HEADER TRANSPORT PROTEIN 28-DEC-04 1YEN
TITLE T-TO-T(HIGH) QUATERNARY TRANSITIONS IN HUMAN HEMOGLOBIN: BETAP36A OXY
TITLE 2 (2MM IHP, 20% PEG) (10 TEST SETS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: HEMOGLOBIN BETA CHAIN;
COMPND 6 CHAIN: B, D;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: HBB;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEMOGLOBIN MUTANT, GLOBIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.KAVANAUGH,P.H.ROGERS,A.ARNONE
REVDAT 5 23-AUG-23 1YEN 1 REMARK
REVDAT 4 20-OCT-21 1YEN 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1YEN 1 VERSN
REVDAT 2 10-MAY-05 1YEN 1 JRNL
REVDAT 1 11-JAN-05 1YEN 0
JRNL AUTH J.S.KAVANAUGH,P.H.ROGERS,A.ARNONE
JRNL TITL CRYSTALLOGRAPHIC EVIDENCE FOR A NEW ENSEMBLE OF
JRNL TITL 2 LIGAND-INDUCED ALLOSTERIC TRANSITIONS IN HEMOGLOBIN: THE
JRNL TITL 3 T-TO-T(HIGH) QUATERNARY TRANSITIONS.
JRNL REF BIOCHEMISTRY V. 44 6101 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15835899
JRNL DOI 10.1021/BI047813A
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 12142
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : 10 SETS MATCHED TO PDB ENTRY
REMARK 3 1Y45
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1365
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1993
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 248
REMARK 3 BIN FREE R VALUE : 0.4040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4316
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.68000
REMARK 3 B22 (A**2) : -1.66000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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): 0.505
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.614
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.300
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
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): 4652 ; 0.024 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4116 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6348 ; 2.054 ; 2.056
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9552 ; 1.276 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 564 ; 3.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 741 ;20.213 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 692 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5114 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 874 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1432 ; 0.305 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4267 ; 0.243 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1 ; 0.026 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 256 ; 0.307 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 11 ; 0.195 ; 0.500
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): 13 ; 0.226 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 17 ; 0.273 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.266 ; 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): 2824 ; 0.814 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4510 ; 1.554 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1828 ; 2.112 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1838 ; 3.512 ; 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 : BABINET MODEL WITH 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 1YEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 169.0
REMARK 200 PH : NULL
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1Y45
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000, 10 MM POTASSIUM
REMARK 280 PHOSPHATE, 100 MM POTASSIUM CHLORIDE, 3 MM SODIUM DITHIONITE, 10
REMARK 280 MG/ML DEOXYHB, PH 7.0, BATCH, TEMPERATURE 298K, 1 ATM N2.
REMARK 280 EXPOSING DEOXY CRYSTAL TO LIGAND: A DEOXY CRYSTAL WAS SOAKED
REMARK 280 (UNDER 1 ATM NITROGEN) IN SUBSTITUTE MOTHER LIQUOR CONTAINING 20%
REMARK 280 PEG 6000, 10 MM POTASSIUM PHOSPHATE (PH 7.0), 100 MM POTASSIUM
REMARK 280 CHLORIDE, AND 2.2 MM IHP. THE IHP-STABILIZED CRYSTAL WAS THEN
REMARK 280 EXPOSED TO 1 ATM OF OXYGEN AT 177K AND DATA WAS COLLECTED AT
REMARK 280 169K.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 47.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.75000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.20000
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT IN THIS ENTRY IS AN
REMARK 300 ALPHA2BETA2 TETRAMER. THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT AND THE
REMARK 300 BIOLOGICAL UNIT ARE EQUIVALENT.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 139
REMARK 465 TYR A 140
REMARK 465 ARG A 141
REMARK 465 LYS C 139
REMARK 465 TYR C 140
REMARK 465 ARG C 141
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 O HOH A 310 O HOH A 342 1.33
REMARK 500 NZ LYS C 7 OD1 ASP C 74 1.68
REMARK 500 N ASN D 102 O HOH D 401 1.78
REMARK 500 O LYS C 56 O HOH C 354 1.81
REMARK 500 OE1 GLU D 101 O HOH D 293 1.83
REMARK 500 NH1 ARG B 104 O HOH B 248 1.85
REMARK 500 CD LYS C 127 O HOH C 394 1.92
REMARK 500 O MET B 55 O HOH B 313 1.93
REMARK 500 O HIS B 146 O HOH B 278 1.96
REMARK 500 O HOH C 257 O HOH C 333 1.97
REMARK 500 ND1 HIS D 143 O HOH D 316 1.99
REMARK 500 O ASN B 139 O HOH B 397 2.04
REMARK 500 OE1 GLU B 121 O HOH B 289 2.06
REMARK 500 O PRO C 4 OG1 THR C 8 2.09
REMARK 500 O SER A 35 O HOH A 291 2.15
REMARK 500 ND2 ASN C 97 O HOH C 436 2.15
REMARK 500 C SER A 138 O HOH A 222 2.15
REMARK 500 OD1 ASN B 57 O HOH B 362 2.16
REMARK 500 OG1 THR C 67 O HOH C 384 2.17
REMARK 500 O HOH B 302 O HOH B 313 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS B 120 O1D HEM C 142 3555 2.10
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 ASP A 64 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 79 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP C 74 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 94 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP D 47 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP D 79 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 52 135.03 -35.47
REMARK 500 ASP A 75 48.94 -150.26
REMARK 500 HIS A 89 -69.19 -124.53
REMARK 500 VAL B 11 -75.55 -66.10
REMARK 500 ALA B 36 -52.34 -6.02
REMARK 500 ARG B 40 -1.65 -56.25
REMARK 500 LEU B 48 43.68 -150.86
REMARK 500 HIS B 77 66.33 -152.60
REMARK 500 ASN B 80 45.25 -152.45
REMARK 500 ASP C 75 23.79 -147.23
REMARK 500 ARG C 92 81.18 58.62
REMARK 500 LEU C 113 60.29 -119.38
REMARK 500 PHE C 117 61.80 -66.84
REMARK 500 PRO C 119 -16.37 -49.25
REMARK 500 HIS D 2 71.94 -48.67
REMARK 500 TYR D 35 66.80 -110.85
REMARK 500 LEU D 48 37.15 -142.73
REMARK 500 ASN D 80 71.14 -168.39
REMARK 500 HIS D 97 47.53 71.53
REMARK 500 LYS D 120 -72.11 -36.61
REMARK 500 GLU D 121 -19.67 -34.71
REMARK 500 PHE D 122 43.55 -89.05
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 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 142 NA 86.1
REMARK 620 3 HEM A 142 NB 93.3 89.4
REMARK 620 4 HEM A 142 NC 102.4 170.3 85.6
REMARK 620 5 HEM A 142 ND 95.6 93.6 170.8 90.1
REMARK 620 6 OXY A 150 O1 169.3 84.2 91.1 87.6 80.5
REMARK 620 7 OXY A 150 O2 171.9 99.3 80.8 71.8 90.2 18.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 147 NA 91.9
REMARK 620 3 HEM B 147 NB 94.4 92.4
REMARK 620 4 HEM B 147 NC 98.2 169.7 84.8
REMARK 620 5 HEM B 147 ND 96.6 83.1 168.3 97.7
REMARK 620 6 OXY B 150 O1 169.0 78.8 92.0 91.4 76.5
REMARK 620 7 OXY B 150 O2 170.7 88.3 76.3 81.5 92.7 17.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 142 NA 93.6
REMARK 620 3 HEM C 142 NB 97.2 87.4
REMARK 620 4 HEM C 142 NC 99.6 165.8 85.6
REMARK 620 5 HEM C 142 ND 96.0 92.4 166.7 91.5
REMARK 620 6 OXY C 150 O1 169.3 76.6 86.8 90.6 80.3
REMARK 620 7 OXY C 150 O2 168.6 92.5 73.5 73.6 93.3 21.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 147 NA 93.5
REMARK 620 3 HEM D 147 NB 83.7 96.4
REMARK 620 4 HEM D 147 NC 98.1 168.0 88.0
REMARK 620 5 HEM D 147 ND 105.2 80.7 170.7 93.2
REMARK 620 6 OXY D 150 O1 161.4 70.3 88.9 98.7 81.8
REMARK 620 7 OXY D 150 O2 160.9 85.2 77.5 84.8 93.5 17.7
REMARK 620 N 1 2 3 4 5 6
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 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY C 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY D 150
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y0W RELATED DB: PDB
REMARK 900 BETAV1M DEOXY LOW-SALT (10 TEST SETS)
REMARK 900 RELATED ID: 1Y45 RELATED DB: PDB
REMARK 900 BETAP36A DEOXY LOW-SALT (10 TEST SETS)
DBREF 1YEN A 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1YEN C 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1YEN B 1 146 UNP P68871 HBB_HUMAN 1 146
DBREF 1YEN D 1 146 UNP P68871 HBB_HUMAN 1 146
SEQADV 1YEN MET B 1 UNP P68871 VAL 1 ENGINEERED MUTATION
SEQADV 1YEN ALA B 36 UNP P68871 PRO 36 ENGINEERED MUTATION
SEQADV 1YEN MET D 1 UNP P68871 VAL 1 ENGINEERED MUTATION
SEQADV 1YEN ALA D 36 UNP P68871 PRO 36 ENGINEERED MUTATION
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 MET HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR ALA TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 MET HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR ALA TRP THR GLN
SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 D 146 LYS TYR HIS
HET HEM A 142 43
HET OXY A 150 2
HET HEM B 147 43
HET OXY B 150 2
HET HEM C 142 43
HET OXY C 150 2
HET HEM D 147 43
HET OXY D 150 2
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM OXY OXYGEN MOLECULE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 OXY 4(O2)
FORMUL 13 HOH *173(H2 O)
HELIX 1 1 SER A 3 GLY A 18 1 16
HELIX 2 2 HIS A 20 PHE A 36 1 17
HELIX 3 3 PRO A 37 PHE A 43 5 7
HELIX 4 4 SER A 52 HIS A 72 1 21
HELIX 5 5 ASP A 75 LEU A 80 1 6
HELIX 6 6 LEU A 80 HIS A 89 1 10
HELIX 7 7 ASP A 94 LEU A 113 1 20
HELIX 8 8 THR A 118 LEU A 136 1 19
HELIX 9 9 THR B 4 GLY B 16 1 13
HELIX 10 10 ASN B 19 TYR B 35 1 17
HELIX 11 11 PHE B 42 GLY B 46 5 5
HELIX 12 12 THR B 50 ASN B 57 1 8
HELIX 13 13 ASN B 57 ALA B 76 1 20
HELIX 14 14 HIS B 77 ASP B 79 5 3
HELIX 15 15 ASN B 80 PHE B 85 1 6
HELIX 16 16 PHE B 85 LYS B 95 1 11
HELIX 17 17 PRO B 100 GLY B 119 1 20
HELIX 18 18 LYS B 120 PHE B 122 5 3
HELIX 19 19 THR B 123 HIS B 143 1 21
HELIX 20 20 SER C 3 GLY C 18 1 16
HELIX 21 21 HIS C 20 PHE C 36 1 17
HELIX 22 22 PRO C 37 PHE C 43 5 7
HELIX 23 23 SER C 52 HIS C 72 1 21
HELIX 24 24 ASP C 75 HIS C 89 1 15
HELIX 25 25 ASP C 94 LEU C 113 1 20
HELIX 26 26 THR C 118 THR C 137 1 20
HELIX 27 27 THR D 4 GLY D 16 1 13
HELIX 28 28 ASN D 19 TYR D 35 1 17
HELIX 29 29 ALA D 36 GLY D 46 5 11
HELIX 30 30 THR D 50 ASN D 57 1 8
HELIX 31 31 ASN D 57 ALA D 76 1 20
HELIX 32 32 HIS D 77 ASP D 79 5 3
HELIX 33 33 ASN D 80 PHE D 85 1 6
HELIX 34 34 PHE D 85 LYS D 95 1 11
HELIX 35 35 GLU D 101 GLY D 119 1 19
HELIX 36 36 LYS D 120 PHE D 122 5 3
HELIX 37 37 THR D 123 HIS D 143 1 21
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.08
LINK FE HEM A 142 O1 OXY A 150 1555 1555 1.76
LINK FE HEM A 142 O2 OXY A 150 1555 1555 2.79
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.11
LINK FE HEM B 147 O1 OXY B 150 1555 1555 1.81
LINK FE HEM B 147 O2 OXY B 150 1555 1555 2.84
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.06
LINK FE HEM C 142 O1 OXY C 150 1555 1555 1.75
LINK FE HEM C 142 O2 OXY C 150 1555 1555 2.69
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 2.08
LINK FE HEM D 147 O1 OXY D 150 1555 1555 1.81
LINK FE HEM D 147 O2 OXY D 150 1555 1555 2.85
SITE 1 AC1 13 TYR A 42 PHE A 43 HIS A 45 HIS A 58
SITE 2 AC1 13 LYS A 61 LEU A 83 HIS A 87 LEU A 91
SITE 3 AC1 13 VAL A 93 ASN A 97 PHE A 98 LEU A 101
SITE 4 AC1 13 OXY A 150
SITE 1 AC2 2 HIS A 58 HEM A 142
SITE 1 AC3 13 PHE B 41 HIS B 63 LYS B 66 LEU B 88
SITE 2 AC3 13 LEU B 91 HIS B 92 VAL B 98 ASN B 102
SITE 3 AC3 13 LEU B 106 VAL B 137 LEU B 141 OXY B 150
SITE 4 AC3 13 HOH B 262
SITE 1 AC4 3 HIS B 63 VAL B 67 HEM B 147
SITE 1 AC5 17 LYS B 120 TYR C 42 PHE C 43 HIS C 45
SITE 2 AC5 17 PHE C 46 HIS C 58 LYS C 61 ALA C 65
SITE 3 AC5 17 LEU C 83 HIS C 87 LEU C 91 VAL C 93
SITE 4 AC5 17 ASN C 97 LEU C 101 LEU C 136 OXY C 150
SITE 5 AC5 17 HOH C 437
SITE 1 AC6 3 HIS C 58 VAL C 62 HEM C 142
SITE 1 AC7 9 LYS C 56 PHE D 41 HIS D 63 LEU D 91
SITE 2 AC7 9 HIS D 92 VAL D 98 PHE D 103 LEU D 141
SITE 3 AC7 9 OXY D 150
SITE 1 AC8 3 HIS D 63 VAL D 67 HEM D 147
CRYST1 95.500 98.400 67.200 90.00 90.00 90.00 P 21 21 2 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 0.010471 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014881 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
