CISY_ECOLI 1 427
SEQADV 1NXE ALA A 383 UNP P0ABH7 PHE 384 ENGINEERED MUTATION
SEQADV 1NXE ALA B 1383 UNP P0ABH7 PHE 384 ENGINEERED MUTATION
SEQRES 1 A 427 MET ALA ASP THR LYS ALA LYS LEU THR LEU ASN GLY ASP
SEQRES 2 A 427 THR ALA VAL GLU LEU ASP VAL LEU LYS GLY THR LEU GLY
SEQRES 3 A 427 GLN ASP VAL ILE ASP ILE ARG THR LEU GLY SER LYS GLY
SEQRES 4 A 427 VAL PHE THR PHE ASP PRO GLY PHE THR SER THR ALA SER
SEQRES 5 A 427 CYS GLU SER LYS ILE THR PHE ILE ASP GLY ASP GLU GLY
SEQRES 6 A 427 ILE LEU LEU HIS ARG GLY PHE PRO ILE ASP GLN LEU ALA
SEQRES 7 A 427 THR ASP SER ASN TYR LEU GLU VAL CYS TYR ILE LEU LEU
SEQRES 8 A 427 ASN GLY GLU LYS PRO THR GLN GLU GLN TYR ASP GLU PHE
SEQRES 9 A 427 LYS THR THR VAL THR ARG HIS THR MET ILE HIS GLU GLN
SEQRES 10 A 427 ILE THR ARG LEU PHE HIS ALA PHE ARG ARG ASP SER HIS
SEQRES 11 A 427 PRO MET ALA VAL MET CYS GLY ILE THR GLY ALA LEU ALA
SEQRES 12 A 427 ALA PHE TYR HIS ASP SER LEU ASP VAL ASN ASN PRO ARG
SEQRES 13 A 427 HIS ARG GLU ILE ALA ALA PHE ARG LEU LEU SER LYS MET
SEQRES 14 A 427 PRO THR MET ALA ALA MET CYS TYR LYS TYR SER ILE GLY
SEQRES 15 A 427 GLN PRO PHE VAL TYR PRO ARG ASN ASP LEU SER TYR ALA
SEQRES 16 A 427 GLY ASN PHE LEU ASN MET MET PHE SER THR PRO CYS GLU
SEQRES 17 A 427 PRO TYR GLU VAL ASN PRO ILE LEU GLU ARG ALA MET ASP
SEQRES 18 A 427 ARG ILE LEU ILE LEU HIS ALA ASP HIS GLU GLN ASN ALA
SEQRES 19 A 427 SER THR SER THR VAL ARG THR ALA GLY SER SER GLY ALA
SEQRES 20 A 427 ASN PRO PHE ALA CYS ILE ALA ALA GLY ILE ALA SER LEU
SEQRES 21 A 427 TRP GLY PRO ALA HIS GLY GLY ALA ASN GLU ALA ALA LEU
SEQRES 22 A 427 LYS MET LEU GLU GLU ILE SER SER VAL LYS HIS ILE PRO
SEQRES 23 A 427 GLU PHE PHE ARG ARG ALA LYS ASP LYS ASN ASP SER PHE
SEQRES 24 A 427 ARG LEU MET GLY PHE GLY HIS ARG VAL TYR LYS ASN TYR
SEQRES 25 A 427 ASP PRO ARG ALA THR VAL MET ARG GLU THR CYS HIS GLU
SEQRES 26 A 427 VAL LEU LYS GLU LEU GLY THR LYS ASP ASP LEU LEU GLU
SEQRES 27 A 427 VAL ALA MET GLU LEU GLU ASN ILE ALA LEU ASN ASP PRO
SEQRES 28 A 427 TYR PHE ILE GLU LYS LYS LEU TYR PRO ASN VAL ASP PHE
SEQRES 29 A 427 TYR SER GLY ILE ILE LEU LYS ALA MET GLY ILE PRO SER
SEQRES 30 A 427 SER MET PHE THR VAL ILE ALA ALA MET ALA ARG THR VAL
SEQRES 31 A 427 GLY TRP ILE ALA HIS TRP SER GLU MET HIS SER ASP GLY
SEQRES 32 A 427 MET LYS ILE ALA ARG PRO ARG GLN LEU TYR THR GLY TYR
SEQRES 33 A 427 GLU LYS ARG ASP PHE LYS SER ASP ILE LYS ARG
SEQRES 1 B 427 MET ALA ASP THR LYS ALA LYS LEU THR LEU ASN GLY ASP
SEQRES 2 B 427 THR ALA VAL GLU LEU ASP VAL LEU LYS GLY THR LEU GLY
SEQRES 3 B 427 GLN ASP VAL ILE ASP ILE ARG THR LEU GLY SER LYS GLY
SEQRES 4 B 427 VAL PHE THR PHE ASP PRO GLY PHE THR SER THR ALA SER
SEQRES 5 B 427 CYS GLU SER LYS ILE THR PHE ILE ASP GLY ASP GLU GLY
SEQRES 6 B 427 ILE LEU LEU HIS ARG GLY PHE PRO ILE ASP GLN LEU ALA
SEQRES 7 B 427 THR ASP SER ASN TYR LEU GLU VAL CYS TYR ILE LEU LEU
SEQRES 8 B 427 ASN GLY GLU LYS PRO THR GLN GLU GLN TYR ASP GLU PHE
SEQRES 9 B 427 LYS THR THR VAL THR ARG HIS THR MET ILE HIS GLU GLN
SEQRES 10 B 427 ILE THR ARG LEU PHE HIS ALA PHE ARG ARG ASP SER HIS
SEQRES 11 B 427 PRO MET ALA VAL MET CYS GLY ILE THR GLY ALA LEU ALA
SEQRES 12 B 427 ALA PHE TYR HIS ASP SER LEU ASP VAL ASN ASN PRO ARG
SEQRES 13 B 427 HIS ARG GLU ILE ALA ALA PHE ARG LEU LEU SER LYS MET
SEQRES 14 B 427 PRO THR MET ALA ALA MET CYS TYR LYS TYR SER ILE GLY
SEQRES 15 B 427 GLN PRO PHE VAL TYR PRO ARG ASN ASP LEU SER TYR ALA
SEQRES 16 B 427 GLY ASN PHE LEU ASN MET MET PHE SER THR PRO CYS GLU
SEQRES 17 B 427 PRO TYR GLU VAL ASN PRO ILE LEU GLU ARG ALA MET ASP
SEQRES 18 B 427 ARG ILE LEU ILE LEU HIS ALA ASP HIS GLU GLN ASN ALA
SEQRES 19 B 427 SER THR SER THR VAL ARG THR ALA GLY SER SER GLY ALA
SEQRES 20 B 427 ASN PRO PHE ALA CYS ILE ALA ALA GLY ILE ALA SER LEU
SEQRES 21 B 427 TRP GLY PRO ALA HIS GLY GLY ALA ASN GLU ALA ALA LEU
SEQRES 22 B 427 LYS MET LEU GLU GLU ILE SER SER VAL LYS HIS ILE PRO
SEQRES 23 B 427 GLU PHE PHE ARG ARG ALA LYS ASP LYS ASN ASP SER PHE
SEQRES 24 B 427 ARG LEU MET GLY PHE GLY HIS ARG VAL TYR LYS ASN TYR
SEQRES 25 B 427 ASP PRO ARG ALA THR VAL MET ARG GLU THR CYS HIS GLU
SEQRES 26 B 427 VAL LEU LYS GLU LEU GLY THR LYS ASP ASP LEU LEU GLU
SEQRES 27 B 427 VAL ALA MET GLU LEU GLU ASN ILE ALA LEU ASN ASP PRO
SEQRES 28 B 427 TYR PHE ILE GLU LYS LYS LEU TYR PRO ASN VAL ASP PHE
SEQRES 29 B 427 TYR SER GLY ILE ILE LEU LYS ALA MET GLY ILE PRO SER
SEQRES 30 B 427 SER MET PHE THR VAL ILE ALA ALA MET ALA ARG THR VAL
SEQRES 31 B 427 GLY TRP ILE ALA HIS TRP SER GLU MET HIS SER ASP GLY
SEQRES 32 B 427 MET LYS ILE ALA ARG PRO ARG GLN LEU TYR THR GLY TYR
SEQRES 33 B 427 GLU LYS ARG ASP PHE LYS SER ASP ILE LYS ARG
HET SO4 A2004 5
HET SO4 A2005 5
HET SO4 A2006 5
HET SO4 B2001 5
HET SO4 B2002 5
HET SO4 B2003 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 HOH *726(H2 O)
HELIX 1 1 ILE A 73 SER A 80 1 8
HELIX 2 2 ASN A 81 GLY A 92 1 12
HELIX 3 3 THR A 96 ARG A 109 1 14
HELIX 4 4 GLN A 116 PHE A 124 5 9
HELIX 5 5 HIS A 129 GLY A 139 1 11
HELIX 6 6 ALA A 140 TYR A 145 1 6
HELIX 7 7 ASN A 153 GLY A 181 1 29
HELIX 8 8 SER A 192 SER A 203 1 12
HELIX 9 9 ASN A 212 LEU A 225 1 14
HELIX 10 10 ASN A 232 SER A 244 1 13
HELIX 11 11 ASN A 247 TRP A 260 1 14
HELIX 12 12 TRP A 260 GLY A 265 1 6
HELIX 13 13 LEU A 272 GLU A 276 5 5
HELIX 14 14 ARG A 314 LYS A 327 1 14
HELIX 15 15 GLU A 337 ASP A 349 1 13
HELIX 16 16 ASP A 349 LYS A 356 1 8
HELIX 17 17 ASN A 360 MET A 372 1 13
HELIX 18 18 MET A 378 GLY A 402 1 25
HELIX 19 19 THR B 1033 GLY B 1038 5 6
HELIX 20 20 GLY B 1061 GLY B 1064 5 4
HELIX 21 21 ILE B 1073 SER B 1080 1 8
HELIX 22 22 ASN B 1081 GLY B 1092 1 12
HELIX 23 23 THR B 1096 ARG B 1109 1 14
HELIX 24 24 HIS B 1114 ALA B 1123 1 10
HELIX 25 25 HIS B 1129 ALA B 1140 1 12
HELIX 26 26 LEU B 1141 PHE B 1144 5 4
HELIX 27 27 ASN B 1153 GLY B 1181 1 29
HELIX 28 28 SER B 1192 SER B 1203 1 12
HELIX 29 29 ASN B 1212 LEU B 1225 1 14
HELIX 30 30 ASN B 1232 SER B 1244 1 13
HELIX 31 31 ASN B 1247 TRP B 1260 1 14
HELIX 32 32 TRP B 1260 GLY B 1265 1 6
HELIX 33 33 LEU B 1272 GLU B 1276 5 5
HELIX 34 34 ARG B 1314 GLY B 1330 1 17
HELIX 35 35 GLU B 1337 ASP B 1349 1 13
HELIX 36 36 ASP B 1349 LYS B 1355 1 7
HELIX 37 37 ASN B 1360 GLY B 1373 1 14
HELIX 38 38 PRO B 1375 SER B 1377 5 3
HELIX 39 39 MET B 1378 HIS B 1399 1 22
SHEET 1 A 8 GLU B1016 LEU B1017 0
SHEET 2 A 8 LEU B1007 ASN B1010 -1 N LEU B1007 O LEU B1017
SHEET 3 A 8 LYS A 6 ASN A 10 -1 N THR A 8 O ASN B1010
SHEET 4 A 8 ALA A 14 LEU A 20 -1 O LEU A 17 N LEU A 7
SHEET 5 A 8 VAL A 28 ASP A 30 -1 O VAL A 28 N LEU A 20
SHEET 6 A 8 THR B1041 PHE B1042 1 O PHE B1042 N ILE A 29
SHEET 7 A 8 THR A 49 SER A 54 1 N ALA A 50 O THR B1041
SHEET 8 A 8 ARG B1409 TYR B1412 1 O LEU B1411 N SER A 54
SHEET 1 B 5 ARG A 409 TYR A 412 0
SHEET 2 B 5 THR B1049 SER B1054 1 O THR B1049 N ARG A 409
SHEET 3 B 5 THR A 41 PHE A 42 1 N THR A 41 O ALA B1050
SHEET 4 B 5 VAL B1028 ASP B1030 1 O ILE B1029 N PHE A 42
SHEET 5 B 5 VAL B1019 LEU B1020 -1 N LEU B1020 O VAL B1028
SHEET 1 C 3 THR A 57 ASP A 60 0
SHEET 2 C 3 ILE A 65 HIS A 68 -1 O ILE A 65 N ASP A 60
SHEET 3 C 3 PHE A 71 PRO A 72 -1 O PHE A 71 N HIS A 68
SHEET 1 D 3 THR B1057 ASP B1060 0
SHEET 2 D 3 ILE B1065 HIS B1068 -1 O LEU B1067 N PHE B1058
SHEET 3 D 3 PHE B1071 PRO B1072 -1 O PHE B1071 N HIS B1068
SITE 1 AC1 6 ARG A 407 HOH B 53 ASN B1232 ALA B1233
SITE 2 AC1 6 ARG B1299 ARG B1306
SITE 1 AC2 6 HOH B 446 HOH B 648 HIS B1110 TYR B1145
SITE 2 AC2 6 ARG B1163 LYS B1167
SITE 1 AC3 8 HOH B 53 HOH B 63 HOH B 194 HIS B1229
SITE 2 AC3 8 ASN B1232 HIS B1305 ARG B1314 ARG B1387
SITE 1 AC4 7 ASN A 232 ALA A 233 ARG A 299 ARG A 306
SITE 2 AC4 7 HOH A2031 HOH A2098 ARG B1407
SITE 1 AC5 4 HIS A 110 TYR A 145 ARG A 163 LYS A 167
SITE 1 AC6 9 HIS A 229 ASN A 232 ARG A 299 HIS A 305
SITE 2 AC6 9 ARG A 314 ARG A 387 HOH A2031 HOH A2321
SITE 3 AC6 9 HOH A2355
CRYST1 165.243 165.243 157.557 90.00 90.00 120.00 H 3 18
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 0.006052 0.003494 0.000000 0.00000
SCALE2 0.000000 0.006988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006347 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
