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HEADER PLANT PROTEIN 19-DEC-22 8FJD
TITLE STRUCTURE OF CHLOROPHYLLASE FROM TRITICUM AESTIVUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPHYLLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE 3 ORGANISM_COMMON: BREAD WHEAT;
SOURCE 4 ORGANISM_TAXID: 4565;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BOGGS,M.JO,J.BRIDWELL-RABB
REVDAT 1 08-FEB-23 8FJD 0
JRNL AUTH M.JO,M.KNAPP,D.BOGGS,M.BRIMBERRY,P.DONNAN,J.BRIDWELL-RABB
JRNL TITL A STRUCTURE-FUNCTION ANALYSIS OF CHLOROPHYLLASE REVEALS A
JRNL TITL 2 MECHANISM FOR ACTIVITY REGULATION DEPENDENT ON DISULFIDE
JRNL TITL 3 BONDS
JRNL REF J.BIOL.CHEM. 2023
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 4.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 6810
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 342
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 49.1300 - 5.6200 0.93 3261 174 0.2645 0.2716
REMARK 3 2 5.6200 - 4.4600 0.97 3207 168 0.2674 0.2888
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.427
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.189
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 124.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.9
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 : 0.012 4603
REMARK 3 ANGLE : 1.591 6272
REMARK 3 CHIRALITY : 0.109 709
REMARK 3 PLANARITY : 0.010 820
REMARK 3 DIHEDRAL : 10.021 1670
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 8FJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-22.
REMARK 100 THE DEPOSITION ID IS D_1000270891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-22
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 : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6846
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.460
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 (%) : 96.8
REMARK 200 DATA REDUNDANCY : 12.57
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.62
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 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M SODIUM
REMARK 280 CACODYLATE (PH 6.5), 40% PEG300, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.55333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.27667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.41500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 16.13833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.69167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.55333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 32.27667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 16.13833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 48.41500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.69167
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: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 THR A 9
REMARK 465 MET A 10
REMARK 465 ASN A 11
REMARK 465 LYS A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 ALA A 17
REMARK 465 GLU A 18
REMARK 465 VAL A 19
REMARK 465 PRO A 20
REMARK 465 GLU A 21
REMARK 465 ALA A 22
REMARK 465 ASN A 321
REMARK 465 LEU A 322
REMARK 465 TYR A 323
REMARK 465 PHE A 324
REMARK 465 GLN A 325
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 ALA B 7
REMARK 465 GLU B 8
REMARK 465 THR B 9
REMARK 465 MET B 10
REMARK 465 ASN B 11
REMARK 465 LYS B 12
REMARK 465 SER B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 GLY B 16
REMARK 465 ALA B 17
REMARK 465 GLU B 18
REMARK 465 VAL B 19
REMARK 465 PRO B 20
REMARK 465 GLU B 21
REMARK 465 ALA B 319
REMARK 465 GLU B 320
REMARK 465 ASN B 321
REMARK 465 LEU B 322
REMARK 465 TYR B 323
REMARK 465 PHE B 324
REMARK 465 GLN B 325
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 PHE A 27 18.07 55.77
REMARK 500 HIS A 88 36.43 -93.27
REMARK 500 LEU A 128 152.53 -49.35
REMARK 500 SER A 145 -129.78 50.39
REMARK 500 PHE A 195 107.02 -59.14
REMARK 500 ASN A 214 10.04 59.74
REMARK 500 ILE A 215 -55.86 65.38
REMARK 500 ALA A 221 73.34 -111.46
REMARK 500 PRO A 222 151.93 -49.29
REMARK 500 ASP A 224 -6.73 74.35
REMARK 500 VAL A 225 25.35 -142.66
REMARK 500 ASN A 226 -163.98 -110.18
REMARK 500 LYS A 258 -53.76 70.09
REMARK 500 GLU A 292 20.26 47.81
REMARK 500 ALA A 295 -76.95 -110.64
REMARK 500 PHE B 23 -119.23 60.64
REMARK 500 SER B 145 -132.69 49.04
REMARK 500 ASP B 172 71.48 27.23
REMARK 500 ASN B 214 -7.12 71.72
REMARK 500 ILE B 215 -70.33 69.19
REMARK 500 ALA B 221 73.69 -110.18
REMARK 500 ASP B 224 -53.60 70.16
REMARK 500 CYS B 238 119.05 -161.76
REMARK 500 ALA B 256 125.55 -33.82
REMARK 500 PHE B 259 1.11 -69.25
REMARK 500 ALA B 289 -84.76 -119.78
REMARK 500 ASP B 312 117.29 -164.50
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255 OD1
REMARK 620 2 ASP A 255 OD2 45.4
REMARK 620 3 HOH A 501 O 96.8 107.6
REMARK 620 4 HOH A 502 O 46.9 60.6 52.8
REMARK 620 5 ASP B 255 OD1 72.2 109.9 108.3 101.7
REMARK 620 6 ASP B 255 OD2 115.6 153.9 90.8 123.8 45.2
REMARK 620 7 HOH B 401 O 84.3 89.2 157.6 131.2 50.7 68.9
REMARK 620 8 HOH B 402 O 85.8 55.2 151.0 115.8 100.0 114.2 51.3
REMARK 620 N 1 2 3 4 5 6 7
DBREF 8FJD A 1 319 UNP W6EIP8 W6EIP8_WHEAT 1 319
DBREF 8FJD B 1 319 UNP W6EIP8 W6EIP8_WHEAT 1 319
SEQADV 8FJD GLU A 320 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD ASN A 321 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD LEU A 322 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD TYR A 323 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD PHE A 324 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD GLN A 325 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD GLU B 320 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD ASN B 321 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD LEU B 322 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD TYR B 323 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD PHE B 324 UNP W6EIP8 EXPRESSION TAG
SEQADV 8FJD GLN B 325 UNP W6EIP8 EXPRESSION TAG
SEQRES 1 A 325 MET ALA ALA ALA ALA PRO ALA GLU THR MET ASN LYS SER
SEQRES 2 A 325 ALA ALA GLY ALA GLU VAL PRO GLU ALA PHE THR SER VAL
SEQRES 3 A 325 PHE GLN PRO GLY LYS LEU ALA VAL GLU ALA ILE GLN VAL
SEQRES 4 A 325 ASP GLU ASN ALA ALA PRO THR PRO PRO ILE PRO VAL LEU
SEQRES 5 A 325 ILE VAL ALA PRO LYS ASP ALA GLY THR TYR PRO VAL ALA
SEQRES 6 A 325 MET LEU LEU HIS GLY PHE PHE LEU HIS ASN HIS PHE TYR
SEQRES 7 A 325 GLU HIS LEU LEU ARG HIS VAL ALA SER HIS GLY PHE ILE
SEQRES 8 A 325 ILE VAL ALA PRO GLN PHE SER ILE SER ILE ILE PRO SER
SEQRES 9 A 325 GLY ASP ALA GLU ASP ILE ALA ALA ALA ALA LYS VAL ALA
SEQRES 10 A 325 ASP TRP LEU PRO ASP GLY LEU PRO SER VAL LEU PRO LYS
SEQRES 11 A 325 GLY VAL GLU PRO GLU LEU SER LYS LEU ALA LEU ALA GLY
SEQRES 12 A 325 HIS SER ARG GLY GLY HIS THR ALA PHE SER LEU ALA LEU
SEQRES 13 A 325 GLY HIS ALA LYS THR GLN LEU THR PHE SER ALA LEU ILE
SEQRES 14 A 325 GLY LEU ASP PRO VAL ALA GLY THR GLY LYS SER SER GLN
SEQRES 15 A 325 LEU GLN PRO LYS ILE LEU THR TYR GLU PRO SER SER PHE
SEQRES 16 A 325 GLY MET ALA MET PRO VAL LEU VAL ILE GLY THR GLY LEU
SEQRES 17 A 325 GLY GLU GLU LYS LYS ASN ILE PHE PHE PRO PRO CYS ALA
SEQRES 18 A 325 PRO LYS ASP VAL ASN HIS ALA GLU PHE TYR ARG GLU CYS
SEQRES 19 A 325 ARG PRO PRO CYS TYR TYR LEU VAL THR LYS ASP TYR GLY
SEQRES 20 A 325 HIS LEU ASP MET LEU ASP ASP ASP ALA PRO LYS PHE ILE
SEQRES 21 A 325 THR CYS VAL CYS LYS ASP GLY ASN GLY CYS LYS GLY LYS
SEQRES 22 A 325 MET ARG ARG CYS VAL ALA GLY ILE MET VAL ALA PHE LEU
SEQRES 23 A 325 ASN ALA ALA LEU GLY GLU LYS ASP ALA ASP LEU GLU ALA
SEQRES 24 A 325 ILE LEU ARG ASP PRO ALA VAL ALA PRO THR THR LEU ASP
SEQRES 25 A 325 PRO VAL GLU HIS ARG VAL ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 B 325 MET ALA ALA ALA ALA PRO ALA GLU THR MET ASN LYS SER
SEQRES 2 B 325 ALA ALA GLY ALA GLU VAL PRO GLU ALA PHE THR SER VAL
SEQRES 3 B 325 PHE GLN PRO GLY LYS LEU ALA VAL GLU ALA ILE GLN VAL
SEQRES 4 B 325 ASP GLU ASN ALA ALA PRO THR PRO PRO ILE PRO VAL LEU
SEQRES 5 B 325 ILE VAL ALA PRO LYS ASP ALA GLY THR TYR PRO VAL ALA
SEQRES 6 B 325 MET LEU LEU HIS GLY PHE PHE LEU HIS ASN HIS PHE TYR
SEQRES 7 B 325 GLU HIS LEU LEU ARG HIS VAL ALA SER HIS GLY PHE ILE
SEQRES 8 B 325 ILE VAL ALA PRO GLN PHE SER ILE SER ILE ILE PRO SER
SEQRES 9 B 325 GLY ASP ALA GLU ASP ILE ALA ALA ALA ALA LYS VAL ALA
SEQRES 10 B 325 ASP TRP LEU PRO ASP GLY LEU PRO SER VAL LEU PRO LYS
SEQRES 11 B 325 GLY VAL GLU PRO GLU LEU SER LYS LEU ALA LEU ALA GLY
SEQRES 12 B 325 HIS SER ARG GLY GLY HIS THR ALA PHE SER LEU ALA LEU
SEQRES 13 B 325 GLY HIS ALA LYS THR GLN LEU THR PHE SER ALA LEU ILE
SEQRES 14 B 325 GLY LEU ASP PRO VAL ALA GLY THR GLY LYS SER SER GLN
SEQRES 15 B 325 LEU GLN PRO LYS ILE LEU THR TYR GLU PRO SER SER PHE
SEQRES 16 B 325 GLY MET ALA MET PRO VAL LEU VAL ILE GLY THR GLY LEU
SEQRES 17 B 325 GLY GLU GLU LYS LYS ASN ILE PHE PHE PRO PRO CYS ALA
SEQRES 18 B 325 PRO LYS ASP VAL ASN HIS ALA GLU PHE TYR ARG GLU CYS
SEQRES 19 B 325 ARG PRO PRO CYS TYR TYR LEU VAL THR LYS ASP TYR GLY
SEQRES 20 B 325 HIS LEU ASP MET LEU ASP ASP ASP ALA PRO LYS PHE ILE
SEQRES 21 B 325 THR CYS VAL CYS LYS ASP GLY ASN GLY CYS LYS GLY LYS
SEQRES 22 B 325 MET ARG ARG CYS VAL ALA GLY ILE MET VAL ALA PHE LEU
SEQRES 23 B 325 ASN ALA ALA LEU GLY GLU LYS ASP ALA ASP LEU GLU ALA
SEQRES 24 B 325 ILE LEU ARG ASP PRO ALA VAL ALA PRO THR THR LEU ASP
SEQRES 25 B 325 PRO VAL GLU HIS ARG VAL ALA GLU ASN LEU TYR PHE GLN
HET CA A 401 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *15(H2 O)
HELIX 1 AA1 HIS A 74 PHE A 77 5 4
HELIX 2 AA2 TYR A 78 HIS A 88 1 11
HELIX 3 AA3 ASP A 106 LEU A 128 1 23
HELIX 4 AA4 SER A 145 GLY A 157 1 13
HELIX 5 AA5 ASN A 226 CYS A 234 1 9
HELIX 6 AA6 ILE A 260 CYS A 264 5 5
HELIX 7 AA7 CYS A 270 GLU A 292 1 23
HELIX 8 AA8 ALA A 295 ASP A 303 1 9
HELIX 9 AA9 PRO A 304 ALA A 307 5 4
HELIX 10 AB1 HIS B 74 PHE B 77 5 4
HELIX 11 AB2 TYR B 78 HIS B 88 1 11
HELIX 12 AB3 ASP B 106 LEU B 128 1 23
HELIX 13 AB4 SER B 145 LEU B 156 1 12
HELIX 14 AB5 LEU B 208 GLU B 210 5 3
HELIX 15 AB6 ASN B 226 GLU B 233 1 8
HELIX 16 AB7 PRO B 257 CYS B 262 1 6
HELIX 17 AB8 CYS B 270 ALA B 288 1 19
HELIX 18 AB9 ALA B 295 ASP B 303 1 9
HELIX 19 AC1 PRO B 304 ALA B 307 5 4
SHEET 1 AA1 9 VAL A 34 ILE A 37 0
SHEET 2 AA1 9 VAL A 51 PRO A 56 -1 O ILE A 53 N ILE A 37
SHEET 3 AA1 9 ILE A 91 PRO A 95 -1 O ILE A 92 N VAL A 54
SHEET 4 AA1 9 GLY A 60 LEU A 68 1 N ALA A 65 O VAL A 93
SHEET 5 AA1 9 VAL A 132 HIS A 144 1 O ALA A 142 N MET A 66
SHEET 6 AA1 9 LEU A 168 LEU A 171 1 O LEU A 171 N GLY A 143
SHEET 7 AA1 9 VAL A 201 THR A 206 1 O LEU A 202 N GLY A 170
SHEET 8 AA1 9 CYS A 238 THR A 243 1 O THR A 243 N GLY A 205
SHEET 9 AA1 9 LEU A 311 ARG A 317 -1 O ASP A 312 N VAL A 242
SHEET 1 AA2 2 GLY A 176 GLY A 178 0
SHEET 2 AA2 2 SER A 181 GLN A 182 -1 O SER A 181 N GLY A 178
SHEET 1 AA3 9 VAL B 34 VAL B 39 0
SHEET 2 AA3 9 VAL B 51 PRO B 56 -1 O ILE B 53 N ILE B 37
SHEET 3 AA3 9 ILE B 91 PRO B 95 -1 O ILE B 92 N VAL B 54
SHEET 4 AA3 9 GLY B 60 LEU B 68 1 N ALA B 65 O VAL B 93
SHEET 5 AA3 9 VAL B 132 HIS B 144 1 O ALA B 140 N MET B 66
SHEET 6 AA3 9 LEU B 168 LEU B 171 1 O LEU B 171 N GLY B 143
SHEET 7 AA3 9 VAL B 201 THR B 206 1 O LEU B 202 N GLY B 170
SHEET 8 AA3 9 CYS B 238 THR B 243 1 O THR B 243 N GLY B 205
SHEET 9 AA3 9 LEU B 311 ARG B 317 -1 O ASP B 312 N VAL B 242
SHEET 1 AA4 2 GLY B 176 GLY B 178 0
SHEET 2 AA4 2 SER B 181 GLN B 182 -1 O SER B 181 N GLY B 178
SSBOND 1 CYS A 220 CYS A 264 1555 1555 2.02
SSBOND 2 CYS A 270 CYS B 270 1555 1555 2.37
SSBOND 3 CYS B 220 CYS B 264 1555 1555 2.04
LINK OD1 ASP A 255 CA CA A 401 1555 1555 3.05
LINK OD2 ASP A 255 CA CA A 401 1555 1555 2.50
LINK CA CA A 401 O HOH A 501 1555 1555 2.28
LINK CA CA A 401 O HOH A 502 1555 1555 2.66
LINK CA CA A 401 OD1 ASP B 255 1555 1555 3.00
LINK CA CA A 401 OD2 ASP B 255 1555 1555 2.67
LINK CA CA A 401 O HOH B 401 1555 1555 2.55
LINK CA CA A 401 O HOH B 402 1555 1555 2.62
CISPEP 1 ALA A 44 PRO A 45 0 -5.49
CISPEP 2 GLN A 184 PRO A 185 0 11.74
CISPEP 3 PRO A 236 PRO A 237 0 -11.81
CISPEP 4 ASP A 312 PRO A 313 0 -8.95
CISPEP 5 ALA B 44 PRO B 45 0 -17.91
CISPEP 6 GLN B 184 PRO B 185 0 -25.89
CISPEP 7 PRO B 236 PRO B 237 0 9.40
CISPEP 8 ASP B 312 PRO B 313 0 11.19
CRYST1 197.520 197.520 96.830 90.00 90.00 120.00 P 65 2 2 24
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 0.005063 0.002923 0.000000 0.00000
SCALE2 0.000000 0.005846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010327 0.00000
TER 2246 GLU A 320
TER 4483 VAL B 318
MASTER 349 0 1 19 22 0 0 6 4497 2 16 50
END |