HEADER ALLERGEN 18-DEC-12 4IH0
TITLE CRYSTAL STRUCTURE OF KIROLA (ACT D 11) FROM CRYSTAL SOAKED WITH
TITLE 2 SEROTONIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIROLA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACT D 11
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINIDIA DELICIOSA;
SOURCE 3 ORGANISM_COMMON: CHINESE GOOSEBERRY,KIWIFRUIT;
SOURCE 4 ORGANISM_TAXID: 3627
KEYWDS MLP/RRP FAMILY, PR-10 RELATED, ALLERGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CHRUSZCZ,M.A.CIARDIELLO,I.GIANGRIECO,T.OSINSKI,W.MINOR
REVDAT 3 20-SEP-23 4IH0 1 REMARK
REVDAT 2 13-APR-22 4IH0 1 AUTHOR JRNL REMARK LINK
REVDAT 1 04-SEP-13 4IH0 0
JRNL AUTH M.CHRUSZCZ,M.A.CIARDIELLO,T.OSINSKI,K.A.MAJOREK,
JRNL AUTH 2 I.GIANGRIECO,J.FONT,H.BREITENEDER,K.THALASSINOS,W.MINOR
JRNL TITL STRUCTURAL AND BIOINFORMATIC ANALYSIS OF THE KIWIFRUIT
JRNL TITL 2 ALLERGEN ACT D 11, A MEMBER OF THE FAMILY OF
JRNL TITL 3 RIPENING-RELATED PROTEINS.
JRNL REF MOL.IMMUNOL. V. 56 794 2013
JRNL REFN ISSN 0161-5890
JRNL PMID 23969108
JRNL DOI 10.1016/J.MOLIMM.2013.07.004
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 16611
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 891
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1069
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1790
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.2140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.16000
REMARK 3 B22 (A**2) : 1.16000
REMARK 3 B33 (A**2) : -1.75000
REMARK 3 B12 (A**2) : 0.58000
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): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.241
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
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): 1270 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 832 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1727 ; 1.704 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2054 ; 0.971 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 156 ; 5.644 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 57 ;34.013 ;25.439
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 235 ;13.371 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;11.791 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 200 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1401 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 257 ; 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): 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 : 1
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 2 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3100 -23.1000 -14.5410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0241 T22: 0.0519
REMARK 3 T33: 0.0345 T12: 0.0039
REMARK 3 T13: -0.0211 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.3361 L22: 1.0140
REMARK 3 L33: 1.8435 L12: -0.0498
REMARK 3 L13: -0.2121 L23: -0.3425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0342 S12: -0.0817 S13: -0.0481
REMARK 3 S21: -0.0009 S22: -0.0757 S23: -0.0663
REMARK 3 S31: 0.0451 S32: 0.0746 S33: 0.0415
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4IH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.9793
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL SI(111)
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-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17592
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 44.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
REMARK 200 R SYM FOR SHELL (I) : 0.64100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4IGV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M CITRIC ACID, 0.35 M MAGNESIUM
REMARK 280 CHLORIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
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 57.01200
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 57.01200
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 57.01200
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 0.00000
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 0.00000
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 57.01200
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 57.01200
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 57.01200
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 CL CL A 205 LIES ON A SPECIAL POSITION.
REMARK 375 MG MG A 208 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 407 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 419 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 437 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 MET A 1
REMARK 465 ASP A 16
REMARK 465 LYS A 108
REMARK 465 GLY A 109
REMARK 465 LYS A 150
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 ASP A 2 CG OD1 OD2
REMARK 470 SER A 15 OG
REMARK 470 GLU A 125 CG CD OE1 OE2
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 MG A 206 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 378 O
REMARK 620 2 HOH A 379 O 97.0
REMARK 620 3 HOH A 380 O 173.9 88.3
REMARK 620 4 HOH A 381 O 90.8 92.2 86.0
REMARK 620 5 HOH A 382 O 94.8 90.8 88.1 173.2
REMARK 620 6 HOH A 383 O 89.1 173.1 85.4 84.4 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 208 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 396 O
REMARK 620 2 HOH A 397 O 108.5
REMARK 620 3 HOH A 427 O 91.0 93.2
REMARK 620 4 HOH A 438 O 174.2 76.2 85.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 208
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IGV RELATED DB: PDB
REMARK 900 RELATED ID: 4IGW RELATED DB: PDB
REMARK 900 RELATED ID: 4IGX RELATED DB: PDB
REMARK 900 RELATED ID: 4IGY RELATED DB: PDB
REMARK 900 RELATED ID: 4IH2 RELATED DB: PDB
REMARK 900 RELATED ID: 4IHR RELATED DB: PDB
DBREF 4IH0 A 1 150 UNP P85524 KIRO_ACTDE 1 150
SEQRES 1 A 150 MET ASP LEU SER GLY LYS MET VAL LYS GLN VAL GLU ILE
SEQRES 2 A 150 LEU SER ASP GLY ILE VAL PHE TYR GLU ILE PHE ARG TYR
SEQRES 3 A 150 ARG LEU TYR LEU ILE SER GLU MET SER PRO VAL ASN ILE
SEQRES 4 A 150 GLN GLY VAL ASP LEU LEU GLU GLY ASN TRP GLY THR VAL
SEQRES 5 A 150 GLY SER VAL ILE PHE PHE LYS TYR THR ILE ASP GLY LYS
SEQRES 6 A 150 GLU LYS THR ALA LYS ASP ILE VAL GLU ALA ILE ASP GLU
SEQRES 7 A 150 GLU THR LYS SER VAL THR PHE LYS ILE VAL GLU GLY ASP
SEQRES 8 A 150 LEU MET GLU LEU TYR LYS THR PHE ILE ILE ILE VAL GLN
SEQRES 9 A 150 VAL ASP THR LYS GLY GLU HIS ASN SER VAL THR TRP THR
SEQRES 10 A 150 PHE HIS TYR GLU LYS LEU LYS GLU ASP VAL GLU GLU PRO
SEQRES 11 A 150 ASN THR LEU MET ASN PHE CYS ILE GLU ILE THR LYS ASP
SEQRES 12 A 150 ILE GLU THR TYR HIS LEU LYS
HET UNL A 201 1
HET UNL A 202 1
HET UNL A 203 1
HET UNL A 204 1
HET CL A 205 1
HET MG A 206 1
HET CL A 207 1
HET MG A 208 1
HETNAM UNL UNKNOWN LIGAND
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 6 CL 2(CL 1-)
FORMUL 7 MG 2(MG 2+)
FORMUL 10 HOH *139(H2 O)
HELIX 1 1 ILE A 18 TYR A 26 1 9
HELIX 2 2 TYR A 29 SER A 35 1 7
HELIX 3 3 LEU A 92 GLU A 94 5 3
HELIX 4 4 PRO A 130 THR A 146 1 17
SHEET 1 A 7 SER A 4 GLU A 12 0
SHEET 2 A 7 SER A 113 LYS A 122 -1 O TRP A 116 N LYS A 9
SHEET 3 A 7 TYR A 96 ASP A 106 -1 N GLN A 104 O THR A 115
SHEET 4 A 7 SER A 82 GLY A 90 -1 N PHE A 85 O ILE A 101
SHEET 5 A 7 LYS A 65 ASP A 77 -1 N LYS A 70 O VAL A 88
SHEET 6 A 7 VAL A 55 ILE A 62 -1 N PHE A 58 O ALA A 69
SHEET 7 A 7 ILE A 39 GLU A 46 -1 N LEU A 45 O VAL A 55
LINK MG MG A 206 O HOH A 378 1555 1555 2.05
LINK MG MG A 206 O HOH A 379 1555 1555 2.16
LINK MG MG A 206 O HOH A 380 1555 1555 2.40
LINK MG MG A 206 O HOH A 381 1555 1555 2.09
LINK MG MG A 206 O HOH A 382 1555 1555 2.02
LINK MG MG A 206 O HOH A 383 1555 1555 2.08
LINK MG MG A 208 O HOH A 396 1555 1555 2.14
LINK MG MG A 208 O HOH A 397 1555 1555 2.24
LINK MG MG A 208 O HOH A 427 1555 1555 1.95
LINK MG MG A 208 O HOH A 438 1555 1555 2.10
SITE 1 AC1 1 VAL A 52
SITE 1 AC2 6 HOH A 378 HOH A 379 HOH A 380 HOH A 381
SITE 2 AC2 6 HOH A 382 HOH A 383
SITE 1 AC3 3 SER A 82 THR A 84 HOH A 397
SITE 1 AC4 4 HOH A 396 HOH A 397 HOH A 427 HOH A 438
CRYST1 70.808 70.808 114.024 90.00 90.00 120.00 P 63 2 2 12
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 0.014123 0.008154 0.000000 0.00000
SCALE2 0.000000 0.016307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008770 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
