HEADER TRANSCRIPTION 08-FEB-19 6QMQ
TITLE NF-YB/C HETERODIMER IN COMPLEX WITH NF-YA-DERIVED PEPTIDE STABILIZED
TITLE 2 WITH C8-HYDROCARBON LINKER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAAT BOX DNA-BINDING PROTEIN SUBUNIT A,NUCLEAR TRANSCRIPTION
COMPND 5 FACTOR Y SUBUNIT A,NF-YA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CAAT BOX DNA-BINDING PROTEIN SUBUNIT B,NUCLEAR TRANSCRIPTION
COMPND 11 FACTOR Y SUBUNIT B,NF-YB;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT GAMMA;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: CAAT BOX DNA-BINDING PROTEIN SUBUNIT C,NUCLEAR TRANSCRIPTION
COMPND 17 FACTOR Y SUBUNIT C,NF-YC,TRANSACTIVATOR HSM-1/2;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: NFYB, HAP3;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: NFYC;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS STAPLED PEPTIDE HISTONE FOLD TRANSCRIPTION FACTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KIEHSTALLER,S.JEGANATHAN,N.M.PEARCE,M.WENDT,T.N.GROSSMANN,S.HENNIG
REVDAT 6 24-JAN-24 6QMQ 1 LINK
REVDAT 5 13-JUL-22 6QMQ 1 SEQRES
REVDAT 4 18-MAY-22 6QMQ 1 COMPND SOURCE AUTHOR REMARK
REVDAT 4 2 1 DBREF SEQADV SEQRES HET
REVDAT 4 3 1 HETNAM HETSYN FORMUL HELIX
REVDAT 4 4 1 SHEET LINK SITE SCALE
REVDAT 4 5 1 ATOM
REVDAT 3 27-NOV-19 6QMQ 1 JRNL
REVDAT 2 30-OCT-19 6QMQ 1 JRNL
REVDAT 1 02-OCT-19 6QMQ 0
JRNL AUTH S.JEGANATHAN,M.WENDT,S.KIEHSTALLER,D.BRANCACCIO,A.KUEPPER,
JRNL AUTH 2 N.POSPIECH,A.CAROTENUTO,E.NOVELLINO,S.HENNIG,T.N.GROSSMANN
JRNL TITL CONSTRAINED PEPTIDES WITH FINE-TUNED FLEXIBILITY INHIBIT
JRNL TITL 2 NF-Y TRANSCRIPTION FACTOR ASSEMBLY.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 58 17351 2019
JRNL REFN ESSN 1521-3773
JRNL PMID 31539186
JRNL DOI 10.1002/ANIE.201907901
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 5661
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 635
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 402
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.46000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : 0.08000
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): 0.328
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.266
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.001
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1573 ; 0.014 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 1591 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2104 ; 1.627 ; 1.889
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3657 ; 1.145 ; 2.717
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 182 ; 5.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;35.790 ;21.307
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ;18.572 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.199 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 238 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1724 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 364 ; 0.001 ; 0.020
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 301 A 319
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8530 9.0830 -36.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0900 T22: 0.1367
REMARK 3 T33: 0.1206 T12: 0.0383
REMARK 3 T13: 0.0128 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 3.8709 L22: 9.6264
REMARK 3 L33: 3.3727 L12: 2.1454
REMARK 3 L13: 0.5453 L23: 0.6360
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: 0.1232 S13: -0.2499
REMARK 3 S21: -0.1058 S22: 0.1576 S23: 0.1350
REMARK 3 S31: 0.2129 S32: -0.0199 S33: -0.0697
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 57 B 143
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9380 5.1270 -23.6190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0574 T22: 0.0486
REMARK 3 T33: 0.0727 T12: -0.0079
REMARK 3 T13: -0.0153 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 4.6974 L22: 3.6227
REMARK 3 L33: 5.9161 L12: -0.4113
REMARK 3 L13: -1.8668 L23: 0.4177
REMARK 3 S TENSOR
REMARK 3 S11: -0.1379 S12: -0.0406 S13: -0.1448
REMARK 3 S21: 0.1834 S22: 0.0984 S23: -0.1632
REMARK 3 S31: 0.3214 S32: 0.2761 S33: 0.0395
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 36 C 119
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2820 6.9230 -20.0900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0698 T22: 0.1261
REMARK 3 T33: 0.0749 T12: -0.0625
REMARK 3 T13: -0.0100 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 3.6273 L22: 6.6411
REMARK 3 L33: 6.8038 L12: -3.3342
REMARK 3 L13: -2.2007 L23: 3.2804
REMARK 3 S TENSOR
REMARK 3 S11: -0.1341 S12: -0.1459 S13: -0.0929
REMARK 3 S21: 0.4078 S22: 0.0062 S23: 0.1166
REMARK 3 S31: 0.0768 S32: -0.1174 S33: 0.1279
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 6QMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1292100362.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 12.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.180
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: 4CSR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH6.5 0.2 M
REMARK 280 CALCIUM ACETATE 37% PEG600, VAPOR DIFFUSION, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 22.50500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.49500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.10500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.49500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.50500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.10500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 LEU A 320
REMARK 465 NH2 A 321
REMARK 465 GLY B 49
REMARK 465 PRO B 50
REMARK 465 SER B 51
REMARK 465 PHE B 52
REMARK 465 ARG B 53
REMARK 465 GLU B 54
REMARK 465 GLN B 55
REMARK 465 ASP B 56
REMARK 465 GLY C 25
REMARK 465 PRO C 26
REMARK 465 MET C 27
REMARK 465 GLU C 28
REMARK 465 GLU C 29
REMARK 465 ILE C 30
REMARK 465 ARG C 31
REMARK 465 ASN C 32
REMARK 465 LEU C 33
REMARK 465 THR C 34
REMARK 465 VAL C 35
REMARK 465 ARG C 120
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 THR B 75 -36.97 -31.93
REMARK 500 LYS B 109 49.66 29.71
REMARK 500 LYS C 59 -68.95 -109.89
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 NA C 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACE A 301 O
REMARK 620 2 GLU B 108 OE1 87.1
REMARK 620 3 GLU B 108 OE2 83.8 3.3
REMARK 620 4 ASP C 109 OD1 80.6 75.8 75.2
REMARK 620 5 ASP C 112 OD1 144.0 59.1 62.3 100.6
REMARK 620 6 ASP C 112 OD2 87.4 18.0 18.5 93.6 56.7
REMARK 620 N 1 2 3 4 5
DBREF 6QMQ A 302 320 UNP P23511 NFYA_HUMAN 267 285
DBREF 6QMQ B 51 143 UNP P25208 NFYB_HUMAN 51 143
DBREF 6QMQ C 27 120 UNP Q13952 NFYC_HUMAN 27 120
SEQADV 6QMQ ACE A 301 UNP P23511 ACETYLATION
SEQADV 6QMQ IC0 A 307 UNP P23511 TYR 272 ENGINEERED MUTATION
SEQADV 6QMQ MH8 A 311 UNP P23511 LEU 276 ENGINEERED MUTATION
SEQADV 6QMQ NH2 A 321 UNP P23511 AMIDATION
SEQADV 6QMQ GLY B 49 UNP P25208 EXPRESSION TAG
SEQADV 6QMQ PRO B 50 UNP P25208 EXPRESSION TAG
SEQADV 6QMQ GLY C 25 UNP Q13952 EXPRESSION TAG
SEQADV 6QMQ PRO C 26 UNP Q13952 EXPRESSION TAG
SEQRES 1 A 21 ACE VAL ASN ALA LYS GLN IC0 HIS ARG ILE MH8 LYS ARG
SEQRES 2 A 21 ARG GLN ALA ARG ALA LYS LEU NH2
SEQRES 1 B 95 GLY PRO SER PHE ARG GLU GLN ASP ILE TYR LEU PRO ILE
SEQRES 2 B 95 ALA ASN VAL ALA ARG ILE MET LYS ASN ALA ILE PRO GLN
SEQRES 3 B 95 THR GLY LYS ILE ALA LYS ASP ALA LYS GLU CYS VAL GLN
SEQRES 4 B 95 GLU CYS VAL SER GLU PHE ILE SER PHE ILE THR SER GLU
SEQRES 5 B 95 ALA SER GLU ARG CYS HIS GLN GLU LYS ARG LYS THR ILE
SEQRES 6 B 95 ASN GLY GLU ASP ILE LEU PHE ALA MET SER THR LEU GLY
SEQRES 7 B 95 PHE ASP SER TYR VAL GLU PRO LEU LYS LEU TYR LEU GLN
SEQRES 8 B 95 LYS PHE ARG GLU
SEQRES 1 C 96 GLY PRO MET GLU GLU ILE ARG ASN LEU THR VAL LYS ASP
SEQRES 2 C 96 PHE ARG VAL GLN GLU LEU PRO LEU ALA ARG ILE LYS LYS
SEQRES 3 C 96 ILE MET LYS LEU ASP GLU ASP VAL LYS MET ILE SER ALA
SEQRES 4 C 96 GLU ALA PRO VAL LEU PHE ALA LYS ALA ALA GLN ILE PHE
SEQRES 5 C 96 ILE THR GLU LEU THR LEU ARG ALA TRP ILE HIS THR GLU
SEQRES 6 C 96 ASP ASN LYS ARG ARG THR LEU GLN ARG ASN ASP ILE ALA
SEQRES 7 C 96 MET ALA ILE THR LYS PHE ASP GLN PHE ASP PHE LEU ILE
SEQRES 8 C 96 ASP ILE VAL PRO ARG
HET ACE A 301 3
HET IC0 A 307 9
HET MH8 A 311 8
HET NA C 201 1
HETNAM ACE ACETYL GROUP
HETNAM IC0 FMOC-(S)-2-(4-PENTENYL)-GLYCINE
HETNAM MH8 (2S)-2-AMINO-2-METHYLHEPT-6-ENOIC ACID
HETNAM NA SODIUM ION
HETSYN IC0 (2S)-2-AZANYLHEPT-6-ENOIC ACID
FORMUL 1 ACE C2 H4 O
FORMUL 1 IC0 C7 H13 N O2
FORMUL 1 MH8 C8 H15 N O2
FORMUL 4 NA NA 1+
FORMUL 5 HOH *7(H2 O)
HELIX 1 AA1 ASN A 303 LYS A 319 1 17
HELIX 2 AA2 PRO B 60 ILE B 72 1 13
HELIX 3 AA3 ALA B 79 GLU B 108 1 30
HELIX 4 AA4 ASN B 114 LEU B 125 1 12
HELIX 5 AA5 PHE B 127 SER B 129 5 3
HELIX 6 AA6 TYR B 130 GLU B 143 1 14
HELIX 7 AA7 ASP C 37 GLU C 42 1 6
HELIX 8 AA8 PRO C 44 LYS C 53 1 10
HELIX 9 AA9 ALA C 63 ASN C 91 1 29
HELIX 10 AB1 GLN C 97 PHE C 108 1 12
HELIX 11 AB2 ASP C 109 ILE C 115 5 7
SHEET 1 AA1 2 LYS B 77 ILE B 78 0
SHEET 2 AA1 2 THR C 95 LEU C 96 1 O LEU C 96 N LYS B 77
SHEET 1 AA2 2 THR B 112 ILE B 113 0
SHEET 2 AA2 2 MET C 60 ILE C 61 1 O MET C 60 N ILE B 113
LINK C ACE A 301 N VAL A 302 1555 1555 1.34
LINK C GLN A 306 N IC0 A 307 1555 1555 1.34
LINK C IC0 A 307 N HIS A 308 1555 1555 1.34
LINK C7 IC0 A 307 CD MH8 A 311 1555 1555 1.48
LINK C ILE A 310 N MH8 A 311 1555 1555 1.34
LINK C MH8 A 311 N LYS A 312 1555 1555 1.34
LINK O ACE A 301 NA NA C 201 1555 1555 2.31
LINK OE1 GLU B 108 NA NA C 201 1555 4554 2.40
LINK OE2 GLU B 108 NA NA C 201 1555 4554 2.39
LINK OD1 ASP C 109 NA NA C 201 1555 1555 2.28
LINK OD1 ASP C 112 NA NA C 201 1555 1555 2.32
LINK OD2 ASP C 112 NA NA C 201 1555 1555 2.29
CRYST1 45.010 52.210 72.990 90.00 90.00 90.00 P 21 21 21 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 0.022217 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013701 0.00000
HETATM 1 C ACE A 301 -14.519 20.836 -31.737 1.00 68.51 C
HETATM 2 O ACE A 301 -13.837 20.558 -30.785 1.00 75.56 O
HETATM 3 CH3 ACE A 301 -15.560 21.952 -31.658 1.00 61.14 C
(ATOM LINES ARE NOT SHOWN.)
END
