HEADER SIGNALING PROTEIN 27-NOV-06 2O09
TITLE CRYSTAL STRUCTURE OF THE H-NOX DOMAIN FROM NOSTOC SP. PCC 7120
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALR2278 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120;
SOURCE 5 GENE: ALR2278;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HEME, NO, CO, GUANYLYL CYCLASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.MA,F.VAN DEN AKKER
REVDAT 4 27-DEC-23 2O09 1 REMARK LINK
REVDAT 3 13-JUL-11 2O09 1 VERSN
REVDAT 2 24-FEB-09 2O09 1 VERSN
REVDAT 1 30-JAN-07 2O09 0
JRNL AUTH X.MA,N.SAYED,A.BEUVE,F.VAN DEN AKKER
JRNL TITL NO AND CO DIFFERENTIALLY ACTIVATE SOLUBLE GUANYLYL CYCLASE
JRNL TITL 2 VIA A HEME PIVOT-BEND MECHANISM.
JRNL REF EMBO J. V. 26 578 2007
JRNL REFN ISSN 0261-4189
JRNL PMID 17215864
JRNL DOI 10.1038/SJ.EMBOJ.7601521
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 35861
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1818
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2866
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.39
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): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.707
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3035 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4130 ; 1.221 ; 2.042
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 362 ; 5.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;36.320 ;24.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 494 ;14.033 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;19.219 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 424 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2336 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1306 ; 0.212 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2069 ; 0.312 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 354 ; 0.194 ; 0.500
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): 77 ; 0.224 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.189 ; 0.500
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): 1860 ; 2.019 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2872 ; 3.309 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1364 ; 3.996 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1254 ; 5.544 ; 6.000
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: NULL
REMARK 4
REMARK 4 2O09 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 35861
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 22.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M TRI-SODIUM CITRATE DIHYDRATE, PH
REMARK 280 5.6-6.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 61.71000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.71000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.71000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.71000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.71000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 61.71000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.71000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.71000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.71000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.71000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.71000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 61.71000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.71000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.71000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.71000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.71000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.71000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 592 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 575 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 597 LIES ON A SPECIAL POSITION.
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 ASP A 183
REMARK 465 SER A 184
REMARK 465 ASN A 185
REMARK 465 LEU A 186
REMARK 465 TYR A 187
REMARK 465 ASP A 188
REMARK 465 ASP A 189
REMARK 465 ASP B 183
REMARK 465 SER B 184
REMARK 465 ASN B 185
REMARK 465 LEU B 186
REMARK 465 TYR B 187
REMARK 465 ASP B 188
REMARK 465 ASP B 189
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 NH1 ARG A 168 O HOH A 611 1.86
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 SER A 126 -175.74 -175.35
REMARK 500 GLU B 57 -74.77 -55.44
REMARK 500 SER B 126 -179.94 -172.08
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 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 105 NE2
REMARK 620 2 HEM A 500 NA 104.8
REMARK 620 3 HEM A 500 NB 98.3 86.1
REMARK 620 4 HEM A 500 NC 91.9 163.0 88.6
REMARK 620 5 HEM A 500 ND 99.1 91.8 162.4 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 105 NE2
REMARK 620 2 HEM B 501 NA 106.1
REMARK 620 3 HEM B 501 NB 101.1 86.1
REMARK 620 4 HEM B 501 NC 90.6 163.3 89.9
REMARK 620 5 HEM B 501 ND 95.5 91.8 163.2 87.4
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O0C RELATED DB: PDB
REMARK 900 RELATED ID: 2O0G RELATED DB: PDB
DBREF 2O09 A 1 189 UNP Q8YUQ7 Q8YUQ7_ANASP 1 189
DBREF 2O09 B 1 189 UNP Q8YUQ7 Q8YUQ7_ANASP 1 189
SEQRES 1 A 189 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 A 189 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 A 189 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 A 189 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 A 189 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 A 189 LEU LEU ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 A 189 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 A 189 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 A 189 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 A 189 PRO ALA PHE GLU CYS GLN HIS THR SER SER LYS SER MET
SEQRES 11 A 189 GLU LEU HIS TYR GLN SER THR ARG CYS GLY LEU ALA PRO
SEQRES 12 A 189 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 A 189 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 A 189 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
SEQRES 15 A 189 ASP SER ASN LEU TYR ASP ASP
SEQRES 1 B 189 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 B 189 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 B 189 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 B 189 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 B 189 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 B 189 LEU LEU ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 B 189 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 B 189 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 B 189 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 B 189 PRO ALA PHE GLU CYS GLN HIS THR SER SER LYS SER MET
SEQRES 11 B 189 GLU LEU HIS TYR GLN SER THR ARG CYS GLY LEU ALA PRO
SEQRES 12 B 189 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 B 189 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 B 189 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
SEQRES 15 B 189 ASP SER ASN LEU TYR ASP ASP
HET HEM A 500 43
HET HEM B 501 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *229(H2 O)
HELIX 1 1 TYR A 2 GLY A 18 1 17
HELIX 2 2 GLY A 18 GLY A 30 1 13
HELIX 3 3 SER A 44 GLY A 60 1 17
HELIX 4 4 PRO A 62 GLU A 81 1 20
HELIX 5 5 TYR A 83 ALA A 90 1 8
HELIX 6 6 SER A 93 PHE A 112 1 20
HELIX 7 7 LEU A 141 PHE A 156 1 16
HELIX 8 8 PHE A 167 GLY A 171 5 5
HELIX 9 9 TYR B 2 GLY B 18 1 17
HELIX 10 10 GLY B 18 ALA B 29 1 12
HELIX 11 11 SER B 44 GLY B 60 1 17
HELIX 12 12 PRO B 62 GLU B 81 1 20
HELIX 13 13 TYR B 83 ALA B 90 1 8
HELIX 14 14 SER B 93 ASN B 100 1 8
HELIX 15 15 ASN B 100 PHE B 112 1 13
HELIX 16 16 LEU B 141 PHE B 156 1 16
HELIX 17 17 PHE B 167 GLY B 171 5 5
SHEET 1 A 4 ALA A 119 HIS A 124 0
SHEET 2 A 4 SER A 129 GLN A 135 -1 O HIS A 133 N GLU A 121
SHEET 3 A 4 ASP A 175 TYR A 181 -1 O PHE A 177 N LEU A 132
SHEET 4 A 4 VAL A 160 ALA A 166 -1 N THR A 163 O SER A 178
SHEET 1 B 4 ALA B 119 SER B 126 0
SHEET 2 B 4 SER B 129 GLN B 135 -1 O HIS B 133 N GLU B 121
SHEET 3 B 4 ASP B 175 TYR B 181 -1 O PHE B 177 N LEU B 132
SHEET 4 B 4 VAL B 160 ALA B 166 -1 N GLU B 161 O LYS B 180
LINK NE2 HIS A 105 FE HEM A 500 1555 1555 2.19
LINK NE2 HIS B 105 FE HEM B 501 1555 1555 2.25
SITE 1 AC1 20 MET A 1 TYR A 2 TRP A 74 TYR A 83
SITE 2 AC1 20 LEU A 86 PHE A 97 LEU A 101 HIS A 105
SITE 3 AC1 20 LEU A 115 ARG A 116 PRO A 118 PHE A 120
SITE 4 AC1 20 TYR A 134 SER A 136 ARG A 138 MET A 144
SITE 5 AC1 20 VAL A 145 LEU A 148 HOH A 505 HOH A 510
SITE 1 AC2 22 MET B 1 TYR B 2 TRP B 74 THR B 78
SITE 2 AC2 22 TYR B 83 LEU B 86 LEU B 87 PHE B 97
SITE 3 AC2 22 LEU B 101 LEU B 104 HIS B 105 LEU B 115
SITE 4 AC2 22 ARG B 116 PRO B 118 TYR B 134 SER B 136
SITE 5 AC2 22 ARG B 138 MET B 144 VAL B 145 LEU B 148
SITE 6 AC2 22 HOH B 502 HOH B 509
CRYST1 123.420 123.420 123.420 90.00 90.00 90.00 P 21 3 24
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 0.008102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
