HEADER HEME-BINDING PROTEIN 27-AUG-13 3WHM
TITLE STRUCTURE OF HEMOGLOBIN COMPLEX WITH 18-CROWN-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: ALPHA-GLOBIN, HEMOGLOBIN ALPHA CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 7 CHAIN: B, F;
COMPND 8 SYNONYM: BETA-GLOBIN, HEMOGLOBIN BETA CHAIN, LVV-HEMORPHIN-7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS 18-CROWN-6, HEME-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.C.LEE,L.L.LIN,A.H.J.WANG
REVDAT 4 08-NOV-23 3WHM 1 REMARK
REVDAT 3 24-AUG-22 3WHM 1 JRNL REMARK LINK
REVDAT 2 24-JUL-19 3WHM 1 REMARK
REVDAT 1 15-OCT-14 3WHM 0
JRNL AUTH C.C.LEE,M.MAESTRE-REYNA,K.C.HSU,H.C.WANG,C.I.LIU,W.Y.JENG,
JRNL AUTH 2 L.L.LIN,R.WOOD,C.C.CHOU,J.M.YANG,A.H.WANG
JRNL TITL CROWNING PROTEINS: MODULATING THE PROTEIN SURFACE PROPERTIES
JRNL TITL 2 USING CROWN ETHERS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 53 13054 2014
JRNL REFN ESSN 1521-3773
JRNL PMID 25287606
JRNL DOI 10.1002/ANIE.201405664
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.0
REMARK 3 NUMBER OF REFLECTIONS : 41996
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2256
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4300
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 268
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.280
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4705 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6418 ; 1.304 ; 2.016
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 562 ; 5.035 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;35.359 ;24.138
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 694 ;15.385 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ; 9.753 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 698 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3488 ; 0.006 ; 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): 2260 ; 1.064 ; 2.036
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2818 ; 1.779 ; 3.044
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2445 ; 1.351 ; 2.218
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7666 ; 4.849 ;17.852
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3WHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000096345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 8.0
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50382
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1A3N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG 3350, 0.2M LITHIUM
REMARK 280 SULFATE, 0.1M TRIS PH 8.0, 25MM 18-CROWN-6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 52.31900
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 ARG A 141
REMARK 465 VAL B 1
REMARK 465 TYR B 145
REMARK 465 HIS B 146
REMARK 465 ARG E 141
REMARK 465 VAL F 1
REMARK 465 TYR F 145
REMARK 465 HIS F 146
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 75 25.74 -141.24
REMARK 500 ASN B 19 94.77 -69.28
REMARK 500 ASN B 80 56.90 -150.23
REMARK 500 ASP E 75 43.25 -143.42
REMARK 500 HIS F 77 53.55 -141.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 375 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH F 382 DISTANCE = 6.41 ANGSTROMS
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 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 201 NA 86.1
REMARK 620 3 HEM A 201 NB 89.9 89.0
REMARK 620 4 HEM A 201 NC 95.2 178.5 90.3
REMARK 620 5 HEM A 201 ND 91.3 91.1 178.8 89.6
REMARK 620 6 OXY A 203 O2 167.0 80.9 88.9 97.7 89.9
REMARK 620 7 OXY A 203 O1 167.6 106.3 90.5 72.4 88.3 25.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 201 NA 88.6
REMARK 620 3 HEM B 201 NB 90.5 89.6
REMARK 620 4 HEM B 201 NC 92.6 178.5 89.5
REMARK 620 5 HEM B 201 ND 90.7 90.8 178.8 90.2
REMARK 620 6 OXY B 203 O1 174.7 86.3 88.3 92.5 90.5
REMARK 620 7 OXY B 203 O2 162.5 107.9 84.0 70.8 94.8 22.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 87 NE2
REMARK 620 2 HEM E 201 NA 89.5
REMARK 620 3 HEM E 201 NB 88.7 89.8
REMARK 620 4 HEM E 201 NC 91.6 178.4 89.1
REMARK 620 5 HEM E 201 ND 92.3 90.2 179.0 90.9
REMARK 620 6 OXY E 204 O2 176.3 86.7 91.3 92.1 87.7
REMARK 620 7 OXY E 204 O1 157.8 112.3 87.5 66.5 91.5 25.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 92 NE2
REMARK 620 2 HEM F 201 NA 83.3
REMARK 620 3 HEM F 201 NB 89.7 88.7
REMARK 620 4 HEM F 201 NC 97.9 178.3 90.1
REMARK 620 5 HEM F 201 ND 91.2 91.1 179.1 90.0
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O4B A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O4B B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O4B E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O4B E 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY E 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O4B F 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WH0 RELATED DB: PDB
DBREF 3WHM A 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 3WHM B 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 3WHM E 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 3WHM F 1 146 UNP P68871 HBB_HUMAN 2 147
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 VAL 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 PRO 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 E 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 E 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 E 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 E 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 E 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 E 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 E 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 E 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 E 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 E 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 E 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 F 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 F 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 F 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 F 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 F 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 F 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 F 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 F 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 F 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 F 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 F 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 F 146 LYS TYR HIS
HET HEM A 201 43
HET O4B A 202 18
HET OXY A 203 2
HET HEM B 201 43
HET O4B B 202 18
HET OXY B 203 2
HET HEM E 201 43
HET O4B E 202 18
HET O4B E 203 18
HET OXY E 204 2
HET HEM F 201 43
HET O4B F 202 18
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM O4B 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE
HETNAM OXY OXYGEN MOLECULE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 O4B 5(C12 H24 O6)
FORMUL 7 OXY 3(O2)
FORMUL 17 HOH *393(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 PRO A 95 LEU A 113 1 19
HELIX 8 8 THR A 118 THR A 137 1 20
HELIX 9 9 THR B 4 GLY B 16 1 13
HELIX 10 10 GLU B 22 TYR B 35 1 14
HELIX 11 11 PRO B 36 GLY B 46 5 11
HELIX 12 12 THR B 50 ASN B 57 1 8
HELIX 13 13 ASN B 57 HIS B 77 1 21
HELIX 14 14 ASN B 80 PHE B 85 1 6
HELIX 15 15 PHE B 85 LYS B 95 1 11
HELIX 16 16 PRO B 100 GLY B 119 1 20
HELIX 17 17 LYS B 120 PHE B 122 5 3
HELIX 18 18 THR B 123 HIS B 143 1 21
HELIX 19 19 SER E 3 LYS E 16 1 14
HELIX 20 20 VAL E 17 ALA E 19 5 3
HELIX 21 21 HIS E 20 PHE E 36 1 17
HELIX 22 22 PRO E 37 PHE E 43 5 7
HELIX 23 23 SER E 52 HIS E 72 1 21
HELIX 24 24 ASP E 75 LEU E 80 1 6
HELIX 25 25 LEU E 80 HIS E 89 1 10
HELIX 26 26 ASP E 94 LEU E 113 1 20
HELIX 27 27 THR E 118 SER E 138 1 21
HELIX 28 28 THR F 4 LYS F 17 1 14
HELIX 29 29 GLU F 22 TYR F 35 1 14
HELIX 30 30 PRO F 36 GLY F 46 5 11
HELIX 31 31 THR F 50 GLY F 56 1 7
HELIX 32 32 ASN F 57 HIS F 77 1 21
HELIX 33 33 ASN F 80 PHE F 85 1 6
HELIX 34 34 PHE F 85 LYS F 95 1 11
HELIX 35 35 PRO F 100 GLY F 119 1 20
HELIX 36 36 LYS F 120 PHE F 122 5 3
HELIX 37 37 THR F 123 HIS F 143 1 21
LINK NE2 HIS A 87 FE HEM A 201 1555 1555 2.14
LINK FE HEM A 201 O2 OXY A 203 1555 1555 2.03
LINK FE HEM A 201 O1 OXY A 203 1555 1555 2.65
LINK NE2 HIS B 92 FE HEM B 201 1555 1555 2.14
LINK FE HEM B 201 O1 OXY B 203 1555 1555 2.01
LINK FE HEM B 201 O2 OXY B 203 1555 1555 2.79
LINK NE2 HIS E 87 FE HEM E 201 1555 1555 2.15
LINK FE HEM E 201 O2 OXY E 204 1555 1555 1.94
LINK FE HEM E 201 O1 OXY E 204 1555 1555 2.58
LINK NE2 HIS F 92 FE HEM F 201 1555 1555 2.44
SITE 1 AC1 18 TYR A 42 PHE A 43 HIS A 45 HIS A 58
SITE 2 AC1 18 LYS A 61 LEU A 83 LEU A 86 HIS A 87
SITE 3 AC1 18 LEU A 91 VAL A 93 ASN A 97 PHE A 98
SITE 4 AC1 18 LEU A 101 LEU A 136 OXY A 203 HOH A 337
SITE 5 AC1 18 HOH A 365 HOH A 396
SITE 1 AC2 5 LEU A 34 PRO A 37 LYS A 40 LEU A 48
SITE 2 AC2 5 O4B B 202
SITE 1 AC3 3 HIS A 58 VAL A 62 HEM A 201
SITE 1 AC4 15 THR B 38 PHE B 41 PHE B 42 HIS B 63
SITE 2 AC4 15 ALA B 70 LEU B 88 HIS B 92 LEU B 96
SITE 3 AC4 15 VAL B 98 ASN B 102 PHE B 103 LEU B 106
SITE 4 AC4 15 LEU B 141 OXY B 203 HOH B 367
SITE 1 AC5 8 LYS A 40 PHE A 43 PRO A 44 PHE A 46
SITE 2 AC5 8 LEU A 48 O4B A 202 LYS B 59 ALA B 62
SITE 1 AC6 3 HIS B 63 VAL B 67 HEM B 201
SITE 1 AC7 17 TYR E 42 PHE E 43 HIS E 45 HIS E 58
SITE 2 AC7 17 LYS E 61 LEU E 83 LEU E 86 HIS E 87
SITE 3 AC7 17 LEU E 91 VAL E 93 ASN E 97 PHE E 98
SITE 4 AC7 17 LEU E 101 LEU E 136 OXY E 204 HOH E 310
SITE 5 AC7 17 HOH E 382
SITE 1 AC8 8 TRP B 15 VAL B 20 GLY B 69 SER B 72
SITE 2 AC8 8 LYS E 11 ALA E 71 VAL E 73 ASP E 74
SITE 1 AC9 5 LEU E 34 PRO E 37 LYS E 40 LEU E 48
SITE 2 AC9 5 O4B F 202
SITE 1 BC1 3 HIS E 58 VAL E 62 HEM E 201
SITE 1 BC2 12 PHE F 41 PHE F 42 HIS F 63 LEU F 88
SITE 2 BC2 12 HIS F 92 LEU F 96 VAL F 98 ASN F 102
SITE 3 BC2 12 PHE F 103 LEU F 106 LEU F 141 HOH F 338
SITE 1 BC3 9 LYS E 40 PHE E 43 PRO E 44 PHE E 46
SITE 2 BC3 9 LEU E 48 O4B E 203 PRO F 58 LYS F 59
SITE 3 BC3 9 ALA F 62
CRYST1 54.158 104.638 59.957 90.00 108.69 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 0.018464 0.000000 0.006246 0.00000
SCALE2 0.000000 0.009557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017607 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
