HEADER LYASE 06-OCT-98 1BXN
TITLE THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7
TITLE 2 ANGSTROMS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN);
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: RUBISCO;
COMPND 5 EC: 4.1.1.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN);
COMPND 9 CHAIN: I, J, K, L;
COMPND 10 SYNONYM: RUBISCO;
COMPND 11 EC: 4.1.1.39;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE 3 ORGANISM_TAXID: 106590;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE 6 ORGANISM_TAXID: 106590
KEYWDS LYASE (CARBON-CARBON), LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HANSEN,V.B.VOLLAN,E.HOUGH,K.ANDERSEN
REVDAT 7 09-AUG-23 1BXN 1 REMARK
REVDAT 6 04-OCT-17 1BXN 1 REMARK
REVDAT 5 13-JUL-11 1BXN 1 VERSN
REVDAT 4 24-FEB-09 1BXN 1 VERSN
REVDAT 3 05-JUN-00 1BXN 1 COMPND REMARK DBREF SEQADV
REVDAT 3 2 1 SEQRES HELIX
REVDAT 2 07-OCT-99 1BXN 3
REVDAT 1 06-OCT-99 1BXN 0
JRNL AUTH S.HANSEN,V.B.VOLLAN,E.HOUGH,K.ANDERSEN
JRNL TITL THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS
JRNL TITL 2 REVEALS A NOVEL CENTRAL EIGHT-STRANDED BETA-BARREL FORMED BY
JRNL TITL 3 BETA-STRANDS FROM FOUR SUBUNITS.
JRNL REF J.MOL.BIOL. V. 288 609 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10329167
JRNL DOI 10.1006/JMBI.1999.2701
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.HANSEN,E.HOUGH,K.ANDERSEN
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES
REMARK 1 TITL 2 OF TWO ISOFORMS OF RUBISCO FROM ALCALIGENES EUTROPHUS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 310 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 65785
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 : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 18104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 0
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.76
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.110
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 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 1BXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9117
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT SYNCHROTRON
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65785
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.5000
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: AMORE
REMARK 200 STARTING MODEL: 1AUS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.40
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 201.35000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 56.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 56.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 302.02500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 56.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 56.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 100.67500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 56.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 302.02500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 56.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 100.67500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 201.35000
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 95060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -442.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, C, J, E, K, G, L
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 0.000000 -1.000000 0.000000 112.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 112.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 201.35000
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 ASN A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 VAL A 7
REMARK 465 GLN A 8
REMARK 465 ALA A 9
REMARK 465 LYS A 10
REMARK 465 PRO A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 ARG A 14
REMARK 465 TYR A 15
REMARK 465 ASP A 16
REMARK 465 ALA A 17
REMARK 465 GLY A 18
REMARK 465 VAL A 19
REMARK 465 MET A 20
REMARK 465 LYS A 21
REMARK 465 SER A 468
REMARK 465 PHE A 469
REMARK 465 ASN A 470
REMARK 465 TYR A 471
REMARK 465 THR A 472
REMARK 465 PRO A 473
REMARK 465 THR A 474
REMARK 465 ASP A 475
REMARK 465 THR A 476
REMARK 465 SER A 477
REMARK 465 ASP A 478
REMARK 465 PHE A 479
REMARK 465 ALA A 480
REMARK 465 PRO A 481
REMARK 465 THR A 482
REMARK 465 ALA A 483
REMARK 465 SER A 484
REMARK 465 VAL A 485
REMARK 465 ALA A 486
REMARK 465 VAL I 130
REMARK 465 GLN I 131
REMARK 465 ALA I 132
REMARK 465 GLY I 133
REMARK 465 PRO I 134
REMARK 465 GLU I 135
REMARK 465 GLY I 136
REMARK 465 SER I 137
REMARK 465 ARG I 138
REMARK 465 TYR I 139
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 ALA C 3
REMARK 465 PRO C 4
REMARK 465 GLU C 5
REMARK 465 SER C 6
REMARK 465 VAL C 7
REMARK 465 GLN C 8
REMARK 465 ALA C 9
REMARK 465 LYS C 10
REMARK 465 PRO C 11
REMARK 465 ARG C 12
REMARK 465 LYS C 13
REMARK 465 ARG C 14
REMARK 465 TYR C 15
REMARK 465 ASP C 16
REMARK 465 ALA C 17
REMARK 465 GLY C 18
REMARK 465 VAL C 19
REMARK 465 MET C 20
REMARK 465 LYS C 21
REMARK 465 SER C 468
REMARK 465 PHE C 469
REMARK 465 ASN C 470
REMARK 465 TYR C 471
REMARK 465 THR C 472
REMARK 465 PRO C 473
REMARK 465 THR C 474
REMARK 465 ASP C 475
REMARK 465 THR C 476
REMARK 465 SER C 477
REMARK 465 ASP C 478
REMARK 465 PHE C 479
REMARK 465 ALA C 480
REMARK 465 PRO C 481
REMARK 465 THR C 482
REMARK 465 ALA C 483
REMARK 465 SER C 484
REMARK 465 VAL C 485
REMARK 465 ALA C 486
REMARK 465 VAL J 130
REMARK 465 GLN J 131
REMARK 465 ALA J 132
REMARK 465 GLY J 133
REMARK 465 PRO J 134
REMARK 465 GLU J 135
REMARK 465 GLY J 136
REMARK 465 SER J 137
REMARK 465 ARG J 138
REMARK 465 TYR J 139
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 PRO E 4
REMARK 465 GLU E 5
REMARK 465 SER E 6
REMARK 465 VAL E 7
REMARK 465 GLN E 8
REMARK 465 ALA E 9
REMARK 465 LYS E 10
REMARK 465 PRO E 11
REMARK 465 ARG E 12
REMARK 465 LYS E 13
REMARK 465 ARG E 14
REMARK 465 TYR E 15
REMARK 465 ASP E 16
REMARK 465 ALA E 17
REMARK 465 GLY E 18
REMARK 465 VAL E 19
REMARK 465 MET E 20
REMARK 465 LYS E 21
REMARK 465 SER E 468
REMARK 465 PHE E 469
REMARK 465 ASN E 470
REMARK 465 TYR E 471
REMARK 465 THR E 472
REMARK 465 PRO E 473
REMARK 465 THR E 474
REMARK 465 ASP E 475
REMARK 465 THR E 476
REMARK 465 SER E 477
REMARK 465 ASP E 478
REMARK 465 PHE E 479
REMARK 465 ALA E 480
REMARK 465 PRO E 481
REMARK 465 THR E 482
REMARK 465 ALA E 483
REMARK 465 SER E 484
REMARK 465 VAL E 485
REMARK 465 ALA E 486
REMARK 465 VAL K 130
REMARK 465 GLN K 131
REMARK 465 ALA K 132
REMARK 465 GLY K 133
REMARK 465 PRO K 134
REMARK 465 GLU K 135
REMARK 465 GLY K 136
REMARK 465 SER K 137
REMARK 465 ARG K 138
REMARK 465 TYR K 139
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 ALA G 3
REMARK 465 PRO G 4
REMARK 465 GLU G 5
REMARK 465 SER G 6
REMARK 465 VAL G 7
REMARK 465 GLN G 8
REMARK 465 ALA G 9
REMARK 465 LYS G 10
REMARK 465 PRO G 11
REMARK 465 ARG G 12
REMARK 465 LYS G 13
REMARK 465 ARG G 14
REMARK 465 TYR G 15
REMARK 465 ASP G 16
REMARK 465 ALA G 17
REMARK 465 GLY G 18
REMARK 465 VAL G 19
REMARK 465 MET G 20
REMARK 465 LYS G 21
REMARK 465 SER G 468
REMARK 465 PHE G 469
REMARK 465 ASN G 470
REMARK 465 TYR G 471
REMARK 465 THR G 472
REMARK 465 PRO G 473
REMARK 465 THR G 474
REMARK 465 ASP G 475
REMARK 465 THR G 476
REMARK 465 SER G 477
REMARK 465 ASP G 478
REMARK 465 PHE G 479
REMARK 465 ALA G 480
REMARK 465 PRO G 481
REMARK 465 THR G 482
REMARK 465 ALA G 483
REMARK 465 SER G 484
REMARK 465 VAL G 485
REMARK 465 ALA G 486
REMARK 465 VAL L 130
REMARK 465 GLN L 131
REMARK 465 ALA L 132
REMARK 465 GLY L 133
REMARK 465 PRO L 134
REMARK 465 GLU L 135
REMARK 465 GLY L 136
REMARK 465 SER L 137
REMARK 465 ARG L 138
REMARK 465 TYR L 139
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 23 -48.02 72.20
REMARK 500 MET A 25 -36.04 -31.43
REMARK 500 THR A 37 50.71 -113.06
REMARK 500 ARG A 44 78.00 -119.63
REMARK 500 ASP A 49 99.57 -59.46
REMARK 500 GLU A 63 34.25 -86.23
REMARK 500 SER A 64 34.18 -163.99
REMARK 500 SER A 65 -150.09 -170.59
REMARK 500 THR A 66 33.00 -71.35
REMARK 500 ALA A 79 -34.25 73.27
REMARK 500 CYS A 80 -90.97 49.85
REMARK 500 ASP A 81 -85.22 49.53
REMARK 500 TYR A 83 40.93 -84.23
REMARK 500 TYR A 88 -91.54 -121.29
REMARK 500 ASN A 96 89.07 -160.86
REMARK 500 PRO A 97 -179.38 -69.13
REMARK 500 GLU A 98 -0.44 65.71
REMARK 500 PRO A 132 -9.23 -52.98
REMARK 500 THR A 156 -66.23 -148.76
REMARK 500 ARG A 170 140.74 -170.53
REMARK 500 LYS A 180 -151.54 56.78
REMARK 500 GLU A 207 -43.72 -15.43
REMARK 500 SER A 211 68.31 -178.35
REMARK 500 PRO A 213 72.79 -65.43
REMARK 500 PHE A 214 -48.48 -174.17
REMARK 500 TYR A 242 83.53 -68.28
REMARK 500 ARG A 297 35.98 -72.56
REMARK 500 ASN A 308 -17.34 -176.83
REMARK 500 ALA A 333 96.59 59.09
REMARK 500 VAL A 334 -41.37 67.47
REMARK 500 GLU A 338 -65.69 -154.70
REMARK 500 ALA A 371 45.75 31.75
REMARK 500 GLN A 413 31.26 -98.52
REMARK 500 ASP A 438 92.24 -64.95
REMARK 500 LEU A 440 -76.00 -56.00
REMARK 500 TRP A 464 74.61 -112.58
REMARK 500 ARG I 2 122.84 -177.60
REMARK 500 THR I 4 38.91 -96.38
REMARK 500 PHE I 8 -1.98 68.80
REMARK 500 PRO I 41 46.50 -83.01
REMARK 500 ARG I 44 48.65 75.07
REMARK 500 ASN I 45 67.25 -104.76
REMARK 500 TYR I 47 61.65 77.05
REMARK 500 PHE I 56 -87.56 -60.49
REMARK 500 ASP I 57 56.16 -93.28
REMARK 500 ASP I 60 99.12 -165.15
REMARK 500 THR I 88 -31.22 -152.77
REMARK 500 HIS I 89 -5.25 -144.14
REMARK 500 THR I 90 82.51 55.65
REMARK 500 PHE I 98 -80.66 -115.72
REMARK 500
REMARK 500 THIS ENTRY HAS 215 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 PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 508
DBREF 1BXN A 1 486 PDB 1BXN 1BXN 1 486
DBREF 1BXN I 1 139 PDB 1BXN 1BXN 1 139
DBREF 1BXN C 1 486 PDB 1BXN 1BXN 1 486
DBREF 1BXN J 1 139 PDB 1BXN 1BXN 1 139
DBREF 1BXN E 1 486 PDB 1BXN 1BXN 1 486
DBREF 1BXN K 1 139 PDB 1BXN 1BXN 1 139
DBREF 1BXN G 1 486 PDB 1BXN 1BXN 1 486
DBREF 1BXN L 1 139 PDB 1BXN 1BXN 1 139
SEQRES 1 A 485 MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES 2 A 485 ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES 3 A 485 TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES 4 A 485 ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES 5 A 485 VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES 6 A 485 ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES 7 A 485 CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES 8 A 485 VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES 9 A 485 TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES 10 A 485 LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES 11 A 485 PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES 12 A 485 VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES 13 A 485 ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES 14 A 485 PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES 15 A 485 SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES 16 A 485 LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES 17 A 485 ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES 18 A 485 PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES 19 A 485 GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES 20 A 485 THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES 21 A 485 SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES 22 A 485 GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES 23 A 485 GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES 24 A 485 GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES 25 A 485 ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES 26 A 485 HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES 27 A 485 ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES 28 A 485 ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES 29 A 485 PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES 30 A 485 VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES 31 A 485 LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES 32 A 485 GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES 33 A 485 GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES 34 A 485 LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES 35 A 485 PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES 36 A 485 LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES 37 A 485 ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES 38 A 485 ALA SER VAL ALA
SEQRES 1 I 139 MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES 2 I 139 LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES 3 I 139 LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES 4 I 139 ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES 5 I 139 LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES 6 I 139 MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES 7 I 139 TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES 8 I 139 GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES 9 I 139 ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES 10 I 139 GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES 11 I 139 GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES 1 C 485 MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES 2 C 485 ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES 3 C 485 TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES 4 C 485 ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES 5 C 485 VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES 6 C 485 ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES 7 C 485 CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES 8 C 485 VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES 9 C 485 TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES 10 C 485 LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES 11 C 485 PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES 12 C 485 VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES 13 C 485 ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES 14 C 485 PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES 15 C 485 SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES 16 C 485 LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES 17 C 485 ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES 18 C 485 PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES 19 C 485 GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES 20 C 485 THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES 21 C 485 SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES 22 C 485 GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES 23 C 485 GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES 24 C 485 GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES 25 C 485 ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES 26 C 485 HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES 27 C 485 ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES 28 C 485 ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES 29 C 485 PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES 30 C 485 VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES 31 C 485 LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES 32 C 485 GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES 33 C 485 GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES 34 C 485 LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES 35 C 485 PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES 36 C 485 LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES 37 C 485 ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES 38 C 485 ALA SER VAL ALA
SEQRES 1 J 139 MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES 2 J 139 LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES 3 J 139 LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES 4 J 139 ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES 5 J 139 LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES 6 J 139 MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES 7 J 139 TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES 8 J 139 GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES 9 J 139 ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES 10 J 139 GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES 11 J 139 GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES 1 E 485 MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES 2 E 485 ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES 3 E 485 TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES 4 E 485 ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES 5 E 485 VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES 6 E 485 ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES 7 E 485 CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES 8 E 485 VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES 9 E 485 TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES 10 E 485 LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES 11 E 485 PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES 12 E 485 VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES 13 E 485 ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES 14 E 485 PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES 15 E 485 SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES 16 E 485 LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES 17 E 485 ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES 18 E 485 PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES 19 E 485 GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES 20 E 485 THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES 21 E 485 SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES 22 E 485 GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES 23 E 485 GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES 24 E 485 GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES 25 E 485 ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES 26 E 485 HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES 27 E 485 ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES 28 E 485 ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES 29 E 485 PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES 30 E 485 VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES 31 E 485 LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES 32 E 485 GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES 33 E 485 GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES 34 E 485 LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES 35 E 485 PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES 36 E 485 LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES 37 E 485 ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES 38 E 485 ALA SER VAL ALA
SEQRES 1 K 139 MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES 2 K 139 LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES 3 K 139 LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES 4 K 139 ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES 5 K 139 LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES 6 K 139 MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES 7 K 139 TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES 8 K 139 GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES 9 K 139 ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES 10 K 139 GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES 11 K 139 GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES 1 G 485 MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES 2 G 485 ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES 3 G 485 TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES 4 G 485 ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES 5 G 485 VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES 6 G 485 ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES 7 G 485 CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES 8 G 485 VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES 9 G 485 TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES 10 G 485 LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES 11 G 485 PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES 12 G 485 VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES 13 G 485 ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES 14 G 485 PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES 15 G 485 SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES 16 G 485 LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES 17 G 485 ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES 18 G 485 PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES 19 G 485 GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES 20 G 485 THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES 21 G 485 SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES 22 G 485 GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES 23 G 485 GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES 24 G 485 GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES 25 G 485 ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES 26 G 485 HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES 27 G 485 ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES 28 G 485 ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES 29 G 485 PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES 30 G 485 VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES 31 G 485 LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES 32 G 485 GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES 33 G 485 GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES 34 G 485 LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES 35 G 485 PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES 36 G 485 LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES 37 G 485 ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES 38 G 485 ALA SER VAL ALA
SEQRES 1 L 139 MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES 2 L 139 LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES 3 L 139 LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES 4 L 139 ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES 5 L 139 LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES 6 L 139 MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES 7 L 139 TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES 8 L 139 GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES 9 L 139 ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES 10 L 139 GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES 11 L 139 GLN ALA GLY PRO GLU GLY SER ARG TYR
HET PO4 A 501 5
HET PO4 A 502 5
HET PO4 C 503 5
HET PO4 C 504 5
HET PO4 E 505 5
HET PO4 E 506 5
HET PO4 G 507 5
HET PO4 G 508 5
HETNAM PO4 PHOSPHATE ION
FORMUL 9 PO4 8(O4 P 3-)
HELIX 1 1 PRO A 53 GLY A 62 1 10
HELIX 2 2 THR A 74 THR A 78 5 5
HELIX 3 3 ASP A 81 TYR A 83 5 3
HELIX 4 4 LEU A 108 LEU A 110 5 3
HELIX 5 5 ILE A 116 ILE A 124 1 9
HELIX 6 6 VAL A 127 SER A 129 5 3
HELIX 7 7 VAL A 145 THR A 150 1 6
HELIX 8 8 ILE A 158 LEU A 165 1 8
HELIX 9 9 GLY A 185 LYS A 197 1 13
HELIX 10 10 TRP A 217 THR A 235 1 19
HELIX 11 11 MET A 250 LEU A 263 1 14
HELIX 12 12 LEU A 272 VAL A 274 5 3
HELIX 13 13 TRP A 276 ASN A 289 1 14
HELIX 14 14 HIS A 300 THR A 304 5 5
HELIX 15 15 PHE A 313 ALA A 323 1 11
HELIX 16 16 PRO A 341 ARG A 352 1 12
HELIX 17 17 LEU A 360 ARG A 362 5 3
HELIX 18 18 ALA A 386 PHE A 396 5 11
HELIX 19 19 GLY A 406 ILE A 409 1 4
HELIX 20 20 GLY A 414 GLU A 435 1 22
HELIX 21 21 ILE A 439 TRP A 453 1 15
HELIX 22 22 GLY A 455 THR A 463 1 9
HELIX 23 23 ASP I 16 GLN I 29 1 14
HELIX 24 24 ALA I 61 THR I 74 1 14
HELIX 25 25 ARG I 102 ALA I 104 5 3
HELIX 26 26 PRO C 53 GLY C 62 1 10
HELIX 27 27 THR C 74 THR C 78 5 5
HELIX 28 28 ASP C 81 TYR C 83 5 3
HELIX 29 29 LEU C 108 LEU C 110 5 3
HELIX 30 30 ILE C 116 ILE C 124 1 9
HELIX 31 31 VAL C 127 SER C 129 5 3
HELIX 32 32 VAL C 145 THR C 150 1 6
HELIX 33 33 ILE C 158 LEU C 165 1 8
HELIX 34 34 GLY C 185 LYS C 197 1 13
HELIX 35 35 TRP C 217 THR C 235 1 19
HELIX 36 36 MET C 250 SER C 262 1 13
HELIX 37 37 LEU C 272 VAL C 274 5 3
HELIX 38 38 TRP C 276 ASN C 289 1 14
HELIX 39 39 HIS C 300 THR C 304 5 5
HELIX 40 40 PHE C 313 ALA C 323 1 11
HELIX 41 41 PRO C 341 ARG C 352 1 12
HELIX 42 42 LEU C 360 ARG C 362 5 3
HELIX 43 43 ALA C 386 LEU C 395 5 10
HELIX 44 44 GLY C 406 ILE C 409 1 4
HELIX 45 45 GLY C 414 GLU C 435 1 22
HELIX 46 46 ILE C 439 TRP C 453 1 15
HELIX 47 47 GLY C 455 THR C 463 1 9
HELIX 48 48 ASP J 16 GLN J 29 1 14
HELIX 49 49 ALA J 61 THR J 74 1 14
HELIX 50 50 ARG J 102 ALA J 104 5 3
HELIX 51 51 PRO E 53 GLY E 62 1 10
HELIX 52 52 THR E 74 THR E 78 5 5
HELIX 53 53 ASP E 81 TYR E 83 5 3
HELIX 54 54 LEU E 108 LEU E 110 5 3
HELIX 55 55 ILE E 116 ILE E 124 1 9
HELIX 56 56 VAL E 127 SER E 129 5 3
HELIX 57 57 VAL E 145 THR E 150 1 6
HELIX 58 58 ILE E 158 LEU E 165 1 8
HELIX 59 59 GLY E 185 LYS E 197 1 13
HELIX 60 60 TRP E 217 THR E 235 1 19
HELIX 61 61 MET E 250 LEU E 263 1 14
HELIX 62 62 LEU E 272 VAL E 274 5 3
HELIX 63 63 TRP E 276 ASN E 289 1 14
HELIX 64 64 HIS E 300 THR E 304 5 5
HELIX 65 65 PHE E 313 ALA E 323 1 11
HELIX 66 66 PRO E 341 ARG E 352 1 12
HELIX 67 67 LEU E 360 ARG E 362 5 3
HELIX 68 68 ALA E 386 PHE E 396 5 11
HELIX 69 69 GLY E 406 ILE E 409 1 4
HELIX 70 70 GLY E 414 GLU E 435 1 22
HELIX 71 71 ILE E 439 TRP E 453 1 15
HELIX 72 72 GLY E 455 THR E 463 1 9
HELIX 73 73 ASP K 16 GLN K 29 1 14
HELIX 74 74 ALA K 61 THR K 74 1 14
HELIX 75 75 ARG K 102 ALA K 104 5 3
HELIX 76 76 PRO G 53 GLY G 62 1 10
HELIX 77 77 THR G 74 THR G 78 5 5
HELIX 78 78 ASP G 81 TYR G 83 5 3
HELIX 79 79 LEU G 108 LEU G 110 5 3
HELIX 80 80 ILE G 116 ILE G 124 1 9
HELIX 81 81 VAL G 127 SER G 129 5 3
HELIX 82 82 VAL G 145 THR G 150 1 6
HELIX 83 83 ILE G 158 LEU G 165 1 8
HELIX 84 84 GLY G 185 LYS G 197 1 13
HELIX 85 85 TRP G 217 THR G 235 1 19
HELIX 86 86 MET G 250 LEU G 263 1 14
HELIX 87 87 LEU G 272 VAL G 274 5 3
HELIX 88 88 TRP G 276 ASN G 289 1 14
HELIX 89 89 HIS G 300 THR G 304 5 5
HELIX 90 90 PHE G 313 ALA G 323 1 11
HELIX 91 91 PRO G 341 ARG G 352 1 12
HELIX 92 92 LEU G 360 ARG G 362 5 3
HELIX 93 93 ALA G 386 PHE G 396 5 11
HELIX 94 94 GLY G 406 ILE G 409 1 4
HELIX 95 95 GLY G 414 GLU G 435 1 22
HELIX 96 96 ILE G 439 TRP G 453 1 15
HELIX 97 97 GLY G 455 THR G 463 1 9
HELIX 98 98 ASP L 16 GLN L 29 1 14
HELIX 99 99 ALA L 61 THR L 74 1 14
HELIX 100 100 ARG L 102 ALA L 104 5 3
SHEET 1 A 4 VAL A 90 PRO A 92 0
SHEET 2 A 4 PHE A 100 ASP A 107 -1 N PHE A 101 O ASP A 91
SHEET 3 A 4 ASP A 38 ILE A 45 -1 N ILE A 45 O PHE A 100
SHEET 4 A 4 LEU A 138 ARG A 142 -1 N ARG A 142 O LEU A 40
SHEET 1 B 6 GLY A 240 TYR A 242 0
SHEET 2 B 6 PHE A 202 LYS A 204 1 N MET A 203 O GLY A 240
SHEET 3 B 6 LEU A 172 THR A 176 1 N ALA A 175 O PHE A 202
SHEET 4 B 6 VAL A 400 PHE A 404 1 N LEU A 402 O LEU A 172
SHEET 5 B 6 MET A 377 GLY A 382 1 N PRO A 378 O VAL A 401
SHEET 6 B 6 HIS A 327 HIS A 329 1 N MET A 328 O MET A 377
SHEET 1 C 2 ILE A 267 ASP A 271 0
SHEET 2 C 2 ILE A 292 HIS A 296 1 N ILE A 292 O ILE A 268
SHEET 1 D 3 ALA I 32 THR I 38 0
SHEET 2 D 3 TYR I 79 ASP I 86 -1 N PHE I 85 O ALA I 32
SHEET 3 D 3 VAL I 91 SER I 97 -1 N MET I 96 O VAL I 82
SHEET 1 E 2 ARG I 110 GLU I 115 0
SHEET 2 E 2 LEU I 121 GLU I 126 -1 N GLU I 126 O ARG I 110
SHEET 1 F 4 VAL C 90 PRO C 92 0
SHEET 2 F 4 PHE C 100 ASP C 107 -1 N PHE C 101 O ASP C 91
SHEET 3 F 4 ASP C 38 ILE C 45 -1 N ILE C 45 O PHE C 100
SHEET 4 F 4 LEU C 138 ARG C 142 -1 N ARG C 142 O LEU C 40
SHEET 1 G 6 GLY C 240 TYR C 242 0
SHEET 2 G 6 PHE C 202 LYS C 204 1 N MET C 203 O GLY C 240
SHEET 3 G 6 LEU C 172 THR C 176 1 N ALA C 175 O PHE C 202
SHEET 4 G 6 VAL C 400 PHE C 404 1 N LEU C 402 O LEU C 172
SHEET 5 G 6 MET C 377 GLY C 382 1 N PRO C 378 O VAL C 401
SHEET 6 G 6 HIS C 327 HIS C 329 1 N MET C 328 O MET C 377
SHEET 1 H 2 ILE C 267 ASP C 271 0
SHEET 2 H 2 ILE C 292 HIS C 296 1 N ILE C 292 O ILE C 268
SHEET 1 I 3 ALA J 32 THR J 38 0
SHEET 2 I 3 TYR J 79 ASP J 86 -1 N PHE J 85 O ALA J 32
SHEET 3 I 3 VAL J 91 SER J 97 -1 N MET J 96 O VAL J 82
SHEET 1 J 2 ARG J 110 GLU J 115 0
SHEET 2 J 2 LEU J 121 GLU J 126 -1 N GLU J 126 O ARG J 110
SHEET 1 K 4 VAL E 90 PRO E 92 0
SHEET 2 K 4 PHE E 100 ASP E 107 -1 N PHE E 101 O ASP E 91
SHEET 3 K 4 ASP E 38 ILE E 45 -1 N ILE E 45 O PHE E 100
SHEET 4 K 4 LEU E 138 ARG E 142 -1 N ARG E 142 O LEU E 40
SHEET 1 L 6 GLY E 240 TYR E 242 0
SHEET 2 L 6 PHE E 202 LYS E 204 1 N MET E 203 O GLY E 240
SHEET 3 L 6 LEU E 172 THR E 176 1 N ALA E 175 O PHE E 202
SHEET 4 L 6 VAL E 400 PHE E 404 1 N LEU E 402 O LEU E 172
SHEET 5 L 6 MET E 377 GLY E 382 1 N PRO E 378 O VAL E 401
SHEET 6 L 6 HIS E 327 HIS E 329 1 N MET E 328 O MET E 377
SHEET 1 M 2 ILE E 267 ASP E 271 0
SHEET 2 M 2 ILE E 292 HIS E 296 1 N ILE E 292 O ILE E 268
SHEET 1 N 3 ALA K 32 THR K 38 0
SHEET 2 N 3 TYR K 79 ASP K 86 -1 N PHE K 85 O ALA K 32
SHEET 3 N 3 VAL K 91 SER K 97 -1 N MET K 96 O VAL K 82
SHEET 1 O 2 ARG K 110 GLU K 115 0
SHEET 2 O 2 LEU K 121 GLU K 126 -1 N GLU K 126 O ARG K 110
SHEET 1 P 4 VAL G 90 PRO G 92 0
SHEET 2 P 4 PHE G 100 ASP G 107 -1 N PHE G 101 O ASP G 91
SHEET 3 P 4 ASP G 38 ILE G 45 -1 N ILE G 45 O PHE G 100
SHEET 4 P 4 LEU G 138 ARG G 142 -1 N ARG G 142 O LEU G 40
SHEET 1 Q 6 GLY G 240 TYR G 242 0
SHEET 2 Q 6 PHE G 202 LYS G 204 1 N MET G 203 O GLY G 240
SHEET 3 Q 6 LEU G 172 THR G 176 1 N ALA G 175 O PHE G 202
SHEET 4 Q 6 VAL G 400 PHE G 404 1 N LEU G 402 O LEU G 172
SHEET 5 Q 6 MET G 377 GLY G 382 1 N PRO G 378 O VAL G 401
SHEET 6 Q 6 HIS G 327 HIS G 329 1 N MET G 328 O MET G 377
SHEET 1 R 2 ILE G 267 ASP G 271 0
SHEET 2 R 2 ILE G 292 HIS G 296 1 N ILE G 292 O ILE G 268
SHEET 1 S 3 ALA L 32 THR L 38 0
SHEET 2 S 3 TYR L 79 ASP L 86 -1 N PHE L 85 O ALA L 32
SHEET 3 S 3 VAL L 91 SER L 97 -1 N MET L 96 O VAL L 82
SHEET 1 T 2 ARG L 110 GLU L 115 0
SHEET 2 T 2 LEU L 121 GLU L 126 -1 N GLU L 126 O ARG L 110
SSBOND 1 CYS A 278 CYS E 278 1555 8665 2.86
SSBOND 2 CYS C 278 CYS C 278 1555 8665 2.78
SSBOND 3 CYS G 278 CYS G 278 1555 8665 2.88
SITE 1 AC1 5 ARG A 297 HIS A 329 GLU A 338 SER A 381
SITE 2 AC1 5 ASN E 126
SITE 1 AC2 5 GLY A 382 GLY A 405 GLY A 406 THR E 68
SITE 2 AC2 5 TRP E 69
SITE 1 AC3 4 ARG C 297 HIS C 329 GLU C 338 SER C 381
SITE 1 AC4 6 THR C 68 TRP C 69 GLY C 382 GLY C 383
SITE 2 AC4 6 GLY C 405 GLY C 406
SITE 1 AC5 4 ARG E 297 HIS E 329 GLU E 338 SER E 381
SITE 1 AC6 5 THR A 68 TRP A 69 GLY E 382 GLY E 405
SITE 2 AC6 5 GLY E 406
SITE 1 AC7 4 ARG G 297 HIS G 329 GLU G 338 SER G 381
SITE 1 AC8 4 THR G 68 TRP G 69 GLY G 405 GLY G 406
CRYST1 112.000 112.000 402.700 90.00 90.00 90.00 P 43 21 2 32
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 0.008929 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002483 0.00000
MTRIX1 1 0.013000 -0.987000 0.163000 93.96200 1
MTRIX2 1 1.000000 0.014000 0.001000 100.37800 1
MTRIX3 1 -0.003000 0.163000 0.987000 -16.07900 1
MTRIX1 2 0.014000 -0.986000 0.168000 93.52000 1
MTRIX2 2 1.000000 0.014000 -0.001000 100.51000 1
MTRIX3 2 -0.001000 0.168000 0.986000 -16.49300 1
MTRIX1 3 -0.987000 0.006000 0.160000 -6.82400 1
MTRIX2 3 0.020000 -0.987000 0.162000 196.01401 1
MTRIX3 3 0.159000 0.164000 0.974000 -15.70500 1
MTRIX1 4 -0.986000 0.012000 0.165000 -7.68900 1
MTRIX2 4 0.015000 -0.987000 0.162000 196.03500 1
MTRIX3 4 0.165000 0.162000 0.973000 -15.43400 1
MTRIX1 5 0.004000 1.000000 0.000000 -101.89000 1
MTRIX2 5 -0.987000 0.004000 0.161000 95.24400 1
MTRIX3 5 0.161000 -0.001000 0.987000 0.53300 1
MTRIX1 6 0.008000 1.000000 0.002000 -102.03200 1
MTRIX2 6 -0.986000 0.008000 0.166000 94.50700 1
MTRIX3 6 0.166000 -0.004000 0.986000 0.95800 1
(ATOM LINES ARE NOT SHOWN.)
END
