HEADER TRANSCRIPTION 10-APR-18 6D0C
TITLE CRYSTAL STRUCTURE OF HIF2A-B*:ARNT-B* COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 239-350;
COMPND 5 SYNONYM: EPAS-1,BASIC-HELIX-LOOP-HELIX-PAS PROTEIN MOP2,CLASS E BASIC
COMPND 6 HELIX-LOOP-HELIX PROTEIN 73,BHLHE73,HIF-1-ALPHA-LIKE FACTOR,HLF,
COMPND 7 HYPOXIA-INDUCIBLE FACTOR 2-ALPHA,HIF2-ALPHA,MEMBER OF PAS PROTEIN 2,
COMPND 8 PAS DOMAIN-CONTAINING PROTEIN 2;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: RESIDUES 356-470;
COMPND 15 SYNONYM: ARNT PROTEIN,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 2,
COMPND 16 BHLHE2,DIOXIN RECEPTOR,NUCLEAR TRANSLOCATOR,HYPOXIA-INDUCIBLE FACTOR
COMPND 17 1-BETA,HIF1-BETA;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPAS1, BHLHE73, HIF2A, MOP2, PASD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ARNT, BHLHE2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIF2A, PAS B DOMAIN, ARNT, HYPOXIA INDUCIBLE FACTOR, EPAS1,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR X.DU
REVDAT 2 04-OCT-23 6D0C 1 REMARK
REVDAT 1 31-OCT-18 6D0C 0
JRNL AUTH X.DU
JRNL TITL CRYSTAL STRUCTURE OF PT1940 BOUND TO HIF2A-B*:ARNT-B*
JRNL TITL 2 COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 35386
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1876
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2268
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.4480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1797
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : -0.51000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.45000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.783
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1849 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2495 ; 2.390 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 217 ; 6.869 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;37.094 ;24.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 324 ;15.023 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.740 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.169 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1407 ; 0.016 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6D0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97901
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37270
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4XT2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS, PH5.4 AND 16% PEG3350,
REMARK 280 SEEDING WITH CRUSHED CRYSTALS RIGHT AFTER SETUP, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 36.80200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.41450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.80200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.41450
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: 1800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 48.63457
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -41.41450
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -39.59060
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 B 502 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 GLY A -2
REMARK 465 GLU A -1
REMARK 465 ARG A 330
REMARK 465 ASN A 331
REMARK 465 LEU A 332
REMARK 465 GLN A 333
REMARK 465 LYS A 349
REMARK 465 ASN A 350
REMARK 465 GLY B 350
REMARK 465 GLU B 351
REMARK 465 PHE B 352
REMARK 465 LYS B 353
REMARK 465 GLY B 354
REMARK 465 LEU B 355
REMARK 465 ASN B 356
REMARK 465 VAL B 357
REMARK 465 SER B 468
REMARK 465 GLN B 469
REMARK 465 GLU B 470
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 OE1 GLU B 398 O HOH B 501 1.84
REMARK 500 O HOH B 572 O HOH B 574 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 2 C LEU A 239 N 0.258
REMARK 500 TRP B 436 CE2 TRP B 436 CD2 0.083
REMARK 500 TRP B 438 CE2 TRP B 438 CD2 0.089
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 GLY A 2 O - C - N ANGL. DEV. = -16.3 DEGREES
REMARK 500 ASP A 258 N - CA - CB ANGL. DEV. = -16.7 DEGREES
REMARK 500 ASP A 258 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 LEU A 319 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 MET A 338 CG - SD - CE ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 409 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 409 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 428 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 MET B 439 CG - SD - CE ANGL. DEV. = -10.5 DEGREES
REMARK 500 PHE B 446 CB - CG - CD1 ANGL. DEV. = -4.8 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 HIS A 313 44.51 -103.81
REMARK 500 ASN A 328 -136.68 -101.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 2 21.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6CZW RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL
DBREF 6D0C A 239 350 UNP Q99814 EPAS1_HUMAN 239 350
DBREF 6D0C B 356 470 UNP P27540 ARNT_HUMAN 356 470
SEQADV 6D0C GLY A -2 UNP Q99814 EXPRESSION TAG
SEQADV 6D0C GLU A -1 UNP Q99814 EXPRESSION TAG
SEQADV 6D0C PHE A 0 UNP Q99814 EXPRESSION TAG
SEQADV 6D0C LYS A 1 UNP Q99814 EXPRESSION TAG
SEQADV 6D0C GLY A 2 UNP Q99814 EXPRESSION TAG
SEQADV 6D0C GLU A 247 UNP Q99814 ARG 247 ENGINEERED MUTATION
SEQADV 6D0C GLY B 350 UNP P27540 EXPRESSION TAG
SEQADV 6D0C GLU B 351 UNP P27540 EXPRESSION TAG
SEQADV 6D0C PHE B 352 UNP P27540 EXPRESSION TAG
SEQADV 6D0C LYS B 353 UNP P27540 EXPRESSION TAG
SEQADV 6D0C GLY B 354 UNP P27540 EXPRESSION TAG
SEQADV 6D0C LEU B 355 UNP P27540 EXPRESSION TAG
SEQADV 6D0C ARG B 362 UNP P27540 GLU 362 ENGINEERED MUTATION
SEQRES 1 A 117 GLY GLU PHE LYS GLY LEU ASP SER LYS THR PHE LEU SER
SEQRES 2 A 117 GLU HIS SER MET ASP MET LYS PHE THR TYR CYS ASP ASP
SEQRES 3 A 117 ARG ILE THR GLU LEU ILE GLY TYR HIS PRO GLU GLU LEU
SEQRES 4 A 117 LEU GLY ARG SER ALA TYR GLU PHE TYR HIS ALA LEU ASP
SEQRES 5 A 117 SER GLU ASN MET THR LYS SER HIS GLN ASN LEU CYS THR
SEQRES 6 A 117 LYS GLY GLN VAL VAL SER GLY GLN TYR ARG MET LEU ALA
SEQRES 7 A 117 LYS HIS GLY GLY TYR VAL TRP LEU GLU THR GLN GLY THR
SEQRES 8 A 117 VAL ILE TYR ASN PRO ARG ASN LEU GLN PRO GLN CYS ILE
SEQRES 9 A 117 MET CYS VAL ASN TYR VAL LEU SER GLU ILE GLU LYS ASN
SEQRES 1 B 121 GLY GLU PHE LYS GLY LEU ASN VAL CYS GLN PRO THR ARG
SEQRES 2 B 121 PHE ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE
SEQRES 3 B 121 VAL ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO
SEQRES 4 B 121 GLN GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS
SEQRES 5 B 121 PRO GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN
SEQRES 6 B 121 VAL VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE
SEQRES 7 B 121 ARG PHE ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG
SEQRES 8 B 121 THR SER SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU
SEQRES 9 B 121 ILE GLU TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN
SEQRES 10 B 121 SER SER GLN GLU
FORMUL 3 HOH *128(H2 O)
HELIX 1 AA1 LEU A 239 SER A 241 5 3
HELIX 2 AA2 ARG A 260 GLY A 266 1 7
HELIX 3 AA3 HIS A 268 LEU A 273 1 6
HELIX 4 AA4 SER A 276 TYR A 281 5 6
HELIX 5 AA5 HIS A 282 LEU A 284 5 3
HELIX 6 AA6 ASP A 285 GLY A 300 1 16
HELIX 7 AA7 ARG B 379 GLY B 385 1 7
HELIX 8 AA8 GLN B 387 LEU B 391 5 5
HELIX 9 AA9 ASN B 395 CYS B 400 5 6
HELIX 10 AB1 HIS B 401 GLU B 403 5 3
HELIX 11 AB2 ASP B 404 VAL B 416 1 13
SHEET 1 AA1 5 PHE A 254 CYS A 257 0
SHEET 2 AA1 5 THR A 243 HIS A 248 -1 N GLU A 247 O THR A 255
SHEET 3 AA1 5 CYS A 336 VAL A 343 -1 O CYS A 339 N SER A 246
SHEET 4 AA1 5 TYR A 316 ILE A 326 -1 N ILE A 326 O CYS A 336
SHEET 5 AA1 5 GLN A 301 VAL A 303 -1 N VAL A 302 O GLY A 323
SHEET 1 AA2 5 PHE A 254 CYS A 257 0
SHEET 2 AA2 5 THR A 243 HIS A 248 -1 N GLU A 247 O THR A 255
SHEET 3 AA2 5 CYS A 336 VAL A 343 -1 O CYS A 339 N SER A 246
SHEET 4 AA2 5 TYR A 316 ILE A 326 -1 N ILE A 326 O CYS A 336
SHEET 5 AA2 5 TYR A 307 LEU A 310 -1 N TYR A 307 O LEU A 319
SHEET 1 AA3 5 PHE B 373 VAL B 376 0
SHEET 2 AA3 5 ARG B 362 HIS B 367 -1 N ARG B 366 O THR B 374
SHEET 3 AA3 5 TYR B 456 ASN B 463 -1 O CYS B 459 N SER B 365
SHEET 4 AA3 5 TRP B 436 PHE B 446 -1 N PHE B 444 O ILE B 458
SHEET 5 AA3 5 LEU B 423 ARG B 430 -1 N PHE B 427 O MET B 439
CRYST1 73.604 82.829 41.321 90.00 106.64 90.00 C 1 2 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 0.013586 0.000000 0.004059 0.00000
SCALE2 0.000000 0.012073 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025258 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
