HEADER OXIDOREDUCTASE 01-DEC-11 3VLM
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE MET244ALA VARIANT OF KATG FROM
TITLE 2 HALOARCULA MARISMORTUI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE-PEROXIDASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: KATG, CP 2, PEROXIDASE/CATALASE 2;
COMPND 5 EC: 1.11.1.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 3 ORGANISM_TAXID: 272569;
SOURCE 4 STRAIN: ATCC 43049;
SOURCE 5 GENE: KATG2;
SOURCE 6 EXPRESSION_SYSTEM: HALOFERAX VOLCANII;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 2246
KEYWDS CATALASE-PEROXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SATO,T.TEN-I,W.HIGUCHI,K.YOSHIMATSU,T.FUJIWARA
REVDAT 2 20-MAR-24 3VLM 1 REMARK SEQADV
REVDAT 1 05-DEC-12 3VLM 0
JRNL AUTH T.SATO,T.TEN-I,W.HIGUCHI,K.YOSHIMATSU,T.FUJIWARA
JRNL TITL CRYSTAL STRUCTURE AND KINETIC STUDIES ON MET244ALA VARIANT
JRNL TITL 2 OF KATG FROM HALOARCULA MARISMORTUI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 71879
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) : 0.285
REMARK 3 R VALUE (WORKING SET) : 0.283
REMARK 3 FREE R VALUE : 0.325
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3776
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) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5226
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.3980
REMARK 3 BIN FREE R VALUE SET COUNT : 231
REMARK 3 BIN FREE R VALUE : 0.4410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10386
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.19000
REMARK 3 B22 (A**2) : -3.08000
REMARK 3 B33 (A**2) : 3.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.57000
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): 0.301
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.524
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10731 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14609 ; 1.796 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1314 ; 6.454 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 556 ;41.369 ;25.468
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1722 ;20.075 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;18.588 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1507 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8489 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 6577 ; 1.046 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10529 ; 1.868 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4154 ; 2.060 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4080 ; 3.067 ; 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 : 1.40
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
REMARK 4
REMARK 4 3VLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000095198.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CONFORCAL MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 3.590
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.57
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.67M AMMONIUM SULFATE, 0.5M POTASSIUM
REMARK 280 CHLORIDE, 20MM SODIUM PHOSPHATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 288K, PH 6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 157.91500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 157.91500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.52500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 PRO A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 ASP A 8
REMARK 465 MET A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 THR A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 ARG A 16
REMARK 465 SER A 17
REMARK 465 LYS A 18
REMARK 465 ARG A 19
REMARK 465 PRO A 20
REMARK 465 LYS A 21
REMARK 465 SER A 22
REMARK 465 ASN A 23
REMARK 465 GLN A 24
REMARK 465 ASP A 25
REMARK 465 TRP A 26
REMARK 465 TRP A 27
REMARK 465 PRO A 28
REMARK 465 ASP A 49
REMARK 465 PHE A 50
REMARK 465 PRO A 189
REMARK 465 GLU A 190
REMARK 465 ASP A 191
REMARK 465 GLU A 192
REMARK 465 PHE A 193
REMARK 465 GLU A 194
REMARK 465 THR A 195
REMARK 465 GLN A 196
REMARK 465 GLU A 197
REMARK 465 ARG A 198
REMARK 465 PHE A 199
REMARK 465 ASP A 200
REMARK 465 GLU A 201
REMARK 465 PRO A 202
REMARK 465 GLY A 203
REMARK 465 GLU A 204
REMARK 465 ILE A 205
REMARK 465 GLN A 206
REMARK 465 GLU A 207
REMARK 465 GLY A 208
REMARK 465 LEU A 209
REMARK 465 GLY A 210
REMARK 465 ALA A 211
REMARK 465 ASN A 292
REMARK 465 LYS A 293
REMARK 465 ASN A 294
REMARK 465 GLY A 295
REMARK 465 ASN A 296
REMARK 465 SER A 297
REMARK 465 LYS A 298
REMARK 465 GLY A 299
REMARK 465 GLY A 300
REMARK 465 GLU A 301
REMARK 465 ARG A 522
REMARK 465 SER A 523
REMARK 465 ASP A 729
REMARK 465 LEU A 730
REMARK 465 GLU A 731
REMARK 465 HIS A 732
REMARK 465 HIS A 733
REMARK 465 HIS A 734
REMARK 465 HIS A 735
REMARK 465 HIS A 736
REMARK 465 HIS A 737
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 PRO B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 ASP B 8
REMARK 465 MET B 9
REMARK 465 SER B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 THR B 13
REMARK 465 GLY B 14
REMARK 465 GLY B 15
REMARK 465 ARG B 16
REMARK 465 SER B 17
REMARK 465 LYS B 18
REMARK 465 ARG B 19
REMARK 465 PRO B 20
REMARK 465 LYS B 21
REMARK 465 SER B 22
REMARK 465 ASN B 23
REMARK 465 GLN B 24
REMARK 465 ASP B 25
REMARK 465 TRP B 26
REMARK 465 TRP B 27
REMARK 465 PRO B 28
REMARK 465 ASP B 48
REMARK 465 ASP B 49
REMARK 465 PHE B 50
REMARK 465 GLY B 188
REMARK 465 PRO B 189
REMARK 465 GLU B 190
REMARK 465 ASP B 191
REMARK 465 GLU B 192
REMARK 465 PHE B 193
REMARK 465 GLU B 194
REMARK 465 THR B 195
REMARK 465 GLN B 196
REMARK 465 GLU B 197
REMARK 465 ARG B 198
REMARK 465 PHE B 199
REMARK 465 ASP B 200
REMARK 465 GLU B 201
REMARK 465 PRO B 202
REMARK 465 GLY B 203
REMARK 465 GLU B 204
REMARK 465 ILE B 205
REMARK 465 GLN B 206
REMARK 465 GLU B 207
REMARK 465 GLY B 208
REMARK 465 LEU B 209
REMARK 465 GLY B 210
REMARK 465 ALA B 211
REMARK 465 SER B 212
REMARK 465 VAL B 213
REMARK 465 MET B 214
REMARK 465 ASN B 292
REMARK 465 LYS B 293
REMARK 465 ASN B 294
REMARK 465 GLY B 295
REMARK 465 ASN B 296
REMARK 465 SER B 297
REMARK 465 LYS B 298
REMARK 465 GLY B 299
REMARK 465 GLY B 300
REMARK 465 GLU B 301
REMARK 465 ASP B 729
REMARK 465 LEU B 730
REMARK 465 GLU B 731
REMARK 465 HIS B 732
REMARK 465 HIS B 733
REMARK 465 HIS B 734
REMARK 465 HIS B 735
REMARK 465 HIS B 736
REMARK 465 HIS B 737
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 CH2 TRP B 95 CE1 TYR B 218 1.94
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 LEU A 31 132.35 -32.93
REMARK 500 ALA A 40 -70.31 -74.61
REMARK 500 PRO A 45 34.29 -97.28
REMARK 500 GLN A 57 1.70 -63.42
REMARK 500 TRP A 79 79.15 -151.91
REMARK 500 TYR A 83 12.68 54.81
REMARK 500 ASP A 105 -5.48 -149.61
REMARK 500 ASN A 128 -2.73 74.89
REMARK 500 ILE A 217 -55.38 -29.29
REMARK 500 TYR A 218 -74.87 -130.99
REMARK 500 ARG A 243 56.72 -63.10
REMARK 500 ALA A 244 -10.90 -167.32
REMARK 500 HIS A 259 4.61 -59.09
REMARK 500 GLU A 272 49.03 -141.35
REMARK 500 THR A 304 -62.53 -140.30
REMARK 500 PRO A 315 -7.85 -50.01
REMARK 500 ALA A 357 -34.57 -39.79
REMARK 500 PRO A 360 -102.07 -60.34
REMARK 500 ASP A 361 40.69 -35.83
REMARK 500 ARG A 409 -25.28 -38.18
REMARK 500 ASP A 437 57.21 -94.77
REMARK 500 ASP A 443 -37.83 -36.00
REMARK 500 ALA A 486 39.35 39.24
REMARK 500 LYS A 494 4.28 -62.37
REMARK 500 GLU A 500 80.42 42.26
REMARK 500 VAL A 581 72.99 -154.91
REMARK 500 ILE A 592 129.11 -27.61
REMARK 500 ALA A 626 52.90 -111.94
REMARK 500 TYR A 628 124.25 -39.31
REMARK 500 ASP A 630 59.48 15.49
REMARK 500 THR A 631 -169.21 -67.88
REMARK 500 GLU A 639 58.81 -113.05
REMARK 500 PRO A 640 159.24 -45.70
REMARK 500 ASN A 645 23.01 -77.21
REMARK 500 ASN A 650 -71.11 -63.84
REMARK 500 ASP A 653 126.78 -39.08
REMARK 500 ASP A 674 -60.76 -96.09
REMARK 500 VAL A 678 118.93 -34.59
REMARK 500 ARG A 727 87.76 -68.96
REMARK 500 LEU B 31 124.67 -39.95
REMARK 500 GLN B 38 -33.23 -39.41
REMARK 500 GLN B 57 -6.83 -57.31
REMARK 500 SER B 74 66.65 -106.56
REMARK 500 TRP B 79 83.52 -173.24
REMARK 500 ASN B 128 -0.92 63.86
REMARK 500 TYR B 218 -75.16 -132.92
REMARK 500 PRO B 228 57.54 -66.44
REMARK 500 ARG B 243 2.90 -57.89
REMARK 500 ALA B 245 -19.44 106.71
REMARK 500 GLU B 271 8.12 -56.17
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
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 HEM A 800 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 259 NE2
REMARK 620 2 HEM A 800 NA 93.6
REMARK 620 3 HEM A 800 NB 72.9 96.5
REMARK 620 4 HEM A 800 NC 82.7 176.2 81.7
REMARK 620 5 HEM A 800 ND 104.4 84.7 177.0 96.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 800 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 259 NE2
REMARK 620 2 HEM B 800 NA 86.6
REMARK 620 3 HEM B 800 NB 93.0 92.0
REMARK 620 4 HEM B 800 NC 91.1 177.6 89.0
REMARK 620 5 HEM B 800 ND 90.4 87.6 176.5 91.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UW8 RELATED DB: PDB
REMARK 900 SER305THR VARIANT
REMARK 900 RELATED ID: 3VLH RELATED DB: PDB
REMARK 900 ARG409LEU VARIANT
REMARK 900 RELATED ID: 3VLI RELATED DB: PDB
REMARK 900 CYANIDE ARG409LEU VARIANT
REMARK 900 RELATED ID: 3VLJ RELATED DB: PDB
REMARK 900 CYANIDE ARG409LEU VARIANT COMPLEXES WITH O-DIANISIDINE
REMARK 900 RELATED ID: 3VLK RELATED DB: PDB
REMARK 900 SER305ALA VARIANT
REMARK 900 RELATED ID: 3VLL RELATED DB: PDB
REMARK 900 SER305ALA VARIANT COMPLEXES WITH INHIBITOR SHA
DBREF 3VLM A 1 731 UNP O59651 KATG2_HALMA 1 731
DBREF 3VLM B 1 731 UNP O59651 KATG2_HALMA 1 731
SEQADV 3VLM ALA A 244 UNP O59651 MET 244 ENGINEERED MUTATION
SEQADV 3VLM HIS A 732 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS A 733 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS A 734 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS A 735 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS A 736 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS A 737 UNP O59651 EXPRESSION TAG
SEQADV 3VLM ALA B 244 UNP O59651 MET 244 ENGINEERED MUTATION
SEQADV 3VLM HIS B 732 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS B 733 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS B 734 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS B 735 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS B 736 UNP O59651 EXPRESSION TAG
SEQADV 3VLM HIS B 737 UNP O59651 EXPRESSION TAG
SEQRES 1 A 737 MET ALA GLU THR PRO ASN SER ASP MET SER GLY ALA THR
SEQRES 2 A 737 GLY GLY ARG SER LYS ARG PRO LYS SER ASN GLN ASP TRP
SEQRES 3 A 737 TRP PRO SER LYS LEU ASN LEU GLU ILE LEU ASP GLN ASN
SEQRES 4 A 737 ALA ARG ASP VAL GLY PRO VAL GLU ASP ASP PHE ASP TYR
SEQRES 5 A 737 ALA GLU GLU PHE GLN LYS LEU ASP LEU GLU ALA VAL LYS
SEQRES 6 A 737 SER ASP LEU GLU GLU LEU MET THR SER SER GLN ASP TRP
SEQRES 7 A 737 TRP PRO ALA ASP TYR GLY HIS TYR GLY PRO LEU PHE ILE
SEQRES 8 A 737 ARG MET ALA TRP HIS SER ALA GLY THR TYR ARG THR ALA
SEQRES 9 A 737 ASP GLY ARG GLY GLY ALA ALA GLY GLY ARG GLN ARG PHE
SEQRES 10 A 737 ALA PRO ILE ASN SER TRP PRO ASP ASN ALA ASN LEU ASP
SEQRES 11 A 737 LYS ALA ARG ARG LEU LEU LEU PRO ILE LYS GLN LYS TYR
SEQRES 12 A 737 GLY GLN LYS ILE SER TRP ALA ASP LEU MET ILE LEU ALA
SEQRES 13 A 737 GLY ASN VAL ALA ILE GLU SER MET GLY PHE LYS THR PHE
SEQRES 14 A 737 GLY TYR ALA GLY GLY ARG GLU ASP ALA PHE GLU GLU ASP
SEQRES 15 A 737 LYS ALA VAL ASN TRP GLY PRO GLU ASP GLU PHE GLU THR
SEQRES 16 A 737 GLN GLU ARG PHE ASP GLU PRO GLY GLU ILE GLN GLU GLY
SEQRES 17 A 737 LEU GLY ALA SER VAL MET GLY LEU ILE TYR VAL ASN PRO
SEQRES 18 A 737 GLU GLY PRO ASP GLY ASN PRO ASP PRO GLU ALA SER ALA
SEQRES 19 A 737 LYS ASN ILE ARG GLN THR PHE ASP ARG ALA ALA MET ASN
SEQRES 20 A 737 ASP LYS GLU THR ALA ALA LEU ILE ALA GLY GLY HIS THR
SEQRES 21 A 737 PHE GLY LYS VAL HIS GLY ALA ASP ASP PRO GLU GLU ASN
SEQRES 22 A 737 LEU GLY PRO GLU PRO GLU ALA ALA PRO ILE GLU GLN GLN
SEQRES 23 A 737 GLY LEU GLY TRP GLN ASN LYS ASN GLY ASN SER LYS GLY
SEQRES 24 A 737 GLY GLU MET ILE THR SER GLY ILE GLU GLY PRO TRP THR
SEQRES 25 A 737 GLN SER PRO THR GLU TRP ASP MET GLY TYR ILE ASN ASN
SEQRES 26 A 737 LEU LEU ASP TYR GLU TRP GLU PRO GLU LYS GLY PRO GLY
SEQRES 27 A 737 GLY ALA TRP GLN TRP ALA PRO LYS SER GLU GLU LEU LYS
SEQRES 28 A 737 ASN SER VAL PRO ASP ALA HIS ASP PRO ASP GLU LYS GLN
SEQRES 29 A 737 THR PRO MET MET LEU THR THR ASP ILE ALA LEU LYS ARG
SEQRES 30 A 737 ASP PRO ASP TYR ARG GLU VAL MET GLU THR PHE GLN GLU
SEQRES 31 A 737 ASN PRO MET GLU PHE GLY MET ASN PHE ALA LYS ALA TRP
SEQRES 32 A 737 TYR LYS LEU THR HIS ARG ASP MET GLY PRO PRO GLU ARG
SEQRES 33 A 737 PHE LEU GLY PRO GLU VAL PRO ASP GLU GLU MET ILE TRP
SEQRES 34 A 737 GLN ASP PRO LEU PRO ASP ALA ASP TYR ASP LEU ILE GLY
SEQRES 35 A 737 ASP GLU GLU ILE ALA GLU LEU LYS GLU GLU ILE LEU ASP
SEQRES 36 A 737 SER ASP LEU SER VAL SER GLN LEU VAL LYS THR ALA TRP
SEQRES 37 A 737 ALA SER ALA SER THR TYR ARG ASP SER ASP LYS ARG GLY
SEQRES 38 A 737 GLY ALA ASN GLY ALA ARG LEU ARG LEU GLU PRO GLN LYS
SEQRES 39 A 737 ASN TRP GLU VAL ASN GLU PRO GLU GLN LEU GLU THR VAL
SEQRES 40 A 737 LEU GLY THR LEU GLU ASN ILE GLN THR GLU PHE ASN ASP
SEQRES 41 A 737 SER ARG SER ASP GLY THR GLN VAL SER LEU ALA ASP LEU
SEQRES 42 A 737 ILE VAL LEU GLY GLY ASN ALA ALA VAL GLU GLN ALA ALA
SEQRES 43 A 737 ALA ASN ALA GLY TYR ASP VAL GLU ILE PRO PHE GLU PRO
SEQRES 44 A 737 GLY ARG VAL ASP ALA GLY PRO GLU HIS THR ASP ALA PRO
SEQRES 45 A 737 SER PHE ASP ALA LEU LYS PRO LYS VAL ASP GLY VAL ARG
SEQRES 46 A 737 ASN TYR ILE GLN ASP ASP ILE THR ARG PRO ALA GLU GLU
SEQRES 47 A 737 VAL LEU VAL ASP ASN ALA ASP LEU LEU ASN LEU THR ALA
SEQRES 48 A 737 SER GLU LEU THR ALA LEU ILE GLY GLY MET ARG SER ILE
SEQRES 49 A 737 GLY ALA ASN TYR GLN ASP THR ASP LEU GLY VAL PHE THR
SEQRES 50 A 737 ASP GLU PRO GLU THR LEU THR ASN ASP PHE PHE VAL ASN
SEQRES 51 A 737 LEU LEU ASP MET GLY THR GLU TRP GLU PRO ALA ALA ASP
SEQRES 52 A 737 SER GLU HIS ARG TYR LYS GLY LEU ASP ARG ASP THR GLY
SEQRES 53 A 737 GLU VAL LYS TRP GLU ALA THR ARG ILE ASP LEU ILE PHE
SEQRES 54 A 737 GLY SER ASN ASP ARG LEU ARG ALA ILE SER GLU VAL TYR
SEQRES 55 A 737 GLY SER ALA ASP ALA GLU LYS LYS LEU VAL HIS ASP PHE
SEQRES 56 A 737 VAL ASP THR TRP SER LYS VAL MET LYS LEU ASP ARG PHE
SEQRES 57 A 737 ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 737 MET ALA GLU THR PRO ASN SER ASP MET SER GLY ALA THR
SEQRES 2 B 737 GLY GLY ARG SER LYS ARG PRO LYS SER ASN GLN ASP TRP
SEQRES 3 B 737 TRP PRO SER LYS LEU ASN LEU GLU ILE LEU ASP GLN ASN
SEQRES 4 B 737 ALA ARG ASP VAL GLY PRO VAL GLU ASP ASP PHE ASP TYR
SEQRES 5 B 737 ALA GLU GLU PHE GLN LYS LEU ASP LEU GLU ALA VAL LYS
SEQRES 6 B 737 SER ASP LEU GLU GLU LEU MET THR SER SER GLN ASP TRP
SEQRES 7 B 737 TRP PRO ALA ASP TYR GLY HIS TYR GLY PRO LEU PHE ILE
SEQRES 8 B 737 ARG MET ALA TRP HIS SER ALA GLY THR TYR ARG THR ALA
SEQRES 9 B 737 ASP GLY ARG GLY GLY ALA ALA GLY GLY ARG GLN ARG PHE
SEQRES 10 B 737 ALA PRO ILE ASN SER TRP PRO ASP ASN ALA ASN LEU ASP
SEQRES 11 B 737 LYS ALA ARG ARG LEU LEU LEU PRO ILE LYS GLN LYS TYR
SEQRES 12 B 737 GLY GLN LYS ILE SER TRP ALA ASP LEU MET ILE LEU ALA
SEQRES 13 B 737 GLY ASN VAL ALA ILE GLU SER MET GLY PHE LYS THR PHE
SEQRES 14 B 737 GLY TYR ALA GLY GLY ARG GLU ASP ALA PHE GLU GLU ASP
SEQRES 15 B 737 LYS ALA VAL ASN TRP GLY PRO GLU ASP GLU PHE GLU THR
SEQRES 16 B 737 GLN GLU ARG PHE ASP GLU PRO GLY GLU ILE GLN GLU GLY
SEQRES 17 B 737 LEU GLY ALA SER VAL MET GLY LEU ILE TYR VAL ASN PRO
SEQRES 18 B 737 GLU GLY PRO ASP GLY ASN PRO ASP PRO GLU ALA SER ALA
SEQRES 19 B 737 LYS ASN ILE ARG GLN THR PHE ASP ARG ALA ALA MET ASN
SEQRES 20 B 737 ASP LYS GLU THR ALA ALA LEU ILE ALA GLY GLY HIS THR
SEQRES 21 B 737 PHE GLY LYS VAL HIS GLY ALA ASP ASP PRO GLU GLU ASN
SEQRES 22 B 737 LEU GLY PRO GLU PRO GLU ALA ALA PRO ILE GLU GLN GLN
SEQRES 23 B 737 GLY LEU GLY TRP GLN ASN LYS ASN GLY ASN SER LYS GLY
SEQRES 24 B 737 GLY GLU MET ILE THR SER GLY ILE GLU GLY PRO TRP THR
SEQRES 25 B 737 GLN SER PRO THR GLU TRP ASP MET GLY TYR ILE ASN ASN
SEQRES 26 B 737 LEU LEU ASP TYR GLU TRP GLU PRO GLU LYS GLY PRO GLY
SEQRES 27 B 737 GLY ALA TRP GLN TRP ALA PRO LYS SER GLU GLU LEU LYS
SEQRES 28 B 737 ASN SER VAL PRO ASP ALA HIS ASP PRO ASP GLU LYS GLN
SEQRES 29 B 737 THR PRO MET MET LEU THR THR ASP ILE ALA LEU LYS ARG
SEQRES 30 B 737 ASP PRO ASP TYR ARG GLU VAL MET GLU THR PHE GLN GLU
SEQRES 31 B 737 ASN PRO MET GLU PHE GLY MET ASN PHE ALA LYS ALA TRP
SEQRES 32 B 737 TYR LYS LEU THR HIS ARG ASP MET GLY PRO PRO GLU ARG
SEQRES 33 B 737 PHE LEU GLY PRO GLU VAL PRO ASP GLU GLU MET ILE TRP
SEQRES 34 B 737 GLN ASP PRO LEU PRO ASP ALA ASP TYR ASP LEU ILE GLY
SEQRES 35 B 737 ASP GLU GLU ILE ALA GLU LEU LYS GLU GLU ILE LEU ASP
SEQRES 36 B 737 SER ASP LEU SER VAL SER GLN LEU VAL LYS THR ALA TRP
SEQRES 37 B 737 ALA SER ALA SER THR TYR ARG ASP SER ASP LYS ARG GLY
SEQRES 38 B 737 GLY ALA ASN GLY ALA ARG LEU ARG LEU GLU PRO GLN LYS
SEQRES 39 B 737 ASN TRP GLU VAL ASN GLU PRO GLU GLN LEU GLU THR VAL
SEQRES 40 B 737 LEU GLY THR LEU GLU ASN ILE GLN THR GLU PHE ASN ASP
SEQRES 41 B 737 SER ARG SER ASP GLY THR GLN VAL SER LEU ALA ASP LEU
SEQRES 42 B 737 ILE VAL LEU GLY GLY ASN ALA ALA VAL GLU GLN ALA ALA
SEQRES 43 B 737 ALA ASN ALA GLY TYR ASP VAL GLU ILE PRO PHE GLU PRO
SEQRES 44 B 737 GLY ARG VAL ASP ALA GLY PRO GLU HIS THR ASP ALA PRO
SEQRES 45 B 737 SER PHE ASP ALA LEU LYS PRO LYS VAL ASP GLY VAL ARG
SEQRES 46 B 737 ASN TYR ILE GLN ASP ASP ILE THR ARG PRO ALA GLU GLU
SEQRES 47 B 737 VAL LEU VAL ASP ASN ALA ASP LEU LEU ASN LEU THR ALA
SEQRES 48 B 737 SER GLU LEU THR ALA LEU ILE GLY GLY MET ARG SER ILE
SEQRES 49 B 737 GLY ALA ASN TYR GLN ASP THR ASP LEU GLY VAL PHE THR
SEQRES 50 B 737 ASP GLU PRO GLU THR LEU THR ASN ASP PHE PHE VAL ASN
SEQRES 51 B 737 LEU LEU ASP MET GLY THR GLU TRP GLU PRO ALA ALA ASP
SEQRES 52 B 737 SER GLU HIS ARG TYR LYS GLY LEU ASP ARG ASP THR GLY
SEQRES 53 B 737 GLU VAL LYS TRP GLU ALA THR ARG ILE ASP LEU ILE PHE
SEQRES 54 B 737 GLY SER ASN ASP ARG LEU ARG ALA ILE SER GLU VAL TYR
SEQRES 55 B 737 GLY SER ALA ASP ALA GLU LYS LYS LEU VAL HIS ASP PHE
SEQRES 56 B 737 VAL ASP THR TRP SER LYS VAL MET LYS LEU ASP ARG PHE
SEQRES 57 B 737 ASP LEU GLU HIS HIS HIS HIS HIS HIS
HET HEM A 800 43
HET HEM B 800 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *151(H2 O)
HELIX 1 1 LEU A 33 GLN A 38 1 6
HELIX 2 2 TYR A 52 GLN A 57 1 6
HELIX 3 3 ASP A 60 MET A 72 1 13
HELIX 4 4 TYR A 86 THR A 100 1 15
HELIX 5 5 GLY A 113 PHE A 117 5 5
HELIX 6 6 PRO A 119 ALA A 127 5 9
HELIX 7 7 ASN A 128 LEU A 135 1 8
HELIX 8 8 LEU A 136 GLY A 144 1 9
HELIX 9 9 GLN A 145 ILE A 147 5 3
HELIX 10 10 SER A 148 SER A 163 1 16
HELIX 11 11 GLY A 223 ASN A 227 5 5
HELIX 12 12 ASP A 229 ARG A 243 1 15
HELIX 13 13 ASN A 247 HIS A 259 1 13
HELIX 14 14 GLU A 277 ALA A 281 5 5
HELIX 15 15 PRO A 282 GLN A 286 5 5
HELIX 16 16 MET A 320 ASP A 328 1 9
HELIX 17 17 LEU A 369 ASP A 378 1 10
HELIX 18 18 ASP A 378 ASN A 391 1 14
HELIX 19 19 ASN A 391 THR A 407 1 17
HELIX 20 20 PRO A 413 PHE A 417 5 5
HELIX 21 21 MET A 427 ASP A 431 5 5
HELIX 22 22 GLY A 442 SER A 456 1 15
HELIX 23 23 SER A 459 SER A 472 1 14
HELIX 24 24 ALA A 486 LEU A 490 5 5
HELIX 25 25 PRO A 492 ASN A 499 5 8
HELIX 26 26 GLU A 500 SER A 521 1 22
HELIX 27 27 SER A 529 ALA A 549 1 21
HELIX 28 28 GLY A 565 THR A 569 5 5
HELIX 29 29 ASP A 570 LYS A 578 5 9
HELIX 30 30 PRO A 595 LEU A 607 1 13
HELIX 31 31 THR A 610 GLY A 625 1 16
HELIX 32 32 ASN A 627 THR A 631 5 5
HELIX 33 33 ASN A 645 ASP A 653 1 9
HELIX 34 34 THR A 683 PHE A 689 1 7
HELIX 35 35 ASN A 692 SER A 704 1 13
HELIX 36 36 ALA A 707 LEU A 725 1 19
HELIX 37 37 LEU B 33 GLN B 38 1 6
HELIX 38 38 ASN B 39 ARG B 41 5 3
HELIX 39 39 TYR B 52 GLN B 57 1 6
HELIX 40 40 ASP B 60 MET B 72 1 13
HELIX 41 41 ALA B 81 HIS B 85 5 5
HELIX 42 42 TYR B 86 THR B 100 1 15
HELIX 43 43 GLY B 113 PHE B 117 5 5
HELIX 44 44 PRO B 119 ALA B 127 5 9
HELIX 45 45 ASN B 128 LEU B 135 1 8
HELIX 46 46 LEU B 136 GLY B 144 1 9
HELIX 47 47 GLN B 145 ILE B 147 5 3
HELIX 48 48 SER B 148 SER B 163 1 16
HELIX 49 49 GLY B 223 ASN B 227 5 5
HELIX 50 50 ASP B 229 ARG B 243 1 15
HELIX 51 51 ASN B 247 THR B 260 1 14
HELIX 52 52 ASP B 269 LEU B 274 1 6
HELIX 53 53 GLU B 277 ALA B 281 5 5
HELIX 54 54 PRO B 282 GLN B 286 5 5
HELIX 55 55 MET B 320 TYR B 329 1 10
HELIX 56 56 LEU B 369 ASP B 378 1 10
HELIX 57 57 ASP B 378 ASN B 391 1 14
HELIX 58 58 ASN B 391 THR B 407 1 17
HELIX 59 59 PRO B 413 PHE B 417 5 5
HELIX 60 60 MET B 427 ASP B 431 5 5
HELIX 61 61 GLY B 442 ASP B 455 1 14
HELIX 62 62 SER B 459 SER B 472 1 14
HELIX 63 63 ALA B 486 LEU B 490 5 5
HELIX 64 64 TRP B 496 ASN B 499 5 4
HELIX 65 65 GLU B 500 SER B 521 1 22
HELIX 66 66 SER B 529 ASN B 548 1 20
HELIX 67 67 ASP B 570 ASP B 575 1 6
HELIX 68 68 ALA B 576 LYS B 578 5 3
HELIX 69 69 GLY B 583 ASN B 586 5 4
HELIX 70 70 PRO B 595 LEU B 607 1 13
HELIX 71 71 THR B 610 GLY B 625 1 16
HELIX 72 72 ASN B 627 THR B 631 5 5
HELIX 73 73 ASN B 645 ASP B 653 1 9
HELIX 74 74 THR B 683 PHE B 689 1 7
HELIX 75 75 ASN B 692 SER B 704 1 13
HELIX 76 76 ALA B 707 LYS B 724 1 18
SHEET 1 A 2 LYS A 263 VAL A 264 0
SHEET 2 A 2 GLY A 309 PRO A 310 -1 O GLY A 309 N VAL A 264
SHEET 1 B 2 TRP A 331 LYS A 335 0
SHEET 2 B 2 TRP A 341 PRO A 345 -1 O ALA A 344 N GLU A 332
SHEET 1 C 2 VAL A 354 PRO A 355 0
SHEET 2 C 2 LYS A 363 GLN A 364 -1 O GLN A 364 N VAL A 354
SHEET 1 D 3 THR A 656 PRO A 660 0
SHEET 2 D 3 TYR A 668 ASP A 672 -1 O LEU A 671 N GLU A 657
SHEET 3 D 3 VAL A 678 ALA A 682 -1 O TRP A 680 N GLY A 670
SHEET 1 E 2 LYS B 263 VAL B 264 0
SHEET 2 E 2 GLY B 309 PRO B 310 -1 O GLY B 309 N VAL B 264
SHEET 1 F 2 TRP B 331 LYS B 335 0
SHEET 2 F 2 TRP B 341 PRO B 345 -1 O ALA B 344 N GLU B 332
SHEET 1 G 2 VAL B 354 PRO B 355 0
SHEET 2 G 2 LYS B 363 GLN B 364 -1 O GLN B 364 N VAL B 354
SHEET 1 H 2 VAL B 581 ASP B 582 0
SHEET 2 H 2 TYR B 587 ILE B 588 -1 O TYR B 587 N ASP B 582
SHEET 1 I 3 THR B 656 PRO B 660 0
SHEET 2 I 3 TYR B 668 ASP B 672 -1 O LYS B 669 N GLU B 659
SHEET 3 I 3 VAL B 678 ALA B 682 -1 O TRP B 680 N GLY B 670
LINK NE2 HIS A 259 FE HEM A 800 1555 1555 2.16
LINK NE2 HIS B 259 FE HEM B 800 1555 1555 2.31
CISPEP 1 ALA A 118 PRO A 119 0 -1.59
CISPEP 2 GLU A 491 PRO A 492 0 -5.83
CISPEP 3 ALA B 118 PRO B 119 0 1.24
CISPEP 4 GLU B 491 PRO B 492 0 -2.95
SITE 1 AC1 18 PRO A 88 LEU A 89 TRP A 95 PRO A 221
SITE 2 AC1 18 ILE A 237 LEU A 254 ILE A 255 GLY A 258
SITE 3 AC1 18 HIS A 259 GLY A 262 LYS A 263 VAL A 264
SITE 4 AC1 18 HIS A 265 THR A 304 SER A 305 TRP A 311
SITE 5 AC1 18 TRP A 403 HOH A 754
SITE 1 AC2 13 PRO B 88 TRP B 95 LEU B 254 GLY B 258
SITE 2 AC2 13 HIS B 259 GLY B 262 LYS B 263 VAL B 264
SITE 3 AC2 13 HIS B 265 THR B 304 SER B 305 THR B 371
SITE 4 AC2 13 TRP B 403
CRYST1 315.830 81.050 74.840 90.00 100.04 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003166 0.000000 0.000561 0.00000
SCALE2 0.000000 0.012338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013570 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
