HEADER HYDROLASE 01-AUG-11 3T81
TITLE CRYSTAL STRUCTURE OF DIIRON ADENINE DEAMINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENINE DEAMINASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADENASE 2, ADENINE AMINASE 2;
COMPND 5 EC: 3.5.4.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 STRAIN: C58;
SOURCE 5 GENE: ADE2, ADEC, AGR_L_883, ATU4426;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSGX3(BC)
KEYWDS PSI-2, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK
KEYWDS 2 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC,
KEYWDS 3 AMIDOHYDROLASE, NUCLEOTIDE BINDING, HYDROLASE, TIM BARREL,
KEYWDS 4 ALPHA/BETA, ADENINE DEAMINASE, ADENINE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 4 06-DEC-23 3T81 1 REMARK
REVDAT 3 13-SEP-23 3T81 1 REMARK
REVDAT 2 10-FEB-21 3T81 1 AUTHOR JRNL REMARK SEQADV
REVDAT 2 2 1 LINK
REVDAT 1 02-NOV-11 3T81 0
JRNL AUTH A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF DIIRON ADENINE DEAMINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.63 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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 31123
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 + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1663
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2259
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.4200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8614
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
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): 0.406
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.102
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8774 ; 0.042 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11938 ; 3.225 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1162 ;10.382 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 352 ;39.319 ;23.409
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1373 ;21.722 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 71 ;21.843 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1392 ; 0.197 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6653 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4472 ; 0.287 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5917 ; 0.347 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 411 ; 0.200 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.219 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 100 ; 0.267 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.102 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5990 ; 1.838 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9190 ; 2.606 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3242 ; 4.821 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2748 ; 6.696 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS, THE SELENOMETS ARE DISODERED
REMARK 4
REMARK 4 3T81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI III
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32849
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
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: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3NQB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1M HEPES 7.5, 25% (W/V) PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 65.92250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A -2
REMARK 465 SER A -1
REMARK 465 LEU A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 GLN A 4
REMARK 465 ILE A 5
REMARK 465 ARG A 6
REMARK 465 LEU A 7
REMARK 465 ALA A 8
REMARK 465 LEU A 596
REMARK 465 GLY A 597
REMARK 465 GLU A 598
REMARK 465 GLY A 599
REMARK 465 HIS A 600
REMARK 465 HIS A 601
REMARK 465 HIS A 602
REMARK 465 HIS A 603
REMARK 465 HIS A 604
REMARK 465 HIS A 605
REMARK 465 MSE B -2
REMARK 465 SER B -1
REMARK 465 LEU B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 GLN B 4
REMARK 465 ILE B 5
REMARK 465 ARG B 6
REMARK 465 LEU B 7
REMARK 465 GLY B 406
REMARK 465 ALA B 407
REMARK 465 LYS B 408
REMARK 465 VAL B 409
REMARK 465 ARG B 410
REMARK 465 LEU B 411
REMARK 465 ALA B 412
REMARK 465 GLU B 424
REMARK 465 VAL B 595
REMARK 465 LEU B 596
REMARK 465 GLY B 597
REMARK 465 GLU B 598
REMARK 465 GLY B 599
REMARK 465 HIS B 600
REMARK 465 HIS B 601
REMARK 465 HIS B 602
REMARK 465 HIS B 603
REMARK 465 HIS B 604
REMARK 465 HIS B 605
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 187 FE FE B 608 1.55
REMARK 500 CE MSE A 588 O SER A 590 2.09
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 GLU A 66 CG GLU A 66 CD 0.117
REMARK 500 GLU A 66 CD GLU A 66 OE2 0.073
REMARK 500 GLY A 80 C GLY A 80 O 0.121
REMARK 500 ALA A 82 CA ALA A 82 CB 0.128
REMARK 500 SER A 98 CB SER A 98 OG -0.083
REMARK 500 VAL A 130 CB VAL A 130 CG1 0.128
REMARK 500 GLU A 141 CG GLU A 141 CD 0.097
REMARK 500 MSE A 189 SE MSE A 189 CE 0.558
REMARK 500 MSE A 201 CG MSE A 201 SE 0.214
REMARK 500 PHE A 230 CD1 PHE A 230 CE1 0.123
REMARK 500 GLU A 245 CD GLU A 245 OE1 0.070
REMARK 500 ASP A 246 CB ASP A 246 CG 0.150
REMARK 500 PHE A 270 CE1 PHE A 270 CZ 0.129
REMARK 500 PHE A 270 CE2 PHE A 270 CD2 0.121
REMARK 500 TYR A 312 CE2 TYR A 312 CD2 0.113
REMARK 500 TRP A 318 CZ3 TRP A 318 CH2 0.105
REMARK 500 LEU A 336 C LEU A 336 O 0.122
REMARK 500 GLU A 351 CB GLU A 351 CG 0.116
REMARK 500 ALA A 358 CA ALA A 358 CB 0.143
REMARK 500 MSE A 451 SE MSE A 451 CE 0.594
REMARK 500 PHE A 460 CZ PHE A 460 CE2 0.157
REMARK 500 LYS A 513 CB LYS A 513 CG 0.175
REMARK 500 GLU A 533 CD GLU A 533 OE1 0.090
REMARK 500 ARG A 536 CG ARG A 536 CD 0.165
REMARK 500 GLU A 543 CG GLU A 543 CD 0.112
REMARK 500 GLU A 543 CD GLU A 543 OE1 0.067
REMARK 500 ASP A 581 CB ASP A 581 CG 0.164
REMARK 500 GLU A 589 CB GLU A 589 CG 0.121
REMARK 500 ALA B 24 C ALA B 24 O 0.125
REMARK 500 ALA B 25 CA ALA B 25 CB -0.144
REMARK 500 VAL B 42 CB VAL B 42 CG2 -0.138
REMARK 500 ALA B 52 CA ALA B 52 CB -0.135
REMARK 500 ARG B 70 CZ ARG B 70 NH2 0.082
REMARK 500 THR B 101 CA THR B 101 CB 0.165
REMARK 500 TRP B 119 CE3 TRP B 119 CZ3 0.130
REMARK 500 VAL B 133 CB VAL B 133 CG2 -0.176
REMARK 500 PHE B 168 CD1 PHE B 168 CE1 0.136
REMARK 500 SER B 202 C SER B 202 O -0.126
REMARK 500 CYS B 216 CA CYS B 216 CB -0.089
REMARK 500 ARG B 220 CB ARG B 220 CG 0.165
REMARK 500 GLN B 298 CG GLN B 298 CD 0.152
REMARK 500 ARG B 311 CZ ARG B 311 NH1 0.084
REMARK 500 ILE B 347 CA ILE B 347 CB -0.164
REMARK 500 GLU B 351 CG GLU B 351 CD 0.099
REMARK 500 CYS B 381 CB CYS B 381 SG -0.117
REMARK 500 MSE B 396 SE MSE B 396 CE 0.444
REMARK 500 VAL B 435 CB VAL B 435 CG1 0.141
REMARK 500 MSE B 442 SE MSE B 442 CE 0.371
REMARK 500 ARG B 448 CZ ARG B 448 NH1 0.111
REMARK 500 MSE B 451 SE MSE B 451 CE 0.361
REMARK 500
REMARK 500 THIS ENTRY HAS 56 BOND DEVIATIONS.
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 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP A 33 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 LEU A 49 CA - CB - CG ANGL. DEV. = -17.6 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 53 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ILE A 61 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 72 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 78 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP A 120 CB - CG - OD1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 PRO A 144 C - N - CA ANGL. DEV. = -12.4 DEGREES
REMARK 500 PRO A 144 C - N - CD ANGL. DEV. = 13.0 DEGREES
REMARK 500 LEU A 145 CB - CG - CD2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 LEU A 149 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASP A 175 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ILE A 195 CG1 - CB - CG2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 238 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 238 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU A 241 CB - CG - CD1 ANGL. DEV. = -19.2 DEGREES
REMARK 500 ASP A 246 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU A 247 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU A 255 CB - CG - CD1 ANGL. DEV. = -12.9 DEGREES
REMARK 500 LEU A 259 CB - CG - CD1 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP A 289 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 289 CB - CG - OD2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 LEU A 302 CA - CB - CG ANGL. DEV. = -17.9 DEGREES
REMARK 500 ARG A 308 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 308 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 333 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 VAL A 349 CB - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 373 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 377 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 LEU A 392 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 399 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 399 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 LEU A 411 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 448 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LEU A 461 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 LEU A 461 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 MSE A 492 CG - SE - CE ANGL. DEV. = 14.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 98 ANGLE DEVIATIONS.
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 ALA A 68 -20.15 57.66
REMARK 500 SER A 69 -8.07 -46.11
REMARK 500 ALA A 73 121.24 -174.22
REMARK 500 ALA A 74 1.56 -57.35
REMARK 500 HIS A 92 116.78 -167.29
REMARK 500 MSE A 99 30.19 75.98
REMARK 500 ALA A 111 -18.32 -31.40
REMARK 500 PRO A 121 46.17 -90.63
REMARK 500 ASN A 224 -103.29 36.43
REMARK 500 ASP A 289 -103.26 49.87
REMARK 500 THR A 324 -86.85 -127.69
REMARK 500 LEU A 336 -168.46 -113.80
REMARK 500 ASP A 382 105.07 -50.74
REMARK 500 LYS A 391 62.46 -116.96
REMARK 500 LEU A 394 143.72 -37.15
REMARK 500 ALA A 397 -69.85 -1.88
REMARK 500 LYS A 403 118.83 -35.20
REMARK 500 ARG A 416 120.47 85.83
REMARK 500 ARG A 418 -65.42 81.07
REMARK 500 LYS A 430 97.06 166.62
REMARK 500 ASP A 431 30.51 98.67
REMARK 500 HIS A 447 108.58 -45.76
REMARK 500 ALA A 452 152.82 172.08
REMARK 500 PRO A 454 34.06 -57.67
REMARK 500 SER A 476 95.76 -162.87
REMARK 500 HIS A 480 44.76 37.64
REMARK 500 ALA A 489 -51.46 -24.01
REMARK 500 ALA A 516 130.60 163.64
REMARK 500 SER A 523 -3.97 62.76
REMARK 500 GLU A 543 -72.33 -56.96
REMARK 500 ALA A 544 -65.54 -28.30
REMARK 500 PRO A 553 164.05 -37.48
REMARK 500 TYR A 555 -51.85 76.59
REMARK 500 LEU A 556 55.87 -108.30
REMARK 500 ILE A 570 128.85 -35.28
REMARK 500 ASP A 576 8.48 -64.30
REMARK 500 MSE A 588 85.71 -46.11
REMARK 500 ALA B 68 7.17 84.99
REMARK 500 ASP B 72 -137.43 -26.92
REMARK 500 ALA B 73 -129.97 104.37
REMARK 500 ALA B 74 -63.17 136.70
REMARK 500 HIS B 92 115.63 -164.57
REMARK 500 PRO B 121 37.77 -92.45
REMARK 500 ALA B 136 -65.93 -27.24
REMARK 500 ALA B 151 109.04 -42.40
REMARK 500 PRO B 152 108.77 -48.55
REMARK 500 LEU B 177 2.07 -55.69
REMARK 500 GLU B 187 103.23 -20.87
REMARK 500 ASN B 224 -119.35 29.32
REMARK 500 GLU B 258 72.41 -100.49
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 48 LEU A 49 144.96
REMARK 500 GLY A 217 HIS A 218 149.38
REMARK 500 MSE A 396 ALA A 397 149.02
REMARK 500 VAL A 402 LYS A 403 149.53
REMARK 500 MSE A 451 ALA A 452 -144.08
REMARK 500 GLY B 160 LEU B 161 147.98
REMARK 500 GLY B 299 GLY B 300 -59.62
REMARK 500 GLY B 365 ARG B 366 -128.95
REMARK 500 ALA B 397 ASN B 398 143.81
REMARK 500 THR B 413 ILE B 414 -149.39
REMARK 500 GLU B 426 ALA B 427 142.12
REMARK 500 GLY B 465 ARG B 466 149.97
REMARK 500 ALA B 489 GLY B 490 -149.73
REMARK 500 ILE B 579 ALA B 580 -146.81
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 FE A 607 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 92 NE2
REMARK 620 2 HIS A 94 NE2 95.1
REMARK 620 3 GLU A 187 OE2 85.0 83.6
REMARK 620 4 ASP A 289 OD1 83.2 87.9 164.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 608 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 122 NE2
REMARK 620 2 GLU A 123 OE1 91.8
REMARK 620 3 GLU A 123 OE2 87.5 58.3
REMARK 620 4 HIS A 477 ND1 168.4 82.5 98.0
REMARK 620 5 ASP A 478 OD1 87.5 92.9 150.5 82.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 606 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 187 OE1
REMARK 620 2 HIS A 218 ND1 85.3
REMARK 620 3 HIS A 239 NE2 83.0 119.5
REMARK 620 4 GLU A 240 OE2 172.5 92.4 91.9
REMARK 620 5 HOH A 630 O 98.8 95.1 145.3 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 606 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HIS B 94 NE2 103.0
REMARK 620 3 ASP B 289 OD1 91.0 93.6
REMARK 620 4 HOH B 635 O 115.3 141.4 82.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 607 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 122 NE2
REMARK 620 2 GLU B 123 OE2 56.2
REMARK 620 3 GLU B 123 OE1 96.0 54.7
REMARK 620 4 HIS B 477 ND1 173.1 118.8 83.3
REMARK 620 5 ASP B 478 OD1 94.8 144.1 116.8 91.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 608 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 218 ND1
REMARK 620 2 HIS B 239 NE2 111.2
REMARK 620 3 GLU B 240 OE2 73.1 101.6
REMARK 620 4 HOH B 635 O 166.3 82.2 101.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 608
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NQB RELATED DB: PDB
REMARK 900 NATIVE FORM
REMARK 900 RELATED ID: NYSGXRC-9206A RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3T8L RELATED DB: PDB
DBREF 3T81 A 1 597 UNP Q7CUX4 ADEC2_AGRT5 1 597
DBREF 3T81 B 1 597 UNP Q7CUX4 ADEC2_AGRT5 1 597
SEQADV 3T81 MSE A -2 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 SER A -1 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 LEU A 0 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 GLU A 598 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 GLY A 599 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 600 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 601 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 602 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 603 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 604 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS A 605 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 MSE B -2 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 SER B -1 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 LEU B 0 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 GLU B 598 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 GLY B 599 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 600 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 601 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 602 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 603 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 604 UNP Q7CUX4 EXPRESSION TAG
SEQADV 3T81 HIS B 605 UNP Q7CUX4 EXPRESSION TAG
SEQRES 1 A 608 MSE SER LEU MSE THR ALA GLN ILE ARG LEU ALA GLU PRO
SEQRES 2 A 608 ALA ASP LEU ASN ASP ASP THR LEU ARG ALA ARG ALA VAL
SEQRES 3 A 608 ALA ALA ALA ARG GLY ASP GLN ARG PHE ASP VAL LEU ILE
SEQRES 4 A 608 THR GLY GLY THR LEU VAL ASP VAL VAL THR GLY GLU LEU
SEQRES 5 A 608 ARG PRO ALA ASP ILE GLY ILE VAL GLY ALA LEU ILE ALA
SEQRES 6 A 608 SER VAL HIS GLU PRO ALA SER ARG ARG ASP ALA ALA GLN
SEQRES 7 A 608 VAL ILE ASP ALA GLY GLY ALA TYR VAL SER PRO GLY LEU
SEQRES 8 A 608 ILE ASP THR HIS MSE HIS ILE GLU SER SER MSE ILE THR
SEQRES 9 A 608 PRO ALA ALA TYR ALA ALA ALA VAL VAL ALA ARG GLY VAL
SEQRES 10 A 608 THR THR ILE VAL TRP ASP PRO HIS GLU PHE GLY ASN VAL
SEQRES 11 A 608 HIS GLY VAL ASP GLY VAL ARG TRP ALA ALA LYS ALA ILE
SEQRES 12 A 608 GLU ASN LEU PRO LEU ARG ALA ILE LEU LEU ALA PRO SER
SEQRES 13 A 608 CYS VAL PRO SER ALA PRO GLY LEU GLU ARG GLY GLY ALA
SEQRES 14 A 608 ASP PHE ASP ALA ALA ILE LEU ALA ASP LEU LEU SER TRP
SEQRES 15 A 608 PRO GLU ILE GLY GLY ILE ALA GLU ILE MSE ASN MSE ARG
SEQRES 16 A 608 GLY VAL ILE GLU ARG ASP PRO ARG MSE SER GLY ILE VAL
SEQRES 17 A 608 GLN ALA GLY LEU ALA ALA GLU LYS LEU VAL CYS GLY HIS
SEQRES 18 A 608 ALA ARG GLY LEU LYS ASN ALA ASP LEU ASN ALA PHE MSE
SEQRES 19 A 608 ALA ALA GLY VAL SER SER ASP HIS GLU LEU VAL SER GLY
SEQRES 20 A 608 GLU ASP LEU MSE ALA LYS LEU ARG ALA GLY LEU THR ILE
SEQRES 21 A 608 GLU LEU ARG GLY SER HIS ASP HIS LEU LEU PRO GLU PHE
SEQRES 22 A 608 VAL ALA ALA LEU ASN THR LEU GLY HIS LEU PRO GLN THR
SEQRES 23 A 608 VAL THR LEU CYS THR ASP ASP VAL PHE PRO ASP ASP LEU
SEQRES 24 A 608 LEU GLN GLY GLY GLY LEU ASP ASP VAL VAL ARG ARG LEU
SEQRES 25 A 608 VAL ARG TYR GLY LEU LYS PRO GLU TRP ALA LEU ARG ALA
SEQRES 26 A 608 ALA THR LEU ASN ALA ALA GLN ARG LEU GLY ARG SER ASP
SEQRES 27 A 608 LEU GLY LEU ILE ALA ALA GLY ARG ARG ALA ASP ILE VAL
SEQRES 28 A 608 VAL PHE GLU ASP LEU ASN GLY PHE SER ALA ARG HIS VAL
SEQRES 29 A 608 LEU ALA SER GLY ARG ALA VAL ALA GLU GLY GLY ARG MSE
SEQRES 30 A 608 LEU VAL ASP ILE PRO THR CYS ASP THR THR VAL LEU LYS
SEQRES 31 A 608 GLY SER MSE LYS LEU PRO LEU ARG MSE ALA ASN ASP PHE
SEQRES 32 A 608 LEU VAL LYS SER GLN GLY ALA LYS VAL ARG LEU ALA THR
SEQRES 33 A 608 ILE ASP ARG PRO ARG PHE THR GLN TRP GLY GLU THR GLU
SEQRES 34 A 608 ALA ASP VAL LYS ASP GLY PHE VAL VAL PRO PRO GLU GLY
SEQRES 35 A 608 ALA THR MSE ILE SER VAL THR HIS ARG HIS GLY MSE ALA
SEQRES 36 A 608 GLU PRO THR THR LYS THR GLY PHE LEU THR GLY TRP GLY
SEQRES 37 A 608 ARG TRP ASN GLY ALA PHE ALA THR THR VAL SER HIS ASP
SEQRES 38 A 608 SER HIS ASN LEU THR VAL PHE GLY GLY ASN ALA GLY ASP
SEQRES 39 A 608 MSE ALA LEU ALA ALA ASN ALA VAL ILE GLY THR GLY GLY
SEQRES 40 A 608 GLY MSE ALA VAL ALA SER GLU GLY LYS VAL THR ALA ILE
SEQRES 41 A 608 LEU PRO LEU PRO LEU SER GLY LEU VAL SER ASP ALA PRO
SEQRES 42 A 608 LEU GLU GLU VAL ALA ARG ALA PHE GLU ASP LEU ARG GLU
SEQRES 43 A 608 ALA VAL GLY LYS VAL VAL GLU TRP GLN PRO PRO TYR LEU
SEQRES 44 A 608 VAL PHE LYS ALA CYS PHE GLY ALA THR LEU ALA CYS ASN
SEQRES 45 A 608 ILE GLY PRO HIS GLN THR ASP MSE GLY ILE ALA ASP VAL
SEQRES 46 A 608 LEU THR GLY LYS VAL MSE GLU SER PRO VAL ILE GLU VAL
SEQRES 47 A 608 LEU GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 608 MSE SER LEU MSE THR ALA GLN ILE ARG LEU ALA GLU PRO
SEQRES 2 B 608 ALA ASP LEU ASN ASP ASP THR LEU ARG ALA ARG ALA VAL
SEQRES 3 B 608 ALA ALA ALA ARG GLY ASP GLN ARG PHE ASP VAL LEU ILE
SEQRES 4 B 608 THR GLY GLY THR LEU VAL ASP VAL VAL THR GLY GLU LEU
SEQRES 5 B 608 ARG PRO ALA ASP ILE GLY ILE VAL GLY ALA LEU ILE ALA
SEQRES 6 B 608 SER VAL HIS GLU PRO ALA SER ARG ARG ASP ALA ALA GLN
SEQRES 7 B 608 VAL ILE ASP ALA GLY GLY ALA TYR VAL SER PRO GLY LEU
SEQRES 8 B 608 ILE ASP THR HIS MSE HIS ILE GLU SER SER MSE ILE THR
SEQRES 9 B 608 PRO ALA ALA TYR ALA ALA ALA VAL VAL ALA ARG GLY VAL
SEQRES 10 B 608 THR THR ILE VAL TRP ASP PRO HIS GLU PHE GLY ASN VAL
SEQRES 11 B 608 HIS GLY VAL ASP GLY VAL ARG TRP ALA ALA LYS ALA ILE
SEQRES 12 B 608 GLU ASN LEU PRO LEU ARG ALA ILE LEU LEU ALA PRO SER
SEQRES 13 B 608 CYS VAL PRO SER ALA PRO GLY LEU GLU ARG GLY GLY ALA
SEQRES 14 B 608 ASP PHE ASP ALA ALA ILE LEU ALA ASP LEU LEU SER TRP
SEQRES 15 B 608 PRO GLU ILE GLY GLY ILE ALA GLU ILE MSE ASN MSE ARG
SEQRES 16 B 608 GLY VAL ILE GLU ARG ASP PRO ARG MSE SER GLY ILE VAL
SEQRES 17 B 608 GLN ALA GLY LEU ALA ALA GLU LYS LEU VAL CYS GLY HIS
SEQRES 18 B 608 ALA ARG GLY LEU LYS ASN ALA ASP LEU ASN ALA PHE MSE
SEQRES 19 B 608 ALA ALA GLY VAL SER SER ASP HIS GLU LEU VAL SER GLY
SEQRES 20 B 608 GLU ASP LEU MSE ALA LYS LEU ARG ALA GLY LEU THR ILE
SEQRES 21 B 608 GLU LEU ARG GLY SER HIS ASP HIS LEU LEU PRO GLU PHE
SEQRES 22 B 608 VAL ALA ALA LEU ASN THR LEU GLY HIS LEU PRO GLN THR
SEQRES 23 B 608 VAL THR LEU CYS THR ASP ASP VAL PHE PRO ASP ASP LEU
SEQRES 24 B 608 LEU GLN GLY GLY GLY LEU ASP ASP VAL VAL ARG ARG LEU
SEQRES 25 B 608 VAL ARG TYR GLY LEU LYS PRO GLU TRP ALA LEU ARG ALA
SEQRES 26 B 608 ALA THR LEU ASN ALA ALA GLN ARG LEU GLY ARG SER ASP
SEQRES 27 B 608 LEU GLY LEU ILE ALA ALA GLY ARG ARG ALA ASP ILE VAL
SEQRES 28 B 608 VAL PHE GLU ASP LEU ASN GLY PHE SER ALA ARG HIS VAL
SEQRES 29 B 608 LEU ALA SER GLY ARG ALA VAL ALA GLU GLY GLY ARG MSE
SEQRES 30 B 608 LEU VAL ASP ILE PRO THR CYS ASP THR THR VAL LEU LYS
SEQRES 31 B 608 GLY SER MSE LYS LEU PRO LEU ARG MSE ALA ASN ASP PHE
SEQRES 32 B 608 LEU VAL LYS SER GLN GLY ALA LYS VAL ARG LEU ALA THR
SEQRES 33 B 608 ILE ASP ARG PRO ARG PHE THR GLN TRP GLY GLU THR GLU
SEQRES 34 B 608 ALA ASP VAL LYS ASP GLY PHE VAL VAL PRO PRO GLU GLY
SEQRES 35 B 608 ALA THR MSE ILE SER VAL THR HIS ARG HIS GLY MSE ALA
SEQRES 36 B 608 GLU PRO THR THR LYS THR GLY PHE LEU THR GLY TRP GLY
SEQRES 37 B 608 ARG TRP ASN GLY ALA PHE ALA THR THR VAL SER HIS ASP
SEQRES 38 B 608 SER HIS ASN LEU THR VAL PHE GLY GLY ASN ALA GLY ASP
SEQRES 39 B 608 MSE ALA LEU ALA ALA ASN ALA VAL ILE GLY THR GLY GLY
SEQRES 40 B 608 GLY MSE ALA VAL ALA SER GLU GLY LYS VAL THR ALA ILE
SEQRES 41 B 608 LEU PRO LEU PRO LEU SER GLY LEU VAL SER ASP ALA PRO
SEQRES 42 B 608 LEU GLU GLU VAL ALA ARG ALA PHE GLU ASP LEU ARG GLU
SEQRES 43 B 608 ALA VAL GLY LYS VAL VAL GLU TRP GLN PRO PRO TYR LEU
SEQRES 44 B 608 VAL PHE LYS ALA CYS PHE GLY ALA THR LEU ALA CYS ASN
SEQRES 45 B 608 ILE GLY PRO HIS GLN THR ASP MSE GLY ILE ALA ASP VAL
SEQRES 46 B 608 LEU THR GLY LYS VAL MSE GLU SER PRO VAL ILE GLU VAL
SEQRES 47 B 608 LEU GLY GLU GLY HIS HIS HIS HIS HIS HIS
MODRES 3T81 MSE A 93 MET SELENOMETHIONINE
MODRES 3T81 MSE A 99 MET SELENOMETHIONINE
MODRES 3T81 MSE A 189 MET SELENOMETHIONINE
MODRES 3T81 MSE A 191 MET SELENOMETHIONINE
MODRES 3T81 MSE A 201 MET SELENOMETHIONINE
MODRES 3T81 MSE A 231 MET SELENOMETHIONINE
MODRES 3T81 MSE A 248 MET SELENOMETHIONINE
MODRES 3T81 MSE A 374 MET SELENOMETHIONINE
MODRES 3T81 MSE A 390 MET SELENOMETHIONINE
MODRES 3T81 MSE A 396 MET SELENOMETHIONINE
MODRES 3T81 MSE A 442 MET SELENOMETHIONINE
MODRES 3T81 MSE A 451 MET SELENOMETHIONINE
MODRES 3T81 MSE A 492 MET SELENOMETHIONINE
MODRES 3T81 MSE A 506 MET SELENOMETHIONINE
MODRES 3T81 MSE A 577 MET SELENOMETHIONINE
MODRES 3T81 MSE A 588 MET SELENOMETHIONINE
MODRES 3T81 MSE B 93 MET SELENOMETHIONINE
MODRES 3T81 MSE B 99 MET SELENOMETHIONINE
MODRES 3T81 MSE B 189 MET SELENOMETHIONINE
MODRES 3T81 MSE B 191 MET SELENOMETHIONINE
MODRES 3T81 MSE B 201 MET SELENOMETHIONINE
MODRES 3T81 MSE B 231 MET SELENOMETHIONINE
MODRES 3T81 MSE B 248 MET SELENOMETHIONINE
MODRES 3T81 MSE B 374 MET SELENOMETHIONINE
MODRES 3T81 MSE B 390 MET SELENOMETHIONINE
MODRES 3T81 MSE B 396 MET SELENOMETHIONINE
MODRES 3T81 MSE B 442 MET SELENOMETHIONINE
MODRES 3T81 MSE B 451 MET SELENOMETHIONINE
MODRES 3T81 MSE B 492 MET SELENOMETHIONINE
MODRES 3T81 MSE B 506 MET SELENOMETHIONINE
MODRES 3T81 MSE B 577 MET SELENOMETHIONINE
MODRES 3T81 MSE B 588 MET SELENOMETHIONINE
HET MSE A 93 8
HET MSE A 99 8
HET MSE A 189 8
HET MSE A 191 8
HET MSE A 201 8
HET MSE A 231 8
HET MSE A 248 8
HET MSE A 374 8
HET MSE A 390 8
HET MSE A 396 8
HET MSE A 442 8
HET MSE A 451 8
HET MSE A 492 8
HET MSE A 506 8
HET MSE A 577 8
HET MSE A 588 8
HET MSE B 93 8
HET MSE B 99 8
HET MSE B 189 8
HET MSE B 191 8
HET MSE B 201 8
HET MSE B 231 8
HET MSE B 248 8
HET MSE B 374 8
HET MSE B 390 8
HET MSE B 396 8
HET MSE B 442 8
HET MSE B 451 8
HET MSE B 492 8
HET MSE B 506 8
HET MSE B 577 8
HET MSE B 588 8
HET FE A 606 1
HET FE A 607 1
HET FE A 608 1
HET FE B 606 1
HET FE B 607 1
HET FE B 608 1
HETNAM MSE SELENOMETHIONINE
HETNAM FE FE (III) ION
FORMUL 1 MSE 32(C5 H11 N O2 SE)
FORMUL 3 FE 6(FE 3+)
FORMUL 9 HOH *54(H2 O)
HELIX 1 1 PRO A 10 ASN A 14 5 5
HELIX 2 2 ASP A 15 GLY A 28 1 14
HELIX 3 3 HIS A 94 MSE A 99 5 6
HELIX 4 4 THR A 101 ALA A 111 1 11
HELIX 5 5 PRO A 121 GLY A 129 1 9
HELIX 6 6 GLY A 129 GLU A 141 1 13
HELIX 7 7 ASP A 169 TRP A 179 1 11
HELIX 8 8 ASN A 190 GLU A 196 1 7
HELIX 9 9 ASP A 198 ALA A 211 1 14
HELIX 10 10 LYS A 223 GLY A 234 1 12
HELIX 11 11 SER A 243 ALA A 253 1 11
HELIX 12 12 LEU A 266 GLY A 278 1 13
HELIX 13 13 PHE A 292 GLY A 299 1 8
HELIX 14 14 GLY A 301 TYR A 312 1 12
HELIX 15 15 LYS A 315 THR A 324 1 10
HELIX 16 16 THR A 324 LEU A 331 1 8
HELIX 17 17 THR A 383 LYS A 387 5 5
HELIX 18 18 MSE A 396 LEU A 401 5 6
HELIX 19 19 ASN A 488 THR A 502 1 15
HELIX 20 20 PRO A 530 LYS A 547 1 18
HELIX 21 21 VAL A 557 GLY A 563 5 7
HELIX 22 22 PRO B 10 ASN B 14 5 5
HELIX 23 23 ASP B 15 GLY B 28 1 14
HELIX 24 24 HIS B 94 MSE B 99 5 6
HELIX 25 25 THR B 101 ALA B 111 1 11
HELIX 26 26 PRO B 121 GLY B 129 1 9
HELIX 27 27 GLY B 129 GLU B 141 1 13
HELIX 28 28 ASP B 169 LEU B 177 1 9
HELIX 29 29 MSE B 191 GLU B 196 1 6
HELIX 30 30 ASP B 198 GLU B 212 1 15
HELIX 31 31 LYS B 223 ALA B 233 1 11
HELIX 32 32 SER B 243 GLY B 254 1 12
HELIX 33 33 HIS B 263 HIS B 265 5 3
HELIX 34 34 LEU B 266 GLY B 278 1 13
HELIX 35 35 PHE B 292 GLY B 299 1 8
HELIX 36 36 GLY B 301 TYR B 312 1 12
HELIX 37 37 LYS B 315 THR B 324 1 10
HELIX 38 38 THR B 324 GLY B 332 1 9
HELIX 39 39 THR B 383 LYS B 387 5 5
HELIX 40 40 MSE B 396 LEU B 401 5 6
HELIX 41 41 ASN B 488 GLY B 503 1 16
HELIX 42 42 PRO B 530 GLY B 546 1 17
HELIX 43 43 LYS B 559 ALA B 564 1 6
SHEET 1 A 4 LEU A 60 HIS A 65 0
SHEET 2 A 4 ASP A 53 VAL A 57 -1 N GLY A 55 O SER A 63
SHEET 3 A 4 VAL A 34 THR A 37 -1 N ILE A 36 O ILE A 54
SHEET 4 A 4 VAL A 76 ASP A 78 1 O ILE A 77 N LEU A 35
SHEET 1 B 7 GLU A 48 PRO A 51 0
SHEET 2 B 7 THR A 40 ASP A 43 -1 N ASP A 43 O GLU A 48
SHEET 3 B 7 TYR A 83 PRO A 86 1 O VAL A 84 N VAL A 42
SHEET 4 B 7 ILE A 347 PHE A 350 -1 O PHE A 350 N TYR A 83
SHEET 5 B 7 ALA A 358 ALA A 363 -1 O LEU A 362 N ILE A 347
SHEET 6 B 7 ARG A 366 GLU A 370 -1 O VAL A 368 N VAL A 361
SHEET 7 B 7 ARG A 373 MSE A 374 -1 O ARG A 373 N GLU A 370
SHEET 1 C 5 LEU A 88 MSE A 93 0
SHEET 2 C 5 VAL A 114 TRP A 119 1 O THR A 116 N ASP A 90
SHEET 3 C 5 ARG A 146 ALA A 151 1 O ARG A 146 N ILE A 117
SHEET 4 C 5 ILE A 182 ILE A 188 1 O ALA A 186 N ALA A 151
SHEET 5 C 5 LEU A 214 GLY A 217 1 O LEU A 214 N ILE A 185
SHEET 1 D 3 SER A 237 ASP A 238 0
SHEET 2 D 3 THR A 256 ARG A 260 1 O GLU A 258 N ASP A 238
SHEET 3 D 3 VAL A 284 CYS A 287 1 O THR A 285 N ILE A 257
SHEET 1 E 8 GLN A 421 ASP A 428 0
SHEET 2 E 8 LYS A 408 ASP A 415 -1 N THR A 413 O GLY A 423
SHEET 3 E 8 THR A 456 THR A 462 1 O PHE A 460 N ILE A 414
SHEET 4 E 8 THR A 441 THR A 446 -1 N THR A 441 O LEU A 461
SHEET 5 E 8 LEU A 482 GLY A 486 -1 O VAL A 484 N SER A 444
SHEET 6 E 8 ALA A 470 THR A 473 -1 N PHE A 471 O PHE A 485
SHEET 7 E 8 GLY A 505 SER A 510 -1 O ALA A 509 N ALA A 470
SHEET 8 E 8 LYS A 513 PRO A 519 -1 O LYS A 513 N SER A 510
SHEET 1 F 3 GLN A 421 ASP A 428 0
SHEET 2 F 3 LYS A 408 ASP A 415 -1 N THR A 413 O GLY A 423
SHEET 3 F 3 VAL A 592 GLU A 594 -1 O ILE A 593 N ARG A 410
SHEET 1 G 3 PRO A 572 THR A 575 0
SHEET 2 G 3 GLY A 578 ASP A 581 -1 O ALA A 580 N HIS A 573
SHEET 3 G 3 VAL A 587 MSE A 588 -1 O MSE A 588 N ILE A 579
SHEET 1 H 4 LEU B 60 HIS B 65 0
SHEET 2 H 4 ASP B 53 VAL B 57 -1 N ASP B 53 O HIS B 65
SHEET 3 H 4 VAL B 34 THR B 37 -1 N VAL B 34 O ILE B 56
SHEET 4 H 4 VAL B 76 ASP B 78 1 O ILE B 77 N LEU B 35
SHEET 1 I 7 LEU B 49 PRO B 51 0
SHEET 2 I 7 THR B 40 VAL B 42 -1 N LEU B 41 O ARG B 50
SHEET 3 I 7 TYR B 83 PRO B 86 1 O VAL B 84 N VAL B 42
SHEET 4 I 7 ILE B 347 PHE B 350 -1 O VAL B 348 N SER B 85
SHEET 5 I 7 ALA B 358 ALA B 363 -1 O LEU B 362 N ILE B 347
SHEET 6 I 7 ARG B 366 GLU B 370 -1 O ARG B 366 N ALA B 363
SHEET 7 I 7 ARG B 373 MSE B 374 -1 O ARG B 373 N GLU B 370
SHEET 1 J 5 LEU B 88 MSE B 93 0
SHEET 2 J 5 VAL B 114 TRP B 119 1 O THR B 115 N LEU B 88
SHEET 3 J 5 ARG B 146 ALA B 151 1 O LEU B 150 N TRP B 119
SHEET 4 J 5 ILE B 182 ILE B 188 1 O GLY B 183 N LEU B 149
SHEET 5 J 5 LEU B 214 GLY B 217 1 O CYS B 216 N ILE B 188
SHEET 1 K 3 SER B 237 ASP B 238 0
SHEET 2 K 3 THR B 256 ARG B 260 1 O GLU B 258 N ASP B 238
SHEET 3 K 3 VAL B 284 CYS B 287 1 O CYS B 287 N LEU B 259
SHEET 1 L 2 ASP B 428 LYS B 430 0
SHEET 2 L 2 PHE B 433 VAL B 435 -1 O VAL B 435 N ASP B 428
SHEET 1 M 6 LYS B 457 THR B 458 0
SHEET 2 M 6 MSE B 442 THR B 446 -1 N VAL B 445 O LYS B 457
SHEET 3 M 6 LEU B 482 GLY B 486 -1 O VAL B 484 N SER B 444
SHEET 4 M 6 ALA B 470 THR B 473 -1 N THR B 473 O THR B 483
SHEET 5 M 6 GLY B 505 SER B 510 -1 O ALA B 509 N ALA B 470
SHEET 6 M 6 LYS B 513 PRO B 519 -1 O LEU B 518 N MSE B 506
SHEET 1 N 2 ILE B 579 ALA B 580 0
SHEET 2 N 2 VAL B 587 MSE B 588 -1 O MSE B 588 N ILE B 579
LINK C HIS A 92 N MSE A 93 1555 1555 1.36
LINK C MSE A 93 N HIS A 94 1555 1555 1.32
LINK C SER A 98 N MSE A 99 1555 1555 1.31
LINK C MSE A 99 N ILE A 100 1555 1555 1.34
LINK C ILE A 188 N MSE A 189 1555 1555 1.32
LINK C MSE A 189 N ASN A 190 1555 1555 1.33
LINK C ASN A 190 N MSE A 191 1555 1555 1.32
LINK C MSE A 191 N ARG A 192 1555 1555 1.34
LINK C ARG A 200 N MSE A 201 1555 1555 1.35
LINK C MSE A 201 N SER A 202 1555 1555 1.33
LINK C PHE A 230 N MSE A 231 1555 1555 1.31
LINK C MSE A 231 N ALA A 232 1555 1555 1.35
LINK C LEU A 247 N MSE A 248 1555 1555 1.33
LINK C MSE A 248 N ALA A 249 1555 1555 1.33
LINK C ARG A 373 N MSE A 374 1555 1555 1.31
LINK C MSE A 374 N LEU A 375 1555 1555 1.31
LINK C SER A 389 N MSE A 390 1555 1555 1.33
LINK C MSE A 390 N LYS A 391 1555 1555 1.34
LINK C ARG A 395 N MSE A 396 1555 1555 1.33
LINK C MSE A 396 N ALA A 397 1555 1555 1.33
LINK C THR A 441 N MSE A 442 1555 1555 1.34
LINK C MSE A 442 N ILE A 443 1555 1555 1.34
LINK C GLY A 450 N MSE A 451 1555 1555 1.33
LINK C MSE A 451 N ALA A 452 1555 1555 1.33
LINK C ASP A 491 N MSE A 492 1555 1555 1.32
LINK C MSE A 492 N ALA A 493 1555 1555 1.34
LINK C GLY A 505 N MSE A 506 1555 1555 1.34
LINK C MSE A 506 N ALA A 507 1555 1555 1.34
LINK C ASP A 576 N MSE A 577 1555 1555 1.32
LINK C MSE A 577 N GLY A 578 1555 1555 1.36
LINK C VAL A 587 N MSE A 588 1555 1555 1.33
LINK C MSE A 588 N GLU A 589 1555 1555 1.32
LINK C HIS B 92 N MSE B 93 1555 1555 1.32
LINK C MSE B 93 N HIS B 94 1555 1555 1.35
LINK C SER B 98 N MSE B 99 1555 1555 1.32
LINK C MSE B 99 N ILE B 100 1555 1555 1.33
LINK C ILE B 188 N MSE B 189 1555 1555 1.33
LINK C MSE B 189 N ASN B 190 1555 1555 1.33
LINK C ASN B 190 N MSE B 191 1555 1555 1.31
LINK C MSE B 191 N ARG B 192 1555 1555 1.34
LINK C ARG B 200 N MSE B 201 1555 1555 1.33
LINK C MSE B 201 N SER B 202 1555 1555 1.32
LINK C PHE B 230 N MSE B 231 1555 1555 1.33
LINK C MSE B 231 N ALA B 232 1555 1555 1.34
LINK C LEU B 247 N MSE B 248 1555 1555 1.34
LINK C MSE B 248 N ALA B 249 1555 1555 1.31
LINK C ARG B 373 N MSE B 374 1555 1555 1.34
LINK C MSE B 374 N LEU B 375 1555 1555 1.33
LINK C SER B 389 N MSE B 390 1555 1555 1.33
LINK C MSE B 390 N LYS B 391 1555 1555 1.34
LINK C ARG B 395 N MSE B 396 1555 1555 1.33
LINK C MSE B 396 N ALA B 397 1555 1555 1.31
LINK C THR B 441 N MSE B 442 1555 1555 1.32
LINK C MSE B 442 N ILE B 443 1555 1555 1.35
LINK C GLY B 450 N MSE B 451 1555 1555 1.36
LINK C MSE B 451 N ALA B 452 1555 1555 1.30
LINK C ASP B 491 N MSE B 492 1555 1555 1.30
LINK C MSE B 492 N ALA B 493 1555 1555 1.33
LINK C GLY B 505 N MSE B 506 1555 1555 1.35
LINK C MSE B 506 N ALA B 507 1555 1555 1.35
LINK C ASP B 576 N MSE B 577 1555 1555 1.34
LINK C MSE B 577 N GLY B 578 1555 1555 1.32
LINK C VAL B 587 N MSE B 588 1555 1555 1.32
LINK C MSE B 588 N GLU B 589 1555 1555 1.33
LINK NE2 HIS A 92 FE FE A 607 1555 1555 2.20
LINK NE2 HIS A 94 FE FE A 607 1555 1555 2.33
LINK NE2 HIS A 122 FE FE A 608 1555 1555 2.28
LINK OE1 GLU A 123 FE FE A 608 1555 1555 1.98
LINK OE2 GLU A 123 FE FE A 608 1555 1555 2.45
LINK OE1 GLU A 187 FE FE A 606 1555 1555 2.25
LINK OE2 GLU A 187 FE FE A 607 1555 1555 2.38
LINK ND1 HIS A 218 FE FE A 606 1555 1555 2.29
LINK NE2 HIS A 239 FE FE A 606 1555 1555 2.11
LINK OE2 GLU A 240 FE FE A 606 1555 1555 2.21
LINK OD1 ASP A 289 FE FE A 607 1555 1555 2.30
LINK ND1 HIS A 477 FE FE A 608 1555 1555 2.41
LINK OD1 ASP A 478 FE FE A 608 1555 1555 2.24
LINK FE FE A 606 O HOH A 630 1555 1555 2.24
LINK NE2 HIS B 92 FE FE B 606 1555 1555 2.08
LINK NE2 HIS B 94 FE FE B 606 1555 1555 1.94
LINK NE2 HIS B 122 FE FE B 607 1555 1555 2.69
LINK OE2 GLU B 123 FE FE B 607 1555 1555 2.17
LINK OE1 GLU B 123 FE FE B 607 1555 1555 2.46
LINK ND1 HIS B 218 FE FE B 608 1555 1555 2.29
LINK NE2 HIS B 239 FE FE B 608 1555 1555 2.65
LINK OE2 GLU B 240 FE FE B 608 1555 1555 1.91
LINK OD1 ASP B 289 FE FE B 606 1555 1555 2.23
LINK ND1 HIS B 477 FE FE B 607 1555 1555 1.88
LINK OD1 ASP B 478 FE FE B 607 1555 1555 2.23
LINK FE FE B 606 O HOH B 635 1555 1555 2.07
LINK FE FE B 608 O HOH B 635 1555 1555 2.32
CISPEP 1 GLU A 9 PRO A 10 0 -13.49
CISPEP 2 VAL A 155 PRO A 156 0 -4.59
CISPEP 3 HIS A 477 ASP A 478 0 5.41
CISPEP 4 PRO A 553 PRO A 554 0 -23.76
CISPEP 5 GLU B 9 PRO B 10 0 -3.46
CISPEP 6 VAL B 155 PRO B 156 0 8.99
CISPEP 7 HIS B 477 ASP B 478 0 9.66
CISPEP 8 PRO B 553 PRO B 554 0 -9.66
SITE 1 AC1 5 GLU A 187 HIS A 218 HIS A 239 GLU A 240
SITE 2 AC1 5 HOH A 630
SITE 1 AC2 4 HIS A 92 HIS A 94 GLU A 187 ASP A 289
SITE 1 AC3 4 HIS A 122 GLU A 123 HIS A 477 ASP A 478
SITE 1 AC4 5 HIS B 92 HIS B 94 GLU B 187 ASP B 289
SITE 2 AC4 5 HOH B 635
SITE 1 AC5 4 HIS B 122 GLU B 123 HIS B 477 ASP B 478
SITE 1 AC6 5 GLU B 187 HIS B 218 HIS B 239 GLU B 240
SITE 2 AC6 5 HOH B 635
CRYST1 61.662 131.845 69.628 90.00 97.04 90.00 P 1 21 1 4
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 0.016217 0.000000 0.002003 0.00000
SCALE2 0.000000 0.007585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014471 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
