HEADER LYASE 18-APR-01 1IGW
TITLE CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM THE A219C MUTANT OF
TITLE 2 ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ISOCITRASE, ISOCITRATASE, ICL;
COMPND 5 EC: 4.1.3.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ACEA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JE10;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PICL
KEYWDS BETA BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.BRITTON,I.S.B.ABEYSINGHE,P.J.BAKER,V.BARYNIN,P.DIEHL,
AUTHOR 2 S.J.LANGRIDGE,B.A.MCFADDEN,S.E.SEDELNIKOVA,T.J.STILLMAN,
AUTHOR 3 K.WEERADECHAPON,D.W.RICE
REVDAT 5 15-NOV-23 1IGW 1 LINK ATOM
REVDAT 4 27-OCT-21 1IGW 1 REMARK SEQADV LINK
REVDAT 3 04-OCT-17 1IGW 1 REMARK
REVDAT 2 24-FEB-09 1IGW 1 VERSN
REVDAT 1 05-SEP-01 1IGW 0
JRNL AUTH K.L.BRITTON,I.S.ABEYSINGHE,P.J.BAKER,V.BARYNIN,P.DIEHL,
JRNL AUTH 2 S.J.LANGRIDGE,B.A.MCFADDEN,S.E.SEDELNIKOVA,T.J.STILLMAN,
JRNL AUTH 3 K.WEERADECHAPON,D.W.RICE
JRNL TITL THE STRUCTURE AND DOMAIN ORGANIZATION OF ESCHERICHIA COLI
JRNL TITL 2 ISOCITRATE LYASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 1209 2001
JRNL REFN ISSN 0907-4449
JRNL PMID 11526312
JRNL DOI 10.1107/S0907444901008642
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.I.ABEYSINGHE,P.J.BAKER,D.W.RICE,H.F.RODGERS,T.J.STILLMAN,
REMARK 1 AUTH 2 Y.H.KO,B.A.MCFADDEN,H.G.NIMMO
REMARK 1 TITL USE OF CHEMICAL MODIFICATION IN THE CRYSTALLIZATION OF
REMARK 1 TITL 2 ISOCITRATE LYASE FROM ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 220 13 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 88762
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4666
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12619
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 767
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.007 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.600 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 33.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.05100
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.21600
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: CCP4, TFFC, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MEPEG 2000, MAGNESIUM CHLORIDE, ETHYL
REMARK 280 MERCURY THIOSALICYLATE, HEPES, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,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 132.93333
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 66.46667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE GIVEN TETRAMER DEFINES THE BIOLOGICAL ASSEMBLY
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 32960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -753.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 196
REMARK 465 HIS A 197
REMARK 465 MET A 198
REMARK 465 GLY A 199
REMARK 465 SER A 319
REMARK 465 PRO A 320
REMARK 465 SER A 321
REMARK 465 PHE A 322
REMARK 465 ASN A 323
REMARK 465 TRP A 324
REMARK 465 GLN A 325
REMARK 465 LYS A 326
REMARK 465 ASN A 327
REMARK 465 LEU A 328
REMARK 465 ASP A 329
REMARK 465 ASP A 330
REMARK 465 LYS A 331
REMARK 465 THR A 332
REMARK 465 ILE A 333
REMARK 465 ALA A 334
REMARK 465 GLY A 418
REMARK 465 THR A 419
REMARK 465 SER A 420
REMARK 465 SER A 421
REMARK 465 VAL A 422
REMARK 465 THR A 423
REMARK 465 ALA A 424
REMARK 465 LEU A 425
REMARK 465 THR A 426
REMARK 465 GLY A 427
REMARK 465 SER A 428
REMARK 465 THR A 429
REMARK 465 GLU A 430
REMARK 465 GLU A 431
REMARK 465 SER A 432
REMARK 465 GLN A 433
REMARK 465 PHE A 434
REMARK 465 MET B 1
REMARK 465 CYS B 195
REMARK 465 GLY B 196
REMARK 465 HIS B 197
REMARK 465 MET B 198
REMARK 465 GLY B 199
REMARK 465 GLY B 418
REMARK 465 THR B 419
REMARK 465 SER B 420
REMARK 465 SER B 421
REMARK 465 VAL B 422
REMARK 465 THR B 423
REMARK 465 ALA B 424
REMARK 465 LEU B 425
REMARK 465 THR B 426
REMARK 465 GLY B 427
REMARK 465 SER B 428
REMARK 465 THR B 429
REMARK 465 GLU B 430
REMARK 465 GLU B 431
REMARK 465 SER B 432
REMARK 465 GLN B 433
REMARK 465 PHE B 434
REMARK 465 MET C 1
REMARK 465 GLY C 418
REMARK 465 THR C 419
REMARK 465 SER C 420
REMARK 465 SER C 421
REMARK 465 VAL C 422
REMARK 465 THR C 423
REMARK 465 ALA C 424
REMARK 465 LEU C 425
REMARK 465 THR C 426
REMARK 465 GLY C 427
REMARK 465 SER C 428
REMARK 465 THR C 429
REMARK 465 GLU C 430
REMARK 465 GLU C 431
REMARK 465 SER C 432
REMARK 465 GLN C 433
REMARK 465 PHE C 434
REMARK 465 MET D 1
REMARK 465 LYS D 193
REMARK 465 LYS D 194
REMARK 465 CYS D 195
REMARK 465 GLY D 196
REMARK 465 HIS D 197
REMARK 465 MET D 198
REMARK 465 GLY D 199
REMARK 465 GLN D 325
REMARK 465 LYS D 326
REMARK 465 ASN D 327
REMARK 465 LEU D 328
REMARK 465 GLY D 418
REMARK 465 THR D 419
REMARK 465 SER D 420
REMARK 465 SER D 421
REMARK 465 VAL D 422
REMARK 465 THR D 423
REMARK 465 ALA D 424
REMARK 465 LEU D 425
REMARK 465 THR D 426
REMARK 465 GLY D 427
REMARK 465 SER D 428
REMARK 465 THR D 429
REMARK 465 GLU D 430
REMARK 465 GLU D 431
REMARK 465 SER D 432
REMARK 465 GLN D 433
REMARK 465 PHE D 434
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 HG HG A 435 O HOH A 1445 1.15
REMARK 500 OE1 GLN D 337 O HOH D 1562 1.28
REMARK 500 HG HG C 438 O HOH C 1640 1.29
REMARK 500 HG HG C 438 O HOH C 1516 1.40
REMARK 500 O HOH C 1516 O HOH C 1640 1.43
REMARK 500 O GLN B 325 N ASN B 327 1.76
REMARK 500 OE1 GLU B 296 NH1 ARG B 299 1.85
REMARK 500 O HOH A 1461 O HOH A 1599 1.91
REMARK 500 OE1 GLN B 416 SG CYS C 195 1.97
REMARK 500 N SER D 319 O HOH D 1580 2.05
REMARK 500 O HOH C 1553 O HOH C 1573 2.05
REMARK 500 O HOH D 1543 O HOH D 1580 2.07
REMARK 500 CB CYS A 195 O HOH D 1565 2.08
REMARK 500 NE2 GLN B 325 OE1 GLN C 383 2.10
REMARK 500 O VAL C 397 O HOH C 1569 2.11
REMARK 500 CB ASP D 409 O HOH D 1539 2.11
REMARK 500 O HOH A 1458 O HOH A 1484 2.15
REMARK 500 ND1 HIS B 306 O HOH B 1454 2.16
REMARK 500 CE2 PHE C 387 O HOH C 1621 2.16
REMARK 500 O HOH C 1592 O HOH C 1610 2.17
REMARK 500 OE1 GLN C 109 O HOH C 1558 2.17
REMARK 500 O HOH C 1533 O HOH C 1621 2.17
REMARK 500 OD2 ASP B 329 CG LYS B 331 2.18
REMARK 500 O HOH C 1683 O HOH C 1686 2.18
REMARK 500 O SER D 291 CE1 PHE D 322 2.18
REMARK 500 ND1 HIS C 306 O HOH C 1447 2.18
REMARK 500 OE1 GLU A 208 O HOH A 1606 2.18
REMARK 500 O HOH D 1550 O HOH D 1578 2.18
REMARK 500 O HOH B 1490 O HOH B 1512 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR B 405 C GLY B 406 N -0.140
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 2 N - CA - C ANGL. DEV. = -25.0 DEGREES
REMARK 500 HIS A 184 CA - CB - CG ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG B 36 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU B 72 CA - CB - CG ANGL. DEV. = 20.2 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 217 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 217 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASN B 327 N - CA - CB ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASN B 327 CA - C - O ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU B 328 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 TYR B 369 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG C 25 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 HIS C 184 CA - CB - CG ANGL. DEV. = 12.1 DEGREES
REMARK 500 CYS C 318 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG D 217 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 217 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 98 18.21 -156.59
REMARK 500 ALA A 99 45.11 -157.43
REMARK 500 ILE A 140 103.38 -54.11
REMARK 500 PRO A 145 15.07 -66.11
REMARK 500 GLU A 159 -123.12 46.08
REMARK 500 VAL A 382 -59.42 -125.34
REMARK 500 SER A 398 71.14 -103.01
REMARK 500 ASP B 98 10.45 -148.92
REMARK 500 ALA B 99 48.77 -150.19
REMARK 500 GLU B 159 -121.48 49.05
REMARK 500 SER B 191 2.51 -62.09
REMARK 500 VAL B 192 25.27 -142.02
REMARK 500 PRO B 226 44.26 -73.21
REMARK 500 PRO B 293 97.07 -66.65
REMARK 500 LYS B 326 -17.46 -24.91
REMARK 500 ASN B 327 131.40 -173.66
REMARK 500 LEU B 328 148.77 157.50
REMARK 500 GLN B 416 76.59 -103.91
REMARK 500 ASP C 98 15.92 -149.76
REMARK 500 ALA C 99 45.70 -155.43
REMARK 500 PRO C 145 -3.52 -46.42
REMARK 500 ARG C 146 15.83 -145.29
REMARK 500 GLU C 159 -125.86 43.83
REMARK 500 HIS C 197 63.76 -19.88
REMARK 500 VAL C 382 -57.32 -124.15
REMARK 500 ASP D 98 12.04 -153.23
REMARK 500 ALA D 99 43.10 -153.02
REMARK 500 PRO D 145 -16.40 -38.63
REMARK 500 GLU D 159 -119.21 50.06
REMARK 500 LEU D 189 77.53 -119.03
REMARK 500 PRO D 226 44.85 -78.88
REMARK 500 PHE D 322 -138.98 -38.87
REMARK 500 ASN D 323 66.07 164.17
REMARK 500 GLN D 416 31.21 -81.66
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 HG A 435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 42 O
REMARK 620 2 CYS A 43 SG 95.8
REMARK 620 3 HOH A1600 O 83.6 169.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD2
REMARK 620 2 PYR A1444 O 76.4
REMARK 620 3 PYR A1444 O3 90.5 70.6
REMARK 620 4 HOH A1630 O 89.9 152.0 85.4
REMARK 620 5 HOH A1631 O 168.7 94.6 93.0 101.1
REMARK 620 6 HOH A1632 O 91.4 89.4 158.8 115.7 81.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 436 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 219 O
REMARK 620 2 CYS A 219 SG 75.9
REMARK 620 3 HOH C1514 O 101.3 156.0
REMARK 620 4 HOH C1571 O 99.1 146.8 57.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 245 O
REMARK 620 2 CYS A 245 SG 87.6
REMARK 620 3 ASP A 246 N 38.0 68.6
REMARK 620 4 HOH B1609 O 152.0 64.4 122.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 438 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 288 O
REMARK 620 2 CYS A 288 SG 73.6
REMARK 620 3 HOH A1561 O 98.5 165.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 439 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 318 SG
REMARK 620 2 HOH A1461 O 147.5
REMARK 620 3 HOH A1507 O 118.8 88.7
REMARK 620 4 HOH A1549 O 60.1 152.2 70.4
REMARK 620 5 HOH A1599 O 113.7 33.8 118.8 170.5
REMARK 620 6 MET D 375 SD 125.6 84.5 51.4 68.3 114.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 436 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1596 O
REMARK 620 2 CYS C 219 SG 173.4
REMARK 620 3 CYS C 219 O 107.7 72.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 42 O
REMARK 620 2 CYS B 43 SG 92.8
REMARK 620 3 HOH B1509 O 101.2 151.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 157 OD2
REMARK 620 2 PYR B1445 O 77.4
REMARK 620 3 PYR B1445 O3 89.3 84.5
REMARK 620 4 HOH B1633 O 90.0 86.6 171.0
REMARK 620 5 HOH B1634 O 173.7 101.0 96.7 83.7
REMARK 620 6 HOH B1635 O 82.3 158.3 87.9 100.9 100.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 436 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 219 SG
REMARK 620 2 CYS B 219 O 74.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 245 SG
REMARK 620 2 CYS B 245 O 85.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 438 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 288 O
REMARK 620 2 CYS B 288 SG 78.4
REMARK 620 3 HOH B1570 O 103.1 162.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 439 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 318 N
REMARK 620 2 CYS B 318 SG 73.4
REMARK 620 3 PHE B 349 O 57.0 104.4
REMARK 620 4 HOH B1453 O 115.6 65.8 169.9
REMARK 620 5 HOH B1490 O 159.6 127.0 111.6 77.6
REMARK 620 6 HOH B1512 O 120.7 159.6 95.9 94.0 39.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 42 O
REMARK 620 2 CYS C 43 SG 93.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 157 OD2
REMARK 620 2 PYR C1446 O 84.3
REMARK 620 3 PYR C1446 O3 94.4 88.1
REMARK 620 4 HOH C1694 O 168.6 99.6 96.4
REMARK 620 5 HOH C1695 O 85.9 164.8 81.2 92.2
REMARK 620 6 HOH C1696 O 87.0 88.9 176.5 82.4 102.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 440 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 195 SG
REMARK 620 2 CYS C 195 O 79.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 245 O
REMARK 620 2 CYS C 245 SG 87.0
REMARK 620 3 HOH C1652 O 150.9 64.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 438 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 288 SG
REMARK 620 2 CYS C 288 O 71.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG C 439 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 318 SG
REMARK 620 2 HOH C1510 O 156.4
REMARK 620 3 HOH C1561 O 138.3 60.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D 437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C1688 O
REMARK 620 2 CYS D 245 O 160.5
REMARK 620 3 CYS D 245 SG 106.5 91.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D 435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 42 O
REMARK 620 2 CYS D 43 SG 91.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 157 OD2
REMARK 620 2 PYR D1447 O3 91.0
REMARK 620 3 PYR D1447 O 97.6 90.9
REMARK 620 4 HOH D1584 O 99.9 168.8 89.7
REMARK 620 5 HOH D1585 O 166.9 87.3 95.5 81.6
REMARK 620 6 HOH D1586 O 79.3 77.6 168.0 102.2 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D 436 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 219 O
REMARK 620 2 CYS D 219 SG 73.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D 438 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 288 SG
REMARK 620 2 CYS D 288 O 70.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D 439 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 318 N
REMARK 620 2 CYS D 318 SG 82.6
REMARK 620 3 PHE D 349 O 55.0 115.3
REMARK 620 4 HOH D1562 O 136.3 136.7 105.1
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 HG A 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 439
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 439
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 439
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 440
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 439
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 1444
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 1445
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 1446
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR D 1447
DBREF 1IGW A 1 434 UNP P0A9G6 ACEA_ECOLI 1 434
DBREF 1IGW B 1 434 UNP P0A9G6 ACEA_ECOLI 1 434
DBREF 1IGW C 1 434 UNP P0A9G6 ACEA_ECOLI 1 434
DBREF 1IGW D 1 434 UNP P0A9G6 ACEA_ECOLI 1 434
SEQADV 1IGW CYS A 219 UNP P0A9G6 ALA 219 ENGINEERED MUTATION
SEQADV 1IGW CYS B 219 UNP P0A9G6 ALA 219 ENGINEERED MUTATION
SEQADV 1IGW CYS C 219 UNP P0A9G6 ALA 219 ENGINEERED MUTATION
SEQADV 1IGW CYS D 219 UNP P0A9G6 ALA 219 ENGINEERED MUTATION
SEQRES 1 A 434 MET LYS THR ARG THR GLN GLN ILE GLU GLU LEU GLN LYS
SEQRES 2 A 434 GLU TRP THR GLN PRO ARG TRP GLU GLY ILE THR ARG PRO
SEQRES 3 A 434 TYR SER ALA GLU ASP VAL VAL LYS LEU ARG GLY SER VAL
SEQRES 4 A 434 ASN PRO GLU CYS THR LEU ALA GLN LEU GLY ALA ALA LYS
SEQRES 5 A 434 MET TRP ARG LEU LEU HIS GLY GLU SER LYS LYS GLY TYR
SEQRES 6 A 434 ILE ASN SER LEU GLY ALA LEU THR GLY GLY GLN ALA LEU
SEQRES 7 A 434 GLN GLN ALA LYS ALA GLY ILE GLU ALA VAL TYR LEU SER
SEQRES 8 A 434 GLY TRP GLN VAL ALA ALA ASP ALA ASN LEU ALA ALA SER
SEQRES 9 A 434 MET TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER VAL
SEQRES 10 A 434 PRO ALA VAL VAL GLU ARG ILE ASN ASN THR PHE ARG ARG
SEQRES 11 A 434 ALA ASP GLN ILE GLN TRP SER ALA GLY ILE GLU PRO GLY
SEQRES 12 A 434 ASP PRO ARG TYR VAL ASP TYR PHE LEU PRO ILE VAL ALA
SEQRES 13 A 434 ASP ALA GLU ALA GLY PHE GLY GLY VAL LEU ASN ALA PHE
SEQRES 14 A 434 GLU LEU MET LYS ALA MET ILE GLU ALA GLY ALA ALA ALA
SEQRES 15 A 434 VAL HIS PHE GLU ASP GLN LEU ALA SER VAL LYS LYS CYS
SEQRES 16 A 434 GLY HIS MET GLY GLY LYS VAL LEU VAL PRO THR GLN GLU
SEQRES 17 A 434 ALA ILE GLN LYS LEU VAL ALA ALA ARG LEU CYS ALA ASP
SEQRES 18 A 434 VAL THR GLY VAL PRO THR LEU LEU VAL ALA ARG THR ASP
SEQRES 19 A 434 ALA ASP ALA ALA ASP LEU ILE THR SER ASP CYS ASP PRO
SEQRES 20 A 434 TYR ASP SER GLU PHE ILE THR GLY GLU ARG THR SER GLU
SEQRES 21 A 434 GLY PHE PHE ARG THR HIS ALA GLY ILE GLU GLN ALA ILE
SEQRES 22 A 434 SER ARG GLY LEU ALA TYR ALA PRO TYR ALA ASP LEU VAL
SEQRES 23 A 434 TRP CYS GLU THR SER THR PRO ASP LEU GLU LEU ALA ARG
SEQRES 24 A 434 ARG PHE ALA GLN ALA ILE HIS ALA LYS TYR PRO GLY LYS
SEQRES 25 A 434 LEU LEU ALA TYR ASN CYS SER PRO SER PHE ASN TRP GLN
SEQRES 26 A 434 LYS ASN LEU ASP ASP LYS THR ILE ALA SER PHE GLN GLN
SEQRES 27 A 434 GLN LEU SER ASP MET GLY TYR LYS PHE GLN PHE ILE THR
SEQRES 28 A 434 LEU ALA GLY ILE HIS SER MET TRP PHE ASN MET PHE ASP
SEQRES 29 A 434 LEU ALA ASN ALA TYR ALA GLN GLY GLU GLY MET LYS HIS
SEQRES 30 A 434 TYR VAL GLU LYS VAL GLN GLN PRO GLU PHE ALA ALA ALA
SEQRES 31 A 434 LYS ASP GLY TYR THR PHE VAL SER HIS GLN GLN GLU VAL
SEQRES 32 A 434 GLY THR GLY TYR PHE ASP LYS VAL THR THR ILE ILE GLN
SEQRES 33 A 434 GLY GLY THR SER SER VAL THR ALA LEU THR GLY SER THR
SEQRES 34 A 434 GLU GLU SER GLN PHE
SEQRES 1 B 434 MET LYS THR ARG THR GLN GLN ILE GLU GLU LEU GLN LYS
SEQRES 2 B 434 GLU TRP THR GLN PRO ARG TRP GLU GLY ILE THR ARG PRO
SEQRES 3 B 434 TYR SER ALA GLU ASP VAL VAL LYS LEU ARG GLY SER VAL
SEQRES 4 B 434 ASN PRO GLU CYS THR LEU ALA GLN LEU GLY ALA ALA LYS
SEQRES 5 B 434 MET TRP ARG LEU LEU HIS GLY GLU SER LYS LYS GLY TYR
SEQRES 6 B 434 ILE ASN SER LEU GLY ALA LEU THR GLY GLY GLN ALA LEU
SEQRES 7 B 434 GLN GLN ALA LYS ALA GLY ILE GLU ALA VAL TYR LEU SER
SEQRES 8 B 434 GLY TRP GLN VAL ALA ALA ASP ALA ASN LEU ALA ALA SER
SEQRES 9 B 434 MET TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER VAL
SEQRES 10 B 434 PRO ALA VAL VAL GLU ARG ILE ASN ASN THR PHE ARG ARG
SEQRES 11 B 434 ALA ASP GLN ILE GLN TRP SER ALA GLY ILE GLU PRO GLY
SEQRES 12 B 434 ASP PRO ARG TYR VAL ASP TYR PHE LEU PRO ILE VAL ALA
SEQRES 13 B 434 ASP ALA GLU ALA GLY PHE GLY GLY VAL LEU ASN ALA PHE
SEQRES 14 B 434 GLU LEU MET LYS ALA MET ILE GLU ALA GLY ALA ALA ALA
SEQRES 15 B 434 VAL HIS PHE GLU ASP GLN LEU ALA SER VAL LYS LYS CYS
SEQRES 16 B 434 GLY HIS MET GLY GLY LYS VAL LEU VAL PRO THR GLN GLU
SEQRES 17 B 434 ALA ILE GLN LYS LEU VAL ALA ALA ARG LEU CYS ALA ASP
SEQRES 18 B 434 VAL THR GLY VAL PRO THR LEU LEU VAL ALA ARG THR ASP
SEQRES 19 B 434 ALA ASP ALA ALA ASP LEU ILE THR SER ASP CYS ASP PRO
SEQRES 20 B 434 TYR ASP SER GLU PHE ILE THR GLY GLU ARG THR SER GLU
SEQRES 21 B 434 GLY PHE PHE ARG THR HIS ALA GLY ILE GLU GLN ALA ILE
SEQRES 22 B 434 SER ARG GLY LEU ALA TYR ALA PRO TYR ALA ASP LEU VAL
SEQRES 23 B 434 TRP CYS GLU THR SER THR PRO ASP LEU GLU LEU ALA ARG
SEQRES 24 B 434 ARG PHE ALA GLN ALA ILE HIS ALA LYS TYR PRO GLY LYS
SEQRES 25 B 434 LEU LEU ALA TYR ASN CYS SER PRO SER PHE ASN TRP GLN
SEQRES 26 B 434 LYS ASN LEU ASP ASP LYS THR ILE ALA SER PHE GLN GLN
SEQRES 27 B 434 GLN LEU SER ASP MET GLY TYR LYS PHE GLN PHE ILE THR
SEQRES 28 B 434 LEU ALA GLY ILE HIS SER MET TRP PHE ASN MET PHE ASP
SEQRES 29 B 434 LEU ALA ASN ALA TYR ALA GLN GLY GLU GLY MET LYS HIS
SEQRES 30 B 434 TYR VAL GLU LYS VAL GLN GLN PRO GLU PHE ALA ALA ALA
SEQRES 31 B 434 LYS ASP GLY TYR THR PHE VAL SER HIS GLN GLN GLU VAL
SEQRES 32 B 434 GLY THR GLY TYR PHE ASP LYS VAL THR THR ILE ILE GLN
SEQRES 33 B 434 GLY GLY THR SER SER VAL THR ALA LEU THR GLY SER THR
SEQRES 34 B 434 GLU GLU SER GLN PHE
SEQRES 1 C 434 MET LYS THR ARG THR GLN GLN ILE GLU GLU LEU GLN LYS
SEQRES 2 C 434 GLU TRP THR GLN PRO ARG TRP GLU GLY ILE THR ARG PRO
SEQRES 3 C 434 TYR SER ALA GLU ASP VAL VAL LYS LEU ARG GLY SER VAL
SEQRES 4 C 434 ASN PRO GLU CYS THR LEU ALA GLN LEU GLY ALA ALA LYS
SEQRES 5 C 434 MET TRP ARG LEU LEU HIS GLY GLU SER LYS LYS GLY TYR
SEQRES 6 C 434 ILE ASN SER LEU GLY ALA LEU THR GLY GLY GLN ALA LEU
SEQRES 7 C 434 GLN GLN ALA LYS ALA GLY ILE GLU ALA VAL TYR LEU SER
SEQRES 8 C 434 GLY TRP GLN VAL ALA ALA ASP ALA ASN LEU ALA ALA SER
SEQRES 9 C 434 MET TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER VAL
SEQRES 10 C 434 PRO ALA VAL VAL GLU ARG ILE ASN ASN THR PHE ARG ARG
SEQRES 11 C 434 ALA ASP GLN ILE GLN TRP SER ALA GLY ILE GLU PRO GLY
SEQRES 12 C 434 ASP PRO ARG TYR VAL ASP TYR PHE LEU PRO ILE VAL ALA
SEQRES 13 C 434 ASP ALA GLU ALA GLY PHE GLY GLY VAL LEU ASN ALA PHE
SEQRES 14 C 434 GLU LEU MET LYS ALA MET ILE GLU ALA GLY ALA ALA ALA
SEQRES 15 C 434 VAL HIS PHE GLU ASP GLN LEU ALA SER VAL LYS LYS CYS
SEQRES 16 C 434 GLY HIS MET GLY GLY LYS VAL LEU VAL PRO THR GLN GLU
SEQRES 17 C 434 ALA ILE GLN LYS LEU VAL ALA ALA ARG LEU CYS ALA ASP
SEQRES 18 C 434 VAL THR GLY VAL PRO THR LEU LEU VAL ALA ARG THR ASP
SEQRES 19 C 434 ALA ASP ALA ALA ASP LEU ILE THR SER ASP CYS ASP PRO
SEQRES 20 C 434 TYR ASP SER GLU PHE ILE THR GLY GLU ARG THR SER GLU
SEQRES 21 C 434 GLY PHE PHE ARG THR HIS ALA GLY ILE GLU GLN ALA ILE
SEQRES 22 C 434 SER ARG GLY LEU ALA TYR ALA PRO TYR ALA ASP LEU VAL
SEQRES 23 C 434 TRP CYS GLU THR SER THR PRO ASP LEU GLU LEU ALA ARG
SEQRES 24 C 434 ARG PHE ALA GLN ALA ILE HIS ALA LYS TYR PRO GLY LYS
SEQRES 25 C 434 LEU LEU ALA TYR ASN CYS SER PRO SER PHE ASN TRP GLN
SEQRES 26 C 434 LYS ASN LEU ASP ASP LYS THR ILE ALA SER PHE GLN GLN
SEQRES 27 C 434 GLN LEU SER ASP MET GLY TYR LYS PHE GLN PHE ILE THR
SEQRES 28 C 434 LEU ALA GLY ILE HIS SER MET TRP PHE ASN MET PHE ASP
SEQRES 29 C 434 LEU ALA ASN ALA TYR ALA GLN GLY GLU GLY MET LYS HIS
SEQRES 30 C 434 TYR VAL GLU LYS VAL GLN GLN PRO GLU PHE ALA ALA ALA
SEQRES 31 C 434 LYS ASP GLY TYR THR PHE VAL SER HIS GLN GLN GLU VAL
SEQRES 32 C 434 GLY THR GLY TYR PHE ASP LYS VAL THR THR ILE ILE GLN
SEQRES 33 C 434 GLY GLY THR SER SER VAL THR ALA LEU THR GLY SER THR
SEQRES 34 C 434 GLU GLU SER GLN PHE
SEQRES 1 D 434 MET LYS THR ARG THR GLN GLN ILE GLU GLU LEU GLN LYS
SEQRES 2 D 434 GLU TRP THR GLN PRO ARG TRP GLU GLY ILE THR ARG PRO
SEQRES 3 D 434 TYR SER ALA GLU ASP VAL VAL LYS LEU ARG GLY SER VAL
SEQRES 4 D 434 ASN PRO GLU CYS THR LEU ALA GLN LEU GLY ALA ALA LYS
SEQRES 5 D 434 MET TRP ARG LEU LEU HIS GLY GLU SER LYS LYS GLY TYR
SEQRES 6 D 434 ILE ASN SER LEU GLY ALA LEU THR GLY GLY GLN ALA LEU
SEQRES 7 D 434 GLN GLN ALA LYS ALA GLY ILE GLU ALA VAL TYR LEU SER
SEQRES 8 D 434 GLY TRP GLN VAL ALA ALA ASP ALA ASN LEU ALA ALA SER
SEQRES 9 D 434 MET TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER VAL
SEQRES 10 D 434 PRO ALA VAL VAL GLU ARG ILE ASN ASN THR PHE ARG ARG
SEQRES 11 D 434 ALA ASP GLN ILE GLN TRP SER ALA GLY ILE GLU PRO GLY
SEQRES 12 D 434 ASP PRO ARG TYR VAL ASP TYR PHE LEU PRO ILE VAL ALA
SEQRES 13 D 434 ASP ALA GLU ALA GLY PHE GLY GLY VAL LEU ASN ALA PHE
SEQRES 14 D 434 GLU LEU MET LYS ALA MET ILE GLU ALA GLY ALA ALA ALA
SEQRES 15 D 434 VAL HIS PHE GLU ASP GLN LEU ALA SER VAL LYS LYS CYS
SEQRES 16 D 434 GLY HIS MET GLY GLY LYS VAL LEU VAL PRO THR GLN GLU
SEQRES 17 D 434 ALA ILE GLN LYS LEU VAL ALA ALA ARG LEU CYS ALA ASP
SEQRES 18 D 434 VAL THR GLY VAL PRO THR LEU LEU VAL ALA ARG THR ASP
SEQRES 19 D 434 ALA ASP ALA ALA ASP LEU ILE THR SER ASP CYS ASP PRO
SEQRES 20 D 434 TYR ASP SER GLU PHE ILE THR GLY GLU ARG THR SER GLU
SEQRES 21 D 434 GLY PHE PHE ARG THR HIS ALA GLY ILE GLU GLN ALA ILE
SEQRES 22 D 434 SER ARG GLY LEU ALA TYR ALA PRO TYR ALA ASP LEU VAL
SEQRES 23 D 434 TRP CYS GLU THR SER THR PRO ASP LEU GLU LEU ALA ARG
SEQRES 24 D 434 ARG PHE ALA GLN ALA ILE HIS ALA LYS TYR PRO GLY LYS
SEQRES 25 D 434 LEU LEU ALA TYR ASN CYS SER PRO SER PHE ASN TRP GLN
SEQRES 26 D 434 LYS ASN LEU ASP ASP LYS THR ILE ALA SER PHE GLN GLN
SEQRES 27 D 434 GLN LEU SER ASP MET GLY TYR LYS PHE GLN PHE ILE THR
SEQRES 28 D 434 LEU ALA GLY ILE HIS SER MET TRP PHE ASN MET PHE ASP
SEQRES 29 D 434 LEU ALA ASN ALA TYR ALA GLN GLY GLU GLY MET LYS HIS
SEQRES 30 D 434 TYR VAL GLU LYS VAL GLN GLN PRO GLU PHE ALA ALA ALA
SEQRES 31 D 434 LYS ASP GLY TYR THR PHE VAL SER HIS GLN GLN GLU VAL
SEQRES 32 D 434 GLY THR GLY TYR PHE ASP LYS VAL THR THR ILE ILE GLN
SEQRES 33 D 434 GLY GLY THR SER SER VAL THR ALA LEU THR GLY SER THR
SEQRES 34 D 434 GLU GLU SER GLN PHE
HET HG A 435 1
HET HG A 436 1
HET HG A 437 1
HET HG A 438 1
HET HG A 439 1
HET MG A 441 1
HET PYR A1444 6
HET HG B 435 1
HET HG B 436 1
HET HG B 437 1
HET HG B 438 1
HET HG B 439 1
HET MG B 441 1
HET PYR B1445 6
HET HG C 435 1
HET HG C 436 1
HET HG C 437 1
HET HG C 438 1
HET HG C 439 1
HET HG C 440 1
HET MG C 441 1
HET PYR C1446 6
HET HG D 435 1
HET HG D 436 1
HET HG D 437 1
HET HG D 438 1
HET HG D 439 1
HET MG D 441 1
HET PYR D1447 6
HETNAM HG MERCURY (II) ION
HETNAM MG MAGNESIUM ION
HETNAM PYR PYRUVIC ACID
FORMUL 5 HG 21(HG 2+)
FORMUL 10 MG 4(MG 2+)
FORMUL 11 PYR 4(C3 H4 O3)
FORMUL 34 HOH *767(H2 O)
HELIX 1 1 THR A 3 TRP A 15 1 13
HELIX 2 2 THR A 16 GLU A 21 5 6
HELIX 3 3 SER A 28 LEU A 35 1 8
HELIX 4 4 CYS A 43 HIS A 58 1 16
HELIX 5 5 THR A 73 GLY A 84 1 12
HELIX 6 6 SER A 91 ALA A 99 1 9
HELIX 7 7 ASN A 115 ALA A 138 1 24
HELIX 8 8 GLY A 164 ALA A 178 1 15
HELIX 9 9 LEU A 189 LYS A 193 5 5
HELIX 10 10 PRO A 205 GLY A 224 1 20
HELIX 11 11 ASP A 246 GLU A 251 5 6
HELIX 12 12 GLY A 268 ALA A 280 1 13
HELIX 13 13 PRO A 281 ALA A 283 5 3
HELIX 14 14 ASP A 294 TYR A 309 1 16
HELIX 15 15 SER A 335 GLY A 344 1 10
HELIX 16 16 LEU A 352 GLY A 372 1 21
HELIX 17 17 GLU A 373 VAL A 382 1 10
HELIX 18 18 VAL A 382 LYS A 391 1 10
HELIX 19 19 SER A 398 VAL A 403 1 6
HELIX 20 20 GLY A 404 GLN A 416 1 13
HELIX 21 21 THR B 3 TRP B 15 1 13
HELIX 22 22 THR B 16 GLU B 21 5 6
HELIX 23 23 SER B 28 LEU B 35 1 8
HELIX 24 24 CYS B 43 HIS B 58 1 16
HELIX 25 25 THR B 73 ALA B 83 1 11
HELIX 26 26 SER B 91 ALA B 99 1 9
HELIX 27 27 ASN B 115 ALA B 138 1 24
HELIX 28 28 GLY B 164 GLY B 179 1 16
HELIX 29 29 LEU B 189 LYS B 193 5 5
HELIX 30 30 PRO B 205 GLY B 224 1 20
HELIX 31 31 ASP B 246 ILE B 253 5 8
HELIX 32 32 GLY B 268 ALA B 280 1 13
HELIX 33 33 PRO B 281 ALA B 283 5 3
HELIX 34 34 ASP B 294 TYR B 309 1 16
HELIX 35 35 ASP B 329 MET B 343 1 15
HELIX 36 36 LEU B 352 GLY B 372 1 21
HELIX 37 37 GLU B 373 VAL B 382 1 10
HELIX 38 38 VAL B 382 ALA B 390 1 9
HELIX 39 39 LYS B 391 GLY B 393 5 3
HELIX 40 40 SER B 398 VAL B 403 1 6
HELIX 41 41 TYR B 407 GLN B 416 1 10
HELIX 42 42 THR C 3 TRP C 15 1 13
HELIX 43 43 THR C 16 GLU C 21 5 6
HELIX 44 44 SER C 28 LYS C 34 1 7
HELIX 45 45 CYS C 43 HIS C 58 1 16
HELIX 46 46 THR C 73 GLY C 84 1 12
HELIX 47 47 SER C 91 ALA C 99 1 9
HELIX 48 48 ASN C 115 ALA C 138 1 24
HELIX 49 49 GLY C 164 GLY C 179 1 16
HELIX 50 50 LEU C 189 LYS C 193 5 5
HELIX 51 51 PRO C 205 GLY C 224 1 20
HELIX 52 52 ASP C 246 GLU C 251 5 6
HELIX 53 53 GLY C 268 ALA C 280 1 13
HELIX 54 54 PRO C 281 ALA C 283 5 3
HELIX 55 55 ASP C 294 TYR C 309 1 16
HELIX 56 56 ASN C 323 LEU C 328 1 6
HELIX 57 57 ASP C 329 MET C 343 1 15
HELIX 58 58 LEU C 352 ALA C 370 1 19
HELIX 59 59 GLU C 373 VAL C 382 1 10
HELIX 60 60 VAL C 382 ALA C 390 1 9
HELIX 61 61 LYS C 391 GLY C 393 5 3
HELIX 62 62 SER C 398 VAL C 403 1 6
HELIX 63 63 GLY C 404 GLN C 416 1 13
HELIX 64 64 THR D 3 THR D 16 1 14
HELIX 65 65 GLN D 17 GLU D 21 5 5
HELIX 66 66 SER D 28 LEU D 35 1 8
HELIX 67 67 CYS D 43 HIS D 58 1 16
HELIX 68 68 THR D 73 ALA D 83 1 11
HELIX 69 69 SER D 91 ALA D 99 1 9
HELIX 70 70 ASN D 115 ALA D 138 1 24
HELIX 71 71 GLY D 164 ALA D 178 1 15
HELIX 72 72 PRO D 205 GLY D 224 1 20
HELIX 73 73 ASP D 246 GLU D 251 5 6
HELIX 74 74 GLY D 268 ALA D 280 1 13
HELIX 75 75 PRO D 281 ALA D 283 5 3
HELIX 76 76 ASP D 294 TYR D 309 1 16
HELIX 77 77 ASP D 329 GLY D 344 1 16
HELIX 78 78 LEU D 352 GLY D 372 1 21
HELIX 79 79 GLU D 373 VAL D 382 1 10
HELIX 80 80 VAL D 382 LYS D 391 1 10
HELIX 81 81 SER D 398 VAL D 403 1 6
HELIX 82 82 GLY D 404 GLN D 416 1 13
SHEET 1 A 8 ILE A 66 LEU A 69 0
SHEET 2 A 8 TYR A 345 ILE A 350 1 O LYS A 346 N ILE A 66
SHEET 3 A 8 LEU A 313 ASN A 317 1 O LEU A 314 N PHE A 347
SHEET 4 A 8 LEU A 285 CYS A 288 1 O VAL A 286 N ALA A 315
SHEET 5 A 8 LEU A 228 THR A 233 1 O LEU A 229 N LEU A 285
SHEET 6 A 8 ALA A 182 GLU A 186 1 O VAL A 183 N VAL A 230
SHEET 7 A 8 ILE A 154 ASP A 157 1 O ILE A 154 N ALA A 182
SHEET 8 A 8 VAL A 88 LEU A 90 1 O VAL A 88 N VAL A 155
SHEET 1 B 4 VAL A 202 LEU A 203 0
SHEET 2 B 4 LEU A 240 ILE A 241 1 O LEU A 240 N LEU A 203
SHEET 3 B 4 PHE A 263 THR A 265 -1 N PHE A 263 O ILE A 241
SHEET 4 B 4 ILE A 253 ARG A 257 -1 N THR A 254 O ARG A 264
SHEET 1 C 8 ILE B 66 LEU B 69 0
SHEET 2 C 8 TYR B 345 ILE B 350 1 O LYS B 346 N ILE B 66
SHEET 3 C 8 LEU B 314 CYS B 318 1 O LEU B 314 N PHE B 347
SHEET 4 C 8 LEU B 285 CYS B 288 1 O VAL B 286 N ALA B 315
SHEET 5 C 8 LEU B 228 THR B 233 1 O LEU B 229 N LEU B 285
SHEET 6 C 8 ALA B 182 GLU B 186 1 O VAL B 183 N VAL B 230
SHEET 7 C 8 ILE B 154 ASP B 157 1 O ILE B 154 N ALA B 182
SHEET 8 C 8 VAL B 88 LEU B 90 1 O VAL B 88 N VAL B 155
SHEET 1 D 3 VAL B 202 LEU B 203 0
SHEET 2 D 3 LEU B 240 ILE B 241 1 O LEU B 240 N LEU B 203
SHEET 3 D 3 PHE B 263 ARG B 264 -1 N PHE B 263 O ILE B 241
SHEET 1 E 8 ILE C 66 LEU C 69 0
SHEET 2 E 8 TYR C 345 ILE C 350 1 O LYS C 346 N ILE C 66
SHEET 3 E 8 LEU C 314 CYS C 318 1 O LEU C 314 N PHE C 347
SHEET 4 E 8 LEU C 285 CYS C 288 1 O VAL C 286 N ALA C 315
SHEET 5 E 8 LEU C 228 THR C 233 1 O LEU C 229 N LEU C 285
SHEET 6 E 8 ALA C 182 GLU C 186 1 O VAL C 183 N VAL C 230
SHEET 7 E 8 ILE C 154 ASP C 157 1 O ILE C 154 N ALA C 182
SHEET 8 E 8 VAL C 88 LEU C 90 1 O VAL C 88 N VAL C 155
SHEET 1 F 4 VAL C 202 LEU C 203 0
SHEET 2 F 4 LEU C 240 ILE C 241 1 O LEU C 240 N LEU C 203
SHEET 3 F 4 PHE C 263 THR C 265 -1 N PHE C 263 O ILE C 241
SHEET 4 F 4 ILE C 253 ARG C 257 -1 N THR C 254 O ARG C 264
SHEET 1 G 8 ILE D 66 LEU D 69 0
SHEET 2 G 8 TYR D 345 ILE D 350 1 O LYS D 346 N ILE D 66
SHEET 3 G 8 LEU D 314 CYS D 318 1 O LEU D 314 N PHE D 347
SHEET 4 G 8 LEU D 285 CYS D 288 1 O VAL D 286 N ALA D 315
SHEET 5 G 8 LEU D 228 THR D 233 1 O LEU D 229 N LEU D 285
SHEET 6 G 8 ALA D 182 GLU D 186 1 N VAL D 183 O LEU D 228
SHEET 7 G 8 ILE D 154 ASP D 157 1 O ILE D 154 N ALA D 182
SHEET 8 G 8 VAL D 88 LEU D 90 1 O VAL D 88 N VAL D 155
SHEET 1 H 4 VAL D 202 LEU D 203 0
SHEET 2 H 4 LEU D 240 ILE D 241 1 O LEU D 240 N LEU D 203
SHEET 3 H 4 PHE D 263 THR D 265 -1 N PHE D 263 O ILE D 241
SHEET 4 H 4 ILE D 253 ARG D 257 -1 N THR D 254 O ARG D 264
LINK O GLU A 42 HG HG A 435 1555 1555 2.96
LINK SG CYS A 43 HG HG A 435 1555 1555 2.36
LINK OD2 ASP A 157 MG MG A 441 1555 1555 2.12
LINK O CYS A 219 HG HG A 436 1555 1555 3.33
LINK SG CYS A 219 HG HG A 436 1555 1555 2.25
LINK O CYS A 245 HG HG A 437 1555 1555 3.36
LINK SG CYS A 245 HG HG A 437 1555 1555 1.75
LINK N ASP A 246 HG HG A 437 1555 1555 3.52
LINK O CYS A 288 HG HG A 438 1555 1555 3.18
LINK SG CYS A 288 HG HG A 438 1555 1555 2.35
LINK SG CYS A 318 HG HG A 439 1555 1555 1.78
LINK HG HG A 435 O HOH A1600 1555 1555 2.67
LINK HG HG A 436 O HOH C1514 1555 1555 1.70
LINK HG HG A 436 O HOH C1571 1555 1555 2.96
LINK HG HG A 437 O HOH B1609 1555 1555 2.34
LINK HG HG A 438 O HOH A1561 1555 1555 2.36
LINK HG HG A 439 O HOH A1461 1555 1555 2.47
LINK HG HG A 439 O HOH A1507 1555 1555 2.48
LINK HG HG A 439 O HOH A1549 1555 1555 2.94
LINK HG HG A 439 O HOH A1599 1555 1555 3.38
LINK HG HG A 439 SD MET D 375 1555 1555 3.18
LINK MG MG A 441 O PYR A1444 1555 1555 2.00
LINK MG MG A 441 O3 PYR A1444 1555 1555 2.34
LINK MG MG A 441 O HOH A1630 1555 1555 1.96
LINK MG MG A 441 O HOH A1631 1555 1555 2.12
LINK MG MG A 441 O HOH A1632 1555 1555 2.19
LINK O HOH A1596 HG HG C 436 1555 1555 2.60
LINK O GLU B 42 HG HG B 435 1555 1555 2.90
LINK SG CYS B 43 HG HG B 435 1555 1555 2.32
LINK OD2 ASP B 157 MG MG B 441 1555 1555 2.14
LINK SG CYS B 219 HG HG B 436 1555 1555 2.06
LINK O CYS B 219 HG HG B 436 1555 1555 3.31
LINK SG CYS B 245 HG HG B 437 1555 1555 1.75
LINK O CYS B 245 HG HG B 437 1555 1555 3.41
LINK O CYS B 288 HG HG B 438 1555 1555 3.20
LINK SG CYS B 288 HG HG B 438 1555 1555 2.39
LINK N CYS B 318 HG HG B 439 1555 1555 3.36
LINK SG CYS B 318 HG HG B 439 1555 1555 2.24
LINK O PHE B 349 HG HG B 439 1555 1555 3.50
LINK HG HG B 435 O HOH B1509 1555 1555 1.56
LINK HG HG B 438 O HOH B1570 1555 1555 2.71
LINK HG HG B 439 O HOH B1453 1555 1555 3.52
LINK HG HG B 439 O HOH B1490 1555 1555 3.39
LINK HG HG B 439 O HOH B1512 1555 1555 2.36
LINK MG MG B 441 O PYR B1445 1555 1555 2.26
LINK MG MG B 441 O3 PYR B1445 1555 1555 2.16
LINK MG MG B 441 O HOH B1633 1555 1555 2.11
LINK MG MG B 441 O HOH B1634 1555 1555 2.17
LINK MG MG B 441 O HOH B1635 1555 1555 2.11
LINK O GLU C 42 HG HG C 435 1555 1555 3.04
LINK SG CYS C 43 HG HG C 435 1555 1555 2.54
LINK OD2 ASP C 157 MG MG C 441 1555 1555 2.14
LINK SG CYS C 195 HG HG C 440 1555 1555 2.39
LINK O CYS C 195 HG HG C 440 1555 1555 3.22
LINK SG CYS C 219 HG HG C 436 1555 1555 2.34
LINK O CYS C 219 HG HG C 436 1555 1555 3.25
LINK O CYS C 245 HG HG C 437 1555 1555 3.50
LINK SG CYS C 245 HG HG C 437 1555 1555 1.73
LINK SG CYS C 288 HG HG C 438 1555 1555 2.05
LINK O CYS C 288 HG HG C 438 1555 1555 3.22
LINK SG CYS C 318 HG HG C 439 1555 1555 2.28
LINK HG HG C 437 O HOH C1652 1555 1555 2.61
LINK HG HG C 439 O HOH C1510 1555 1555 2.78
LINK HG HG C 439 O HOH C1561 1555 1555 1.41
LINK MG MG C 441 O PYR C1446 1555 1555 1.98
LINK MG MG C 441 O3 PYR C1446 1555 1555 2.15
LINK MG MG C 441 O HOH C1694 1555 1555 2.25
LINK MG MG C 441 O HOH C1695 1555 1555 1.98
LINK MG MG C 441 O HOH C1696 1555 1555 2.06
LINK O HOH C1688 HG HG D 437 1555 1555 2.66
LINK O GLU D 42 HG HG D 435 1555 1555 2.95
LINK SG CYS D 43 HG HG D 435 1555 1555 2.30
LINK OD2 ASP D 157 MG MG D 441 1555 1555 2.11
LINK O CYS D 219 HG HG D 436 1555 1555 3.32
LINK SG CYS D 219 HG HG D 436 1555 1555 1.96
LINK O CYS D 245 HG HG D 437 1555 1555 3.32
LINK SG CYS D 245 HG HG D 437 1555 1555 1.86
LINK SG CYS D 288 HG HG D 438 1555 1555 2.40
LINK O CYS D 288 HG HG D 438 1555 1555 3.28
LINK N CYS D 318 HG HG D 439 1555 1555 3.14
LINK SG CYS D 318 HG HG D 439 1555 1555 3.09
LINK O PHE D 349 HG HG D 439 1555 1555 3.52
LINK HG HG D 439 O HOH D1562 1555 1555 2.81
LINK MG MG D 441 O3 PYR D1447 1555 1555 2.19
LINK MG MG D 441 O PYR D1447 1555 1555 1.99
LINK MG MG D 441 O HOH D1584 1555 1555 2.19
LINK MG MG D 441 O HOH D1585 1555 1555 2.18
LINK MG MG D 441 O HOH D1586 1555 1555 2.08
CISPEP 1 SER B 319 PRO B 320 0 0.33
CISPEP 2 SER C 319 PRO C 320 0 -1.57
CISPEP 3 SER D 319 PRO D 320 0 -0.19
SITE 1 AC1 4 GLU A 42 CYS A 43 HOH A1445 HOH A1600
SITE 1 AC2 5 LYS A 173 CYS A 219 THR A 223 HOH C1514
SITE 2 AC2 5 HOH C1571
SITE 1 AC3 3 CYS A 245 ASP A 246 HOH B1609
SITE 1 AC4 3 CYS A 288 THR A 290 HOH A1561
SITE 1 AC5 5 CYS A 318 HOH A1461 HOH A1507 HOH A1549
SITE 2 AC5 5 MET D 375
SITE 1 AC6 3 GLU B 42 CYS B 43 HOH B1509
SITE 1 AC7 2 CYS B 219 THR B 223
SITE 1 AC8 1 CYS B 245
SITE 1 AC9 3 CYS B 288 THR B 290 HOH B1570
SITE 1 BC1 4 CYS B 318 PHE B 349 HOH B1512 MET C 375
SITE 1 BC2 2 GLU C 42 CYS C 43
SITE 1 BC3 3 HOH A1596 CYS C 219 THR C 223
SITE 1 BC4 4 CYS C 245 ASP C 246 HOH C1652 GLU D 260
SITE 1 BC5 4 CYS C 288 THR C 290 HOH C1516 HOH C1640
SITE 1 BC6 5 MET B 375 CYS C 318 PHE C 349 HOH C1510
SITE 2 BC6 5 HOH C1561
SITE 1 BC7 2 CYS C 195 HIS C 197
SITE 1 BC8 2 GLU D 42 CYS D 43
SITE 1 BC9 3 LYS D 173 CYS D 219 THR D 223
SITE 1 CC1 4 GLU C 260 HOH C1688 CYS D 245 ASP D 246
SITE 1 CC2 2 CYS D 288 THR D 290
SITE 1 CC3 4 CYS D 318 GLN D 337 PHE D 349 HOH D1562
SITE 1 CC4 5 ASP A 157 PYR A1444 HOH A1630 HOH A1631
SITE 2 CC4 5 HOH A1632
SITE 1 CC5 5 ASP B 157 PYR B1445 HOH B1633 HOH B1634
SITE 2 CC5 5 HOH B1635
SITE 1 CC6 5 ASP C 157 PYR C1446 HOH C1694 HOH C1695
SITE 2 CC6 5 HOH C1696
SITE 1 CC7 5 ASP D 157 PYR D1447 HOH D1584 HOH D1585
SITE 2 CC7 5 HOH D1586
SITE 1 CC8 13 TYR A 89 SER A 91 GLY A 92 TRP A 93
SITE 2 CC8 13 ASP A 157 HIS A 184 ARG A 232 THR A 351
SITE 3 CC8 13 MG A 441 HOH A1570 HOH A1630 HOH A1631
SITE 4 CC8 13 HOH A1632
SITE 1 CC9 11 TYR B 89 SER B 91 GLY B 92 TRP B 93
SITE 2 CC9 11 ASP B 157 HIS B 184 ARG B 232 THR B 351
SITE 3 CC9 11 MG B 441 HOH B1633 HOH B1635
SITE 1 DC1 13 TYR C 89 SER C 91 GLY C 92 TRP C 93
SITE 2 DC1 13 ASP C 157 HIS C 184 ARG C 232 THR C 351
SITE 3 DC1 13 MG C 441 HOH C1552 HOH C1635 HOH C1695
SITE 4 DC1 13 HOH C1696
SITE 1 DC2 13 TYR D 89 SER D 91 GLY D 92 TRP D 93
SITE 2 DC2 13 ASP D 157 HIS D 184 ARG D 232 THR D 351
SITE 3 DC2 13 MG D 441 HOH D1552 HOH D1584 HOH D1585
SITE 4 DC2 13 HOH D1586
CRYST1 88.650 88.650 199.400 90.00 90.00 120.00 P 32 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 0.011280 0.006510 0.000000 0.00000
SCALE2 0.000000 0.013030 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005020 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
