HEADER TRANSCRIPTION 25-MAY-19 5QRU
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF HUMAN
TITLE 2 BRACHYURY IN COMPLEX WITH Z235341991
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-BOX TRANSCRIPTION FACTOR T;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BRACHYURY PROTEIN,PROTEIN T;
COMPND 5 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: TBXT, T;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SGC - DIAMOND I04-1 FRAGMENT SCREENING, PANDDA, XCHEMEXPLORER,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.NEWMAN,A.E.GAVARD,A.FERNANDEZ-CID,L.SHERESTHA,N.A.BURGESS-BROWN,
AUTHOR 2 F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,O.GILEADI
REVDAT 3 06-MAR-24 5QRU 1 LINK
REVDAT 2 07-AUG-19 5QRU 1 REMARK
REVDAT 1 10-JUL-19 5QRU 0
JRNL AUTH J.A.NEWMAN,A.E.GAVARD,A.FERNANDEZ-CID,L.SHERESTHA,
JRNL AUTH 2 N.A.BURGESS-BROWN,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,
JRNL AUTH 3 C.BOUNTRA,O.GILEADI
JRNL TITL PANDDA ANALYSIS GROUP DEPOSITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19693
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1002
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1398
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1369
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.45000
REMARK 3 B22 (A**2) : 1.45000
REMARK 3 B33 (A**2) : -2.91000
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.801
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1876 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1556 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2321 ; 1.622 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3638 ; 1.297 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 213 ; 7.954 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;30.395 ;23.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 280 ;17.365 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;19.066 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 209 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1931 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 338 ; 0.002 ; 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): 918 ; 3.610 ; 4.514
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 915 ; 3.612 ; 4.512
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1049 ; 5.587 ; 6.661
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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5QRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1001402327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20742
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 55.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : 2.43700
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 6F58
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CDCL, 0.1 M ACETATE PH 4.5, 32%
REMARK 280 PEG 400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 55.06500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.53250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 82.59750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.06500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.59750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 27.53250
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: 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 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 CD CD A 301 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 40
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2
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 A 59 107.73 69.02
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 A 470 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 471 DISTANCE = 6.60 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 CD A 304 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 100 NE2
REMARK 620 2 HOH A 458 O 100.3
REMARK 620 3 HOH A 459 O 102.3 122.0
REMARK 620 4 HOH A 460 O 113.2 106.3 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 303 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 122 SG
REMARK 620 2 HOH A 454 O 93.2
REMARK 620 3 HOH A 470 O 86.8 170.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 305 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 122 SG
REMARK 620 2 HOH A 449 O 99.0
REMARK 620 3 HOH A 471 O 87.6 172.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 301 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 167 OE1
REMARK 620 2 GLU A 167 OE1 0.0
REMARK 620 3 CYS A 186 SG 92.3 92.3
REMARK 620 4 CYS A 186 SG 88.6 88.6 38.3
REMARK 620 5 CYS A 186 SG 92.3 92.3 0.0 38.3
REMARK 620 6 CYS A 186 SG 88.6 88.6 38.3 0.0 38.3
REMARK 620 7 HOH A 455 O 89.9 89.9 111.5 149.7 111.5 149.7
REMARK 620 8 HOH A 455 O 92.9 92.9 78.3 116.6 78.3 116.6 33.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 302 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 167 OE1
REMARK 620 2 GLU A 167 OE2 50.0
REMARK 620 3 CYS A 186 SG 33.5 74.5
REMARK 620 4 CYS A 186 SG 45.9 77.0 15.8
REMARK 620 5 HOH A 453 O 143.4 103.4 126.8 111.0
REMARK 620 6 HOH A 461 O 106.5 104.5 127.8 143.1 104.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NY7 A 306
DBREF 5QRU A 41 211 UNP O15178 TBXT_HUMAN 41 211
SEQADV 5QRU GLY A 40 UNP O15178 EXPRESSION TAG
SEQRES 1 A 172 GLY GLU LEU ARG VAL GLY LEU GLU GLU SER GLU LEU TRP
SEQRES 2 A 172 LEU ARG PHE LYS GLU LEU THR ASN GLU MET ILE VAL THR
SEQRES 3 A 172 LYS ASN GLY ARG ARG MET PHE PRO VAL LEU LYS VAL ASN
SEQRES 4 A 172 VAL SER GLY LEU ASP PRO ASN ALA MET TYR SER PHE LEU
SEQRES 5 A 172 LEU ASP PHE VAL ALA ALA ASP ASN HIS ARG TRP LYS TYR
SEQRES 6 A 172 VAL ASN GLY GLU TRP VAL PRO GLY GLY LYS PRO GLU PRO
SEQRES 7 A 172 GLN ALA PRO SER CYS VAL TYR ILE HIS PRO ASP SER PRO
SEQRES 8 A 172 ASN PHE GLY ALA HIS TRP MET LYS ALA PRO VAL SER PHE
SEQRES 9 A 172 SER LYS VAL LYS LEU THR ASN LYS LEU ASN GLY GLY GLY
SEQRES 10 A 172 GLN ILE MET LEU ASN SER LEU HIS LYS TYR GLU PRO ARG
SEQRES 11 A 172 ILE HIS ILE VAL ARG VAL GLY GLY PRO GLN ARG MET ILE
SEQRES 12 A 172 THR SER HIS CYS PHE PRO GLU THR GLN PHE ILE ALA VAL
SEQRES 13 A 172 THR ALA TYR GLN ASN GLU GLU ILE THR ALA LEU LYS ILE
SEQRES 14 A 172 LYS TYR ASN
HET CD A 301 1
HET CD A 302 1
HET CD A 303 1
HET CD A 304 1
HET CD A 305 1
HET NY7 A 306 14
HETNAM CD CADMIUM ION
HETNAM NY7 N-(2-METHOXY-5-METHYLPHENYL)GLYCINAMIDE
FORMUL 2 CD 5(CD 2+)
FORMUL 7 NY7 C10 H14 N2 O2
FORMUL 8 HOH *71(H2 O)
HELIX 1 AA1 GLU A 48 LEU A 58 1 11
HELIX 2 AA2 GLY A 133 LYS A 138 1 6
HELIX 3 AA3 PRO A 188 GLN A 191 5 4
HELIX 4 AA4 ASN A 200 ASN A 211 1 12
SHEET 1 AA1 3 ARG A 43 LEU A 46 0
SHEET 2 AA1 3 LYS A 76 SER A 80 -1 O ASN A 78 N GLY A 45
SHEET 3 AA1 3 VAL A 141 SER A 142 -1 O VAL A 141 N VAL A 77
SHEET 1 AA2 5 GLU A 61 ILE A 63 0
SHEET 2 AA2 5 PHE A 192 VAL A 195 1 O VAL A 195 N MET A 62
SHEET 3 AA2 5 LYS A 165 VAL A 175 -1 N TYR A 166 O PHE A 192
SHEET 4 AA2 5 MET A 87 ALA A 96 -1 N ASP A 93 O ARG A 169
SHEET 5 AA2 5 ASN A 131 PHE A 132 -1 O ASN A 131 N TYR A 88
SHEET 1 AA3 4 TYR A 124 ILE A 125 0
SHEET 2 AA3 4 MET A 87 ALA A 96 -1 N LEU A 92 O TYR A 124
SHEET 3 AA3 4 LYS A 165 VAL A 175 -1 O ARG A 169 N ASP A 93
SHEET 4 AA3 4 MET A 181 CYS A 186 -1 O THR A 183 N ILE A 172
SHEET 1 AA4 3 ARG A 69 ARG A 70 0
SHEET 2 AA4 3 LYS A 147 THR A 149 -1 O LEU A 148 N ARG A 69
SHEET 3 AA4 3 ILE A 158 MET A 159 1 O ILE A 158 N LYS A 147
SHEET 1 AA5 2 TRP A 102 VAL A 105 0
SHEET 2 AA5 2 GLU A 108 PRO A 111 -1 O GLU A 108 N VAL A 105
LINK NE2 HIS A 100 CD CD A 304 1555 1555 2.23
LINK SG CYS A 122 CD CD A 303 1555 1555 2.70
LINK SG CYS A 122 CD CD A 305 1555 1555 2.39
LINK OE1 GLU A 167 CD CD A 301 1555 1555 2.55
LINK OE1 GLU A 167 CD CD A 301 1555 5655 2.55
LINK OE1 GLU A 167 CD CD A 302 1555 1555 2.69
LINK OE2 GLU A 167 CD CD A 302 1555 1555 2.30
LINK SG ACYS A 186 CD CD A 301 1555 1555 2.53
LINK SG BCYS A 186 CD CD A 301 1555 1555 2.46
LINK SG ACYS A 186 CD CD A 301 1555 5655 2.53
LINK SG BCYS A 186 CD CD A 301 1555 5655 2.46
LINK SG ACYS A 186 CD CD A 302 1555 5655 2.57
LINK SG BCYS A 186 CD CD A 302 1555 5655 2.50
LINK CD CD A 301 O HOH A 455 1555 1555 2.19
LINK CD CD A 301 O HOH A 455 1555 5655 2.19
LINK CD CD A 302 O HOH A 453 1555 5655 2.41
LINK CD CD A 302 O HOH A 461 1555 1555 2.39
LINK CD CD A 303 O HOH A 454 1555 1555 2.40
LINK CD CD A 303 O HOH A 470 1555 1555 2.55
LINK CD CD A 304 O HOH A 458 1555 1555 2.42
LINK CD CD A 304 O HOH A 459 1555 1555 2.47
LINK CD CD A 304 O HOH A 460 1555 1555 2.21
LINK CD CD A 305 O HOH A 449 1555 1555 2.56
LINK CD CD A 305 O HOH A 471 1555 1555 2.62
CISPEP 1 PHE A 72 PRO A 73 0 -6.66
CISPEP 2 SER A 129 PRO A 130 0 -17.18
SITE 1 AC1 4 GLU A 167 CYS A 186 CD A 302 HOH A 455
SITE 1 AC2 5 GLU A 167 CYS A 186 CD A 301 HOH A 453
SITE 2 AC2 5 HOH A 461
SITE 1 AC3 4 CYS A 122 HOH A 450 HOH A 454 HOH A 470
SITE 1 AC4 4 HIS A 100 HOH A 458 HOH A 459 HOH A 460
SITE 1 AC5 4 CYS A 122 HOH A 449 HOH A 470 HOH A 471
SITE 1 AC6 7 PRO A 117 GLN A 118 ALA A 119 SER A 121
SITE 2 AC6 7 MET A 159 LEU A 160 ASN A 161
CRYST1 60.080 60.080 110.130 90.00 90.00 90.00 P 41 2 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 0.016644 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009080 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
