7f5w-pdb | HEADER PLANT PROTEIN 23-JUN-21 7F5W
TITLE CONSERVED AND DIVERGENT STRIGOLACTONE SIGNALING IN SACCHARUM
TITLE 2 SPONTANEUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH TILLERING AND DWARF 2 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHARUM HYBRID CULTIVAR ROC22;
SOURCE 3 ORGANISM_TAXID: 676074;
SOURCE 4 GENE: HTD2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS HYDROLASE PROTEIN DWARF 14 SL RECEPTOR, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.Q.ZHAO,Z.H.MING
REVDAT 1 04-MAY-22 7F5W 0
JRNL AUTH A.HU,Q.ZHAO,L.CHEN,J.ZHAO,Y.WANG,K.FENG,L.WU,M.XIE,X.ZHOU,
JRNL AUTH 2 L.XIAO,Z.MING,M.ZHANG,R.YAO
JRNL TITL IDENTIFICATION OF CONSERVED AND DIVERGENT STRIGOLACTONE
JRNL TITL 2 RECEPTORS IN SUGARCANE REVEALS A KEY RESIDUE CRUCIAL FOR
JRNL TITL 3 PLANT BRANCHING CONTROL.
JRNL REF FRONT PLANT SCI V. 12 47160 2021
JRNL REFN ESSN 1664-462X
JRNL PMID 34858455
JRNL DOI 10.3389/FPLS.2021.747160
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15_3459
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 110054
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.440
REMARK 3 FREE R VALUE TEST SET COUNT : 3790
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 4.9665 - 4.9627 0.99 4186 147 0.1680 0.1771
REMARK 3 2 4.9627 - 3.9391 1.00 4238 154 0.1410 0.1613
REMARK 3 3 3.9391 - 3.4412 0.89 3667 132 0.1565 0.2187
REMARK 3 4 3.4412 - 3.1266 0.99 3996 147 0.1717 0.2279
REMARK 3 5 3.1266 - 2.9025 1.00 4220 152 0.1771 0.2024
REMARK 3 6 2.9025 - 2.7313 1.00 4191 144 0.1864 0.2479
REMARK 3 7 2.7313 - 2.5945 1.00 4240 152 0.1840 0.2222
REMARK 3 8 2.5945 - 2.4816 1.00 4256 153 0.1903 0.2020
REMARK 3 9 2.4816 - 2.3861 1.00 4195 143 0.1907 0.2548
REMARK 3 10 2.3861 - 2.3037 1.00 4226 150 0.1790 0.2144
REMARK 3 11 2.3037 - 2.2317 1.00 4197 151 0.1965 0.2523
REMARK 3 12 2.2317 - 2.1679 1.00 4239 151 0.1950 0.2393
REMARK 3 13 2.1679 - 2.1108 1.00 4183 150 0.1923 0.1935
REMARK 3 14 2.1108 - 2.0593 0.91 918 31 0.2016 0.2350
REMARK 3 15 2.0593 - 2.0125 0.99 3601 128 0.2272 0.2543
REMARK 3 16 2.0125 - 1.9697 1.00 4184 154 0.2292 0.2543
REMARK 3 17 1.9697 - 1.9303 1.00 4263 150 0.2333 0.2565
REMARK 3 18 1.9303 - 1.8938 0.38 1599 55 0.2523 0.2965
REMARK 3 19 1.8938 - 1.8600 1.00 4173 148 0.2596 0.2792
REMARK 3 20 1.8600 - 1.8285 0.99 4181 153 0.2762 0.3508
REMARK 3 21 1.8285 - 1.7990 1.00 4223 153 0.2866 0.3566
REMARK 3 22 1.7990 - 1.7713 1.00 4203 151 0.2945 0.3196
REMARK 3 23 1.7713 - 1.7452 1.00 4203 146 0.3134 0.4001
REMARK 3 24 1.7452 - 1.7207 0.99 4242 153 0.3215 0.3507
REMARK 3 25 1.7207 - 1.6974 0.99 4173 150 0.3167 0.3315
REMARK 3 26 1.6974 - 1.6754 0.98 4151 140 0.3402 0.4174
REMARK 3 27 1.6754 - 1.6544 0.98 4116 152 0.3477 0.3982
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4898 2.9856 -4.7336
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.1121
REMARK 3 T33: 0.1126 T12: 0.0232
REMARK 3 T13: -0.0113 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.1212 L22: 0.4140
REMARK 3 L33: 0.4720 L12: 0.1350
REMARK 3 L13: -0.1864 L23: -0.1198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.0062 S13: -0.0100
REMARK 3 S21: -0.0506 S22: 0.0513 S23: -0.0439
REMARK 3 S31: 0.1244 S32: 0.0226 S33: 0.0049
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7F5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1300022939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-19
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 : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183
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 : 110054
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 70.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 6.144
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3VXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.05 M TRIS HYDROCHLORIDE PH 7.5, 5% V/V 2-PROPANOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 24.40500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.26050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.14750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.26050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.40500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.14750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 MET A -39
REMARK 465 LEU A -38
REMARK 465 ARG A -37
REMARK 465 SER A -36
REMARK 465 THR A -35
REMARK 465 HIS A -34
REMARK 465 SER A -33
REMARK 465 PRO A -32
REMARK 465 SER A -31
REMARK 465 GLY A -30
REMARK 465 SER A -29
REMARK 465 SER A -28
REMARK 465 SER A -27
REMARK 465 ALA A -26
REMARK 465 ALA A -25
REMARK 465 PRO A -24
REMARK 465 ALA A -23
REMARK 465 SER A -22
REMARK 465 SER A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 ASP A -18
REMARK 465 ALA A -17
REMARK 465 ALA A -16
REMARK 465 MET A -15
REMARK 465 VAL A -14
REMARK 465 GLY A -13
REMARK 465 GLY A -12
REMARK 465 GLY A -11
REMARK 465 GLY A -10
REMARK 465 ALA A -9
REMARK 465 ALA A -8
REMARK 465 ALA A -7
REMARK 465 ALA A -6
REMARK 465 ALA A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 MET B -39
REMARK 465 LEU B -38
REMARK 465 ARG B -37
REMARK 465 SER B -36
REMARK 465 THR B -35
REMARK 465 HIS B -34
REMARK 465 SER B -33
REMARK 465 PRO B -32
REMARK 465 SER B -31
REMARK 465 GLY B -30
REMARK 465 SER B -29
REMARK 465 SER B -28
REMARK 465 SER B -27
REMARK 465 ALA B -26
REMARK 465 ALA B -25
REMARK 465 PRO B -24
REMARK 465 ALA B -23
REMARK 465 SER B -22
REMARK 465 SER B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 ASP B -18
REMARK 465 ALA B -17
REMARK 465 ALA B -16
REMARK 465 MET B -15
REMARK 465 VAL B -14
REMARK 465 GLY B -13
REMARK 465 GLY B -12
REMARK 465 GLY B -11
REMARK 465 GLY B -10
REMARK 465 ALA B -9
REMARK 465 ALA B -8
REMARK 465 ALA B -7
REMARK 465 ALA B -6
REMARK 465 ALA B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
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 OE2 GLU B 174 O HOH B 301 1.82
REMARK 500 NH1 ARG A 47 O HOH A 301 1.93
REMARK 500 O HOH B 449 O HOH B 475 1.99
REMARK 500 O HOH A 356 O HOH A 438 2.01
REMARK 500 O HOH A 465 O HOH A 472 2.02
REMARK 500 O PRO B 1 O HOH B 302 2.04
REMARK 500 O HOH A 452 O HOH A 473 2.05
REMARK 500 ND1 HIS A 133 O HOH A 302 2.05
REMARK 500 O HOH A 385 O HOH A 427 2.07
REMARK 500 NH1 ARG B 262 O HOH B 303 2.08
REMARK 500 OH TYR B 159 O HOH B 304 2.19
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 OE2 GLU A 140 NH1 ARG A 230 4545 1.90
REMARK 500 O HOH A 457 O HOH B 412 4455 1.97
REMARK 500 O HOH A 461 O HOH B 446 2555 2.16
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 ARG A 230 NE - CZ - NH1 ANGL. DEV. = -3.3 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 97 -123.23 62.83
REMARK 500 ARG A 125 127.37 -172.16
REMARK 500 ASP A 129 85.55 -166.29
REMARK 500 ASN A 130 -110.38 56.13
REMARK 500 ASN A 151 83.12 -154.70
REMARK 500 ASN B 17 29.05 -146.91
REMARK 500 SER B 97 -123.39 66.29
REMARK 500 GLN B 243 20.94 -78.40
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 B 484 DISTANCE = 5.95 ANGSTROMS
DBREF1 7F5W A -39 268 UNP A0A0D5NT23_9POAL
DBREF2 7F5W A A0A0D5NT23 1 308
DBREF1 7F5W B -39 268 UNP A0A0D5NT23_9POAL
DBREF2 7F5W B A0A0D5NT23 1 308
SEQRES 1 A 308 MET LEU ARG SER THR HIS SER PRO SER GLY SER SER SER
SEQRES 2 A 308 ALA ALA PRO ALA SER SER SER SER ASP ALA ALA MET VAL
SEQRES 3 A 308 GLY GLY GLY GLY ALA ALA ALA ALA ALA GLY SER GLY GLY
SEQRES 4 A 308 ALA PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL
SEQRES 5 A 308 ARG VAL VAL GLY ASN GLY ASP ARG VAL VAL VAL LEU SER
SEQRES 6 A 308 HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL
SEQRES 7 A 308 LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR
SEQRES 8 A 308 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO GLU HIS PHE
SEQRES 9 A 308 ASP PHE ARG ARG TYR ASP THR LEU ASP SER TYR VAL ASP
SEQRES 10 A 308 ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG
SEQRES 11 A 308 CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 12 A 308 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE ALA LYS
SEQRES 13 A 308 LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 14 A 308 ASN ASP TYR HIS GLY GLY PHE GLU LEU PRO GLU ILE GLN
SEQRES 15 A 308 GLN VAL PHE ASP ALA MET ALA ALA ASN TYR SER ALA TRP
SEQRES 16 A 308 ALA VAL GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 17 A 308 PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN
SEQRES 18 A 308 MET ARG PRO ASP ILE SER LEU HIS VAL CYS ARG THR VAL
SEQRES 19 A 308 PHE ASN THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG
SEQRES 20 A 308 SER PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER
SEQRES 21 A 308 VAL PRO ALA SER VAL ALA ALA TYR LEU ARG ALA HIS LEU
SEQRES 22 A 308 GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY
SEQRES 23 A 308 HIS LEU PRO HIS LEU SER ALA PRO GLY LEU LEU ALA GLN
SEQRES 24 A 308 VAL LEU ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 B 308 MET LEU ARG SER THR HIS SER PRO SER GLY SER SER SER
SEQRES 2 B 308 ALA ALA PRO ALA SER SER SER SER ASP ALA ALA MET VAL
SEQRES 3 B 308 GLY GLY GLY GLY ALA ALA ALA ALA ALA GLY SER GLY GLY
SEQRES 4 B 308 ALA PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL
SEQRES 5 B 308 ARG VAL VAL GLY ASN GLY ASP ARG VAL VAL VAL LEU SER
SEQRES 6 B 308 HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL
SEQRES 7 B 308 LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR
SEQRES 8 B 308 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO GLU HIS PHE
SEQRES 9 B 308 ASP PHE ARG ARG TYR ASP THR LEU ASP SER TYR VAL ASP
SEQRES 10 B 308 ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG
SEQRES 11 B 308 CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 12 B 308 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE ALA LYS
SEQRES 13 B 308 LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 14 B 308 ASN ASP TYR HIS GLY GLY PHE GLU LEU PRO GLU ILE GLN
SEQRES 15 B 308 GLN VAL PHE ASP ALA MET ALA ALA ASN TYR SER ALA TRP
SEQRES 16 B 308 ALA VAL GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 17 B 308 PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN
SEQRES 18 B 308 MET ARG PRO ASP ILE SER LEU HIS VAL CYS ARG THR VAL
SEQRES 19 B 308 PHE ASN THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG
SEQRES 20 B 308 SER PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER
SEQRES 21 B 308 VAL PRO ALA SER VAL ALA ALA TYR LEU ARG ALA HIS LEU
SEQRES 22 B 308 GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY
SEQRES 23 B 308 HIS LEU PRO HIS LEU SER ALA PRO GLY LEU LEU ALA GLN
SEQRES 24 B 308 VAL LEU ARG ARG ALA LEU ALA ARG TYR
FORMUL 3 HOH *357(H2 O)
HELIX 1 AA1 SER A 2 LEU A 10 1 9
HELIX 2 AA2 ASP A 31 SER A 36 5 6
HELIX 3 AA3 VAL A 38 LEU A 42 5 5
HELIX 4 AA4 ASN A 60 PHE A 64 5 5
HELIX 5 AA5 ARG A 67 ASP A 70 5 4
HELIX 6 AA6 THR A 71 LEU A 86 1 16
HELIX 7 AA7 SER A 97 ARG A 110 1 14
HELIX 8 AA8 GLU A 137 ASN A 151 1 15
HELIX 9 AA9 ASN A 151 GLY A 165 1 15
HELIX 10 AB1 VAL A 168 MET A 182 1 15
HELIX 11 AB2 ARG A 183 ASN A 196 1 14
HELIX 12 AB3 LEU A 199 VAL A 206 5 8
HELIX 13 AB4 ALA A 223 LEU A 233 1 11
HELIX 14 AB5 LEU A 248 ALA A 253 1 6
HELIX 15 AB6 ALA A 253 LEU A 265 1 13
HELIX 16 AB7 SER B 2 LEU B 10 1 9
HELIX 17 AB8 ASP B 31 SER B 36 5 6
HELIX 18 AB9 VAL B 38 LEU B 42 5 5
HELIX 19 AC1 ASN B 60 PHE B 64 5 5
HELIX 20 AC2 ARG B 67 ASP B 70 5 4
HELIX 21 AC3 THR B 71 LEU B 86 1 16
HELIX 22 AC4 SER B 97 ARG B 110 1 14
HELIX 23 AC5 GLU B 137 ASN B 151 1 15
HELIX 24 AC6 ASN B 151 GLY B 165 1 15
HELIX 25 AC7 VAL B 168 ASN B 181 1 14
HELIX 26 AC8 ARG B 183 ASN B 196 1 14
HELIX 27 AC9 LEU B 199 VAL B 206 5 8
HELIX 28 AD1 PRO B 222 LEU B 233 1 12
HELIX 29 AD2 LEU B 248 ALA B 253 1 6
HELIX 30 AD3 ALA B 253 LEU B 265 1 13
SHEET 1 AA1 7 ARG A 13 GLY A 16 0
SHEET 2 AA1 7 ARG A 47 LEU A 50 -1 O VAL A 48 N VAL A 15
SHEET 3 AA1 7 VAL A 21 SER A 25 1 N VAL A 22 O VAL A 49
SHEET 4 AA1 7 CYS A 91 HIS A 96 1 O VAL A 94 N VAL A 23
SHEET 5 AA1 7 PHE A 114 ILE A 120 1 O ILE A 120 N GLY A 95
SHEET 6 AA1 7 CYS A 210 THR A 215 1 O VAL A 213 N LEU A 119
SHEET 7 AA1 7 THR A 237 LEU A 242 1 O GLU A 240 N GLN A 214
SHEET 1 AA2 7 ARG B 13 VAL B 15 0
SHEET 2 AA2 7 HIS B 46 LEU B 50 -1 O VAL B 48 N VAL B 15
SHEET 3 AA2 7 ARG B 20 SER B 25 1 N ARG B 20 O ARG B 47
SHEET 4 AA2 7 CYS B 91 HIS B 96 1 O VAL B 94 N VAL B 23
SHEET 5 AA2 7 PHE B 114 ILE B 120 1 O ALA B 115 N CYS B 91
SHEET 6 AA2 7 CYS B 210 GLN B 214 1 O VAL B 213 N LEU B 119
SHEET 7 AA2 7 THR B 237 PHE B 241 1 O GLU B 240 N GLN B 214
CRYST1 48.810 88.295 118.521 90.00 90.00 90.00 P 21 21 21 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 0.020488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011326 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008437 0.00000
TER 2079 TYR A 268
TER 4153 TYR B 268
MASTER 420 0 0 30 14 0 0 6 4508 2 0 48
END
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