HEADER TRANSPORT PROTEIN/UNKNOWN FUNCTION 10-JAN-17 5WY2
TITLE HUMAN SNX5 PX DOMAIN IN COMPLEX WITH CHLAMYDIA INCE C TERMINUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SORTING NEXIN-5;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 20-180;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INCE;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: UNP RESIDUES 111-131;
COMPND 10 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: SNX5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: CHLAMYDIA TRACHOMATIS;
SOURCE 12 ORGANISM_TAXID: 813
KEYWDS COMPLEX, INCE, PX DOMAIN, SNX5, TRANSPORT PROTEIN-UNKNOWN FUNCTION
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.SUN,X.YONG,D.JIA
REVDAT 3 22-NOV-23 5WY2 1 REMARK
REVDAT 2 25-DEC-19 5WY2 1 JRNL
REVDAT 1 22-NOV-17 5WY2 0
JRNL AUTH Q.SUN,X.YONG,X.SUN,F.YANG,Z.DAI,Y.GONG,L.ZHOU,X.ZHANG,D.NIU,
JRNL AUTH 2 L.DAI,J.J.LIU,D.JIA
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO SORTING NEXIN 5/6
JRNL TITL 2 INTERACTION WITH BACTERIAL EFFECTOR INCE.
JRNL REF SIGNAL TRANSDUCT TARGET THER V. 2 17030 2017
JRNL REFN ISSN 2095-9907
JRNL PMID 29263922
JRNL DOI 10.1038/SIGTRANS.2017.30
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 26308
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1347
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1807
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.95000
REMARK 3 B12 (A**2) : -0.24000
REMARK 3 B13 (A**2) : -0.22000
REMARK 3 B23 (A**2) : 0.31000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.376
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2715 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2513 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3671 ; 1.587 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5862 ; 0.950 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 5.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;37.966 ;24.462
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 481 ;16.090 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;19.642 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 411 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2954 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 540 ; 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): 1311 ; 1.664 ; 2.614
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1310 ; 1.664 ; 2.613
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1630 ; 2.864 ; 3.894
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1631 ; 2.863 ; 3.896
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1404 ; 1.488 ; 2.734
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1405 ; 1.487 ; 2.735
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2042 ; 2.487 ; 4.003
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3080 ; 5.240 ;30.811
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3079 ; 5.238 ;30.807
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 28 176 C 28 176 8826 0.09 0.05
REMARK 3 2 B 111 131 D 111 131 934 0.17 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 28 A 176
REMARK 3 RESIDUE RANGE : A 201 A 320
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9599 0.0301 0.1713
REMARK 3 T TENSOR
REMARK 3 T11: 0.0789 T22: 0.0710
REMARK 3 T33: 0.1080 T12: -0.0079
REMARK 3 T13: 0.0641 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 3.8461 L22: 3.9039
REMARK 3 L33: 4.3399 L12: 0.5638
REMARK 3 L13: -1.5067 L23: 0.7186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0331 S12: -0.3617 S13: -0.1797
REMARK 3 S21: 0.5305 S22: -0.1063 S23: 0.3021
REMARK 3 S31: 0.0536 S32: -0.2161 S33: 0.0732
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 111 B 131
REMARK 3 RESIDUE RANGE : B 201 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4293 4.4561 14.8108
REMARK 3 T TENSOR
REMARK 3 T11: 0.1724 T22: 0.1719
REMARK 3 T33: 0.0731 T12: -0.0040
REMARK 3 T13: 0.0101 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 9.2764 L22: 2.5502
REMARK 3 L33: 0.5955 L12: 0.5360
REMARK 3 L13: -1.1282 L23: 0.1802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: -0.1698 S13: 0.1678
REMARK 3 S21: 0.0592 S22: -0.0286 S23: -0.0499
REMARK 3 S31: 0.0287 S32: 0.0051 S33: 0.0456
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 28 C 176
REMARK 3 RESIDUE RANGE : C 201 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5625 -17.4593 -26.8872
REMARK 3 T TENSOR
REMARK 3 T11: 0.1649 T22: 0.0542
REMARK 3 T33: 0.1464 T12: -0.0052
REMARK 3 T13: 0.0428 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 3.1934 L22: 3.4082
REMARK 3 L33: 5.1149 L12: -0.2265
REMARK 3 L13: 1.7846 L23: 0.8379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: 0.2717 S13: 0.0674
REMARK 3 S21: -0.6062 S22: -0.1410 S23: 0.2157
REMARK 3 S31: -0.1045 S32: -0.1782 S33: 0.1983
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 111 D 131
REMARK 3 RESIDUE RANGE : D 201 D 205
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1853 -22.2012 -39.9294
REMARK 3 T TENSOR
REMARK 3 T11: 0.2877 T22: 0.2209
REMARK 3 T33: 0.0798 T12: 0.0187
REMARK 3 T13: 0.0111 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 14.5931 L22: 5.3889
REMARK 3 L33: 3.2004 L12: -1.5147
REMARK 3 L13: 2.5334 L23: -0.4159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: 0.6571 S13: -0.4801
REMARK 3 S21: -0.0803 S22: -0.0190 S23: -0.1376
REMARK 3 S31: -0.0474 S32: 0.0868 S33: -0.0011
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
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
REMARK 4
REMARK 4 5WY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1300002570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-15
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 : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NONIUS KAPPA CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27655
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.85900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3HPC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M SODIUM
REMARK 280 ACETATE PH 4.6, 30% W/V POLYETHYLENE GLYCOL 4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 GLY A 18
REMARK 465 GLY A 19
REMARK 465 SER A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 ASP A 24
REMARK 465 LEU A 25
REMARK 465 ASN A 26
REMARK 465 VAL A 27
REMARK 465 GLY A 110
REMARK 465 GLU A 111
REMARK 465 GLY A 112
REMARK 465 GLU A 113
REMARK 465 GLY A 114
REMARK 465 SER A 115
REMARK 465 MET A 116
REMARK 465 THR A 117
REMARK 465 LYS A 118
REMARK 465 GLU A 119
REMARK 465 GLU A 120
REMARK 465 LYS A 177
REMARK 465 ASN A 178
REMARK 465 THR A 179
REMARK 465 LYS A 180
REMARK 465 GLY C 18
REMARK 465 GLY C 19
REMARK 465 SER C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 VAL C 23
REMARK 465 ASP C 24
REMARK 465 LEU C 25
REMARK 465 ASN C 26
REMARK 465 VAL C 27
REMARK 465 LYS C 177
REMARK 465 ASN C 178
REMARK 465 THR C 179
REMARK 465 LYS C 180
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 149 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 176 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ARG A 42 -108.97 46.30
REMARK 500 ASP A 169 49.70 -95.69
REMARK 500 LYS B 120 -106.88 91.85
REMARK 500 ASN B 121 -72.11 -86.63
REMARK 500 ARG C 42 -107.91 49.28
REMARK 500 ASP C 169 57.57 -100.72
REMARK 500 SER C 173 -71.52 -24.51
REMARK 500 ASN D 121 -84.45 47.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5WY2 A 20 180 UNP Q9Y5X3 SNX5_HUMAN 20 180
DBREF 5WY2 B 111 131 UNP B7SCI5 B7SCI5_CHLTH 111 131
DBREF 5WY2 C 20 180 UNP Q9Y5X3 SNX5_HUMAN 20 180
DBREF 5WY2 D 111 131 UNP B7SCI5 B7SCI5_CHLTH 111 131
SEQADV 5WY2 GLY A 18 UNP Q9Y5X3 EXPRESSION TAG
SEQADV 5WY2 GLY A 19 UNP Q9Y5X3 EXPRESSION TAG
SEQADV 5WY2 SER A 56 UNP Q9Y5X3 PRO 56 CONFLICT
SEQADV 5WY2 THR A 80 UNP Q9Y5X3 ILE 80 CONFLICT
SEQADV 5WY2 THR A 142 UNP Q9Y5X3 SER 142 CONFLICT
SEQADV 5WY2 GLY C 18 UNP Q9Y5X3 EXPRESSION TAG
SEQADV 5WY2 GLY C 19 UNP Q9Y5X3 EXPRESSION TAG
SEQADV 5WY2 SER C 56 UNP Q9Y5X3 PRO 56 CONFLICT
SEQADV 5WY2 THR C 80 UNP Q9Y5X3 ILE 80 CONFLICT
SEQADV 5WY2 THR C 142 UNP Q9Y5X3 SER 142 CONFLICT
SEQRES 1 A 163 GLY GLY SER VAL SER VAL ASP LEU ASN VAL ASP PRO SER
SEQRES 2 A 163 LEU GLN ILE ASP ILE PRO ASP ALA LEU SER GLU ARG ASP
SEQRES 3 A 163 LYS VAL LYS PHE THR VAL HIS THR LYS THR THR LEU SER
SEQRES 4 A 163 THR PHE GLN SER PRO GLU PHE SER VAL THR ARG GLN HIS
SEQRES 5 A 163 GLU ASP PHE VAL TRP LEU HIS ASP THR LEU THR GLU THR
SEQRES 6 A 163 THR ASP TYR ALA GLY LEU ILE ILE PRO PRO ALA PRO THR
SEQRES 7 A 163 LYS PRO ASP PHE ASP GLY PRO ARG GLU LYS MET GLN LYS
SEQRES 8 A 163 LEU GLY GLU GLY GLU GLY SER MET THR LYS GLU GLU PHE
SEQRES 9 A 163 ALA LYS MET LYS GLN GLU LEU GLU ALA GLU TYR LEU ALA
SEQRES 10 A 163 VAL PHE LYS LYS THR VAL SER THR HIS GLU VAL PHE LEU
SEQRES 11 A 163 GLN ARG LEU SER SER HIS PRO VAL LEU SER LYS ASP ARG
SEQRES 12 A 163 ASN PHE HIS VAL PHE LEU GLU TYR ASP GLN ASP LEU SER
SEQRES 13 A 163 VAL ARG ARG LYS ASN THR LYS
SEQRES 1 B 21 GLY PRO ALA VAL GLN PHE PHE LYS GLY LYS ASN GLY SER
SEQRES 2 B 21 ALA ASP GLN VAL ILE LEU VAL THR
SEQRES 1 C 163 GLY GLY SER VAL SER VAL ASP LEU ASN VAL ASP PRO SER
SEQRES 2 C 163 LEU GLN ILE ASP ILE PRO ASP ALA LEU SER GLU ARG ASP
SEQRES 3 C 163 LYS VAL LYS PHE THR VAL HIS THR LYS THR THR LEU SER
SEQRES 4 C 163 THR PHE GLN SER PRO GLU PHE SER VAL THR ARG GLN HIS
SEQRES 5 C 163 GLU ASP PHE VAL TRP LEU HIS ASP THR LEU THR GLU THR
SEQRES 6 C 163 THR ASP TYR ALA GLY LEU ILE ILE PRO PRO ALA PRO THR
SEQRES 7 C 163 LYS PRO ASP PHE ASP GLY PRO ARG GLU LYS MET GLN LYS
SEQRES 8 C 163 LEU GLY GLU GLY GLU GLY SER MET THR LYS GLU GLU PHE
SEQRES 9 C 163 ALA LYS MET LYS GLN GLU LEU GLU ALA GLU TYR LEU ALA
SEQRES 10 C 163 VAL PHE LYS LYS THR VAL SER THR HIS GLU VAL PHE LEU
SEQRES 11 C 163 GLN ARG LEU SER SER HIS PRO VAL LEU SER LYS ASP ARG
SEQRES 12 C 163 ASN PHE HIS VAL PHE LEU GLU TYR ASP GLN ASP LEU SER
SEQRES 13 C 163 VAL ARG ARG LYS ASN THR LYS
SEQRES 1 D 21 GLY PRO ALA VAL GLN PHE PHE LYS GLY LYS ASN GLY SER
SEQRES 2 D 21 ALA ASP GLN VAL ILE LEU VAL THR
FORMUL 5 HOH *245(H2 O)
HELIX 1 AA1 HIS A 69 GLU A 81 1 13
HELIX 2 AA2 THR A 82 ALA A 86 5 5
HELIX 3 AA3 PHE A 99 LEU A 109 1 11
HELIX 4 AA4 ALA A 122 HIS A 153 1 32
HELIX 5 AA5 VAL A 155 LYS A 158 5 4
HELIX 6 AA6 ASP A 159 TYR A 168 1 10
HELIX 7 AA7 ASP A 171 ARG A 176 1 6
HELIX 8 AA8 HIS C 69 GLU C 81 1 13
HELIX 9 AA9 THR C 82 ALA C 86 5 5
HELIX 10 AB1 PHE C 99 GLY C 112 1 14
HELIX 11 AB2 GLU C 113 SER C 115 5 3
HELIX 12 AB3 THR C 117 SER C 152 1 36
HELIX 13 AB4 VAL C 155 LYS C 158 5 4
HELIX 14 AB5 ASP C 159 TYR C 168 1 10
SHEET 1 AA1 3 LEU A 31 ASP A 34 0
SHEET 2 AA1 3 LYS A 44 THR A 53 -1 O HIS A 50 N ASP A 34
SHEET 3 AA1 3 GLU A 62 GLN A 68 -1 O ARG A 67 N PHE A 47
SHEET 1 AA2 5 LEU A 31 ASP A 34 0
SHEET 2 AA2 5 LYS A 44 THR A 53 -1 O HIS A 50 N ASP A 34
SHEET 3 AA2 5 ASP A 37 GLU A 41 -1 N LEU A 39 O LYS A 46
SHEET 4 AA2 5 ALA B 113 PHE B 117 -1 O PHE B 116 N ALA A 38
SHEET 5 AA2 5 GLN B 126 VAL B 130 -1 O VAL B 130 N ALA B 113
SHEET 1 AA3 3 LEU C 31 ASP C 34 0
SHEET 2 AA3 3 LYS C 44 THR C 53 -1 O HIS C 50 N ASP C 34
SHEET 3 AA3 3 GLU C 62 GLN C 68 -1 O ARG C 67 N PHE C 47
SHEET 1 AA4 5 LEU C 31 ASP C 34 0
SHEET 2 AA4 5 LYS C 44 THR C 53 -1 O HIS C 50 N ASP C 34
SHEET 3 AA4 5 ASP C 37 GLU C 41 -1 N GLU C 41 O LYS C 44
SHEET 4 AA4 5 ALA D 113 PHE D 117 -1 O PHE D 116 N ALA C 38
SHEET 5 AA4 5 GLN D 126 VAL D 130 -1 O VAL D 130 N ALA D 113
CRYST1 37.443 43.711 60.070 94.79 99.81 100.97 P 1 2
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 0.026707 0.005179 0.005276 0.00000
SCALE2 0.000000 0.023304 0.002813 0.00000
SCALE3 0.000000 0.000000 0.017017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
