HEADER PROTEIN TRANSPORT 20-APR-07 2PM9
TITLE CRYSTAL STRUCTURE OF YEAST SEC13/31 VERTEX ELEMENT OF THE COPII
TITLE 2 VESICULAR COAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC31;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-411;
COMPND 5 SYNONYM: PROTEIN WEB1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC13;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: WEB1, SEC31;
SOURCE 6 EXPRESSION_SYSTEM: HI5 INSECT CELLS;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 10 ORGANISM_TAXID: 4932;
SOURCE 11 GENE: SEC13, ANU3;
SOURCE 12 EXPRESSION_SYSTEM: HI5 INSECT CELLS
KEYWDS BETA PROPELLER, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GOLDBERG,S.FATH,J.D.MANCIAS,X.BI
REVDAT 6 21-FEB-24 2PM9 1 REMARK
REVDAT 5 20-OCT-21 2PM9 1 SEQADV
REVDAT 4 18-OCT-17 2PM9 1 REMARK
REVDAT 3 24-FEB-09 2PM9 1 VERSN
REVDAT 2 17-JUL-07 2PM9 1 JRNL
REVDAT 1 03-JUL-07 2PM9 0
JRNL AUTH S.FATH,J.D.MANCIAS,X.BI,J.GOLDBERG
JRNL TITL STRUCTURE AND ORGANIZATION OF COAT PROTEINS IN THE COPII
JRNL TITL 2 CAGE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 129 1325 2007
JRNL REFN ISSN 0092-8674
JRNL PMID 17604721
JRNL DOI 10.1016/J.CELL.2007.05.036
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.9
REMARK 3 NUMBER OF REFLECTIONS : 18996
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 959
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.36
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 651
REMARK 3 BIN R VALUE (WORKING SET) : 0.4040
REMARK 3 BIN FREE R VALUE : 0.5240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5168
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.92600
REMARK 3 B22 (A**2) : -10.92600
REMARK 3 B33 (A**2) : 21.85100
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.636
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.025 ; 3.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.842 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.972 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.460 ; 4.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 28.75
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042532.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
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 : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20444
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : 0.34700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, RESOLVE 2.01
REMARK 200 STARTING MODEL: YEAST SEC13
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.1M TRI-SODIUM CITRATE,
REMARK 280 10MM MANGANESE CHLORIDE, PH 7.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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+3/4
REMARK 290 4555 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 29.93300
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 44.89950
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 14.96650
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 300 REMARK: THE BIOLOGICAL ASSEMBLY UNIT INVOLVES THIS STRUCTURE OF THE
REMARK 300 SEC13/31 VERTEX ELEMENT TOGETHER WITH THE SEC13/31 EDGE ELEMENT.
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: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 LYS A 3
REMARK 465 LEU A 4
REMARK 465 GLN A 340
REMARK 465 GLU A 341
REMARK 465 THR A 342
REMARK 465 GLU A 343
REMARK 465 THR A 344
REMARK 465 LYS A 345
REMARK 465 GLN A 346
REMARK 465 GLN A 347
REMARK 465 GLU A 348
REMARK 465 SER A 349
REMARK 465 GLU A 350
REMARK 465 THR A 351
REMARK 465 ASP A 352
REMARK 465 PHE A 353
REMARK 465 TRP A 354
REMARK 465 ASN A 355
REMARK 465 ASN A 356
REMARK 465 VAL A 357
REMARK 465 SER A 358
REMARK 465 ARG A 359
REMARK 465 GLU A 360
REMARK 465 GLU A 361
REMARK 465 GLY A 411
REMARK 465 MET B 1
REMARK 465 ILE B 158
REMARK 465 GLU B 159
REMARK 465 GLU B 160
REMARK 465 ASP B 161
REMARK 465 GLY B 162
REMARK 465 GLU B 163
REMARK 465 HIS B 164
REMARK 465 ASN B 165
REMARK 465 GLY B 166
REMARK 465 THR B 167
REMARK 465 LYS B 168
REMARK 465 GLY B 293
REMARK 465 GLU B 294
REMARK 465 VAL B 295
REMARK 465 HIS B 296
REMARK 465 GLN B 297
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 O VAL A 368 N HIS A 370 2.02
REMARK 500 O ASN A 73 N LYS A 75 2.11
REMARK 500 O HIS A 72 ND2 ASN A 74 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 PRO A 313 C - N - CA ANGL. DEV. = 9.6 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 PHE A 7 -143.45 -150.96
REMARK 500 ARG A 9 -161.75 -69.63
REMARK 500 THR A 10 122.09 -7.78
REMARK 500 ALA A 11 152.42 172.35
REMARK 500 SER A 16 -145.38 -75.23
REMARK 500 HIS A 17 23.59 -153.85
REMARK 500 ASP A 33 -161.33 -55.51
REMARK 500 THR A 38 -61.55 -136.41
REMARK 500 LEU A 42 36.44 71.69
REMARK 500 LEU A 48 -68.74 -98.87
REMARK 500 ALA A 49 150.19 -17.24
REMARK 500 ASP A 51 23.37 45.74
REMARK 500 SER A 52 50.45 26.12
REMARK 500 ALA A 57 116.64 -165.11
REMARK 500 LEU A 59 69.63 -168.53
REMARK 500 GLN A 60 135.41 -27.47
REMARK 500 ASP A 62 -72.17 -61.99
REMARK 500 HIS A 72 76.66 -65.61
REMARK 500 ASN A 73 -9.73 64.75
REMARK 500 ASN A 74 32.77 -54.09
REMARK 500 LYS A 75 56.06 37.71
REMARK 500 SER A 90 -59.34 -121.44
REMARK 500 THR A 91 106.49 64.14
REMARK 500 GLU A 93 106.16 94.43
REMARK 500 ALA A 94 134.11 -29.22
REMARK 500 ASN A 95 -13.67 85.45
REMARK 500 ALA A 97 122.03 -174.83
REMARK 500 MET A 101 -139.73 -98.74
REMARK 500 SER A 105 37.53 -173.41
REMARK 500 ASN A 106 7.33 -67.86
REMARK 500 SER A 109 68.73 23.71
REMARK 500 SER A 110 111.28 160.73
REMARK 500 LYS A 112 -63.80 -103.89
REMARK 500 ASP A 121 0.88 -55.12
REMARK 500 GLU A 143 -90.69 -37.63
REMARK 500 SER A 146 -54.63 -14.24
REMARK 500 ASN A 147 27.26 163.97
REMARK 500 TYR A 148 135.33 -27.98
REMARK 500 GLN A 155 149.43 178.46
REMARK 500 SER A 156 -97.89 58.47
REMARK 500 SER A 159 -72.40 172.79
REMARK 500 VAL A 160 9.42 -160.17
REMARK 500 LYS A 193 71.50 35.67
REMARK 500 LYS A 194 153.46 160.60
REMARK 500 SER A 200 110.20 -166.93
REMARK 500 THR A 202 0.53 -158.47
REMARK 500 PRO A 204 -14.18 -35.36
REMARK 500 PRO A 219 2.36 -67.53
REMARK 500 LYS A 220 -47.77 -144.60
REMARK 500 SER A 231 133.23 -36.60
REMARK 500
REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PM6 RELATED DB: PDB
REMARK 900 EDGE ELEMENT OF THE SEC13/31 COMPLEX, NATIVE PROTEIN
REMARK 900 RELATED ID: 2PM7 RELATED DB: PDB
REMARK 900 EDGE ELEMENT OF THE SEC13/31 COMPLEX, SELENOMETHIONINE PROTEIN
DBREF 2PM9 A 1 411 UNP P38968 WEB1_YEAST 1 411
DBREF 2PM9 B 1 297 UNP Q04491 SEC13_YEAST 1 297
SEQADV 2PM9 GLY A -4 UNP P38968 CLONING ARTIFACT
SEQADV 2PM9 ALA A -3 UNP P38968 CLONING ARTIFACT
SEQADV 2PM9 MET A -2 UNP P38968 CLONING ARTIFACT
SEQADV 2PM9 GLY A -1 UNP P38968 CLONING ARTIFACT
SEQADV 2PM9 SER A 0 UNP P38968 CLONING ARTIFACT
SEQADV 2PM9 MET B 11 UNP Q04491 LEU 11 ENGINEERED MUTATION
SEQADV 2PM9 MET B 17 UNP Q04491 LEU 17 ENGINEERED MUTATION
SEQADV 2PM9 MET B 24 UNP Q04491 LEU 24 ENGINEERED MUTATION
SEQADV 2PM9 MET B 80 UNP Q04491 LEU 80 ENGINEERED MUTATION
SEQADV 2PM9 MET B 115 UNP Q04491 LEU 115 ENGINEERED MUTATION
SEQADV 2PM9 MET B 222 UNP Q04491 LEU 222 ENGINEERED MUTATION
SEQRES 1 A 416 GLY ALA MET GLY SER MET VAL LYS LEU ALA GLU PHE SER
SEQRES 2 A 416 ARG THR ALA THR PHE ALA TRP SER HIS ASP LYS ILE PRO
SEQRES 3 A 416 LEU LEU VAL SER GLY THR VAL SER GLY THR VAL ASP ALA
SEQRES 4 A 416 ASN PHE SER THR ASP SER SER LEU GLU LEU TRP SER LEU
SEQRES 5 A 416 LEU ALA ALA ASP SER GLU LYS PRO ILE ALA SER LEU GLN
SEQRES 6 A 416 VAL ASP SER LYS PHE ASN ASP LEU ASP TRP SER HIS ASN
SEQRES 7 A 416 ASN LYS ILE ILE ALA GLY ALA LEU ASP ASN GLY SER LEU
SEQRES 8 A 416 GLU LEU TYR SER THR ASN GLU ALA ASN ASN ALA ILE ASN
SEQRES 9 A 416 SER MET ALA ARG PHE SER ASN HIS SER SER SER VAL LYS
SEQRES 10 A 416 THR VAL LYS PHE ASN ALA LYS GLN ASP ASN VAL LEU ALA
SEQRES 11 A 416 SER GLY GLY ASN ASN GLY GLU ILE PHE ILE TRP ASP MET
SEQRES 12 A 416 ASN LYS CYS THR GLU SER PRO SER ASN TYR THR PRO LEU
SEQRES 13 A 416 THR PRO GLY GLN SER MET SER SER VAL ASP GLU VAL ILE
SEQRES 14 A 416 SER LEU ALA TRP ASN GLN SER LEU ALA HIS VAL PHE ALA
SEQRES 15 A 416 SER ALA GLY SER SER ASN PHE ALA SER ILE TRP ASP LEU
SEQRES 16 A 416 LYS ALA LYS LYS GLU VAL ILE HIS LEU SER TYR THR SER
SEQRES 17 A 416 PRO ASN SER GLY ILE LYS GLN GLN LEU SER VAL VAL GLU
SEQRES 18 A 416 TRP HIS PRO LYS ASN SER THR ARG VAL ALA THR ALA THR
SEQRES 19 A 416 GLY SER ASP ASN ASP PRO SER ILE LEU ILE TRP ASP LEU
SEQRES 20 A 416 ARG ASN ALA ASN THR PRO LEU GLN THR LEU ASN GLN GLY
SEQRES 21 A 416 HIS GLN LYS GLY ILE LEU SER LEU ASP TRP CYS HIS GLN
SEQRES 22 A 416 ASP GLU HIS LEU LEU LEU SER SER GLY ARG ASP ASN THR
SEQRES 23 A 416 VAL LEU LEU TRP ASN PRO GLU SER ALA GLU GLN LEU SER
SEQRES 24 A 416 GLN PHE PRO ALA ARG GLY ASN TRP CYS PHE LYS THR LYS
SEQRES 25 A 416 PHE ALA PRO GLU ALA PRO ASP LEU PHE ALA CYS ALA SER
SEQRES 26 A 416 PHE ASP ASN LYS ILE GLU VAL GLN THR LEU GLN ASN LEU
SEQRES 27 A 416 THR ASN THR LEU ASP GLU GLN GLU THR GLU THR LYS GLN
SEQRES 28 A 416 GLN GLU SER GLU THR ASP PHE TRP ASN ASN VAL SER ARG
SEQRES 29 A 416 GLU GLU SER LYS GLU LYS PRO SER VAL PHE HIS LEU GLN
SEQRES 30 A 416 ALA PRO THR TRP TYR GLY GLU PRO SER PRO ALA ALA HIS
SEQRES 31 A 416 TRP ALA PHE GLY GLY LYS LEU VAL GLN ILE THR PRO ASP
SEQRES 32 A 416 GLY LYS GLY VAL SER ILE THR ASN PRO LYS ILE SER GLY
SEQRES 1 B 297 MET VAL VAL ILE ALA ASN ALA HIS ASN GLU MET ILE HIS
SEQRES 2 B 297 ASP ALA VAL MET ASP TYR TYR GLY LYS ARG MET ALA THR
SEQRES 3 B 297 CYS SER SER ASP LYS THR ILE LYS ILE PHE GLU VAL GLU
SEQRES 4 B 297 GLY GLU THR HIS LYS LEU ILE ASP THR LEU THR GLY HIS
SEQRES 5 B 297 GLU GLY PRO VAL TRP ARG VAL ASP TRP ALA HIS PRO LYS
SEQRES 6 B 297 PHE GLY THR ILE LEU ALA SER CYS SER TYR ASP GLY LYS
SEQRES 7 B 297 VAL MET ILE TRP LYS GLU GLU ASN GLY ARG TRP SER GLN
SEQRES 8 B 297 ILE ALA VAL HIS ALA VAL HIS SER ALA SER VAL ASN SER
SEQRES 9 B 297 VAL GLN TRP ALA PRO HIS GLU TYR GLY PRO MET LEU LEU
SEQRES 10 B 297 VAL ALA SER SER ASP GLY LYS VAL SER VAL VAL GLU PHE
SEQRES 11 B 297 LYS GLU ASN GLY THR THR SER PRO ILE ILE ILE ASP ALA
SEQRES 12 B 297 HIS ALA ILE GLY VAL ASN SER ALA SER TRP ALA PRO ALA
SEQRES 13 B 297 THR ILE GLU GLU ASP GLY GLU HIS ASN GLY THR LYS GLU
SEQRES 14 B 297 SER ARG LYS PHE VAL THR GLY GLY ALA ASP ASN LEU VAL
SEQRES 15 B 297 LYS ILE TRP LYS TYR ASN SER ASP ALA GLN THR TYR VAL
SEQRES 16 B 297 LEU GLU SER THR LEU GLU GLY HIS SER ASP TRP VAL ARG
SEQRES 17 B 297 ASP VAL ALA TRP SER PRO THR VAL LEU LEU ARG SER TYR
SEQRES 18 B 297 MET ALA SER VAL SER GLN ASP ARG THR CYS ILE ILE TRP
SEQRES 19 B 297 THR GLN ASP ASN GLU GLN GLY PRO TRP LYS LYS THR LEU
SEQRES 20 B 297 LEU LYS GLU GLU LYS PHE PRO ASP VAL LEU TRP ARG ALA
SEQRES 21 B 297 SER TRP SER LEU SER GLY ASN VAL LEU ALA LEU SER GLY
SEQRES 22 B 297 GLY ASP ASN LYS VAL THR LEU TRP LYS GLU ASN LEU GLU
SEQRES 23 B 297 GLY LYS TRP GLU PRO ALA GLY GLU VAL HIS GLN
FORMUL 3 HOH *28(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 HIS B 63 GLY B 67 5 5
HELIX 3 3 GLU B 85 ARG B 88 5 4
SHEET 1 A 4 GLU A 6 ARG A 9 0
SHEET 2 A 4 LYS A 324 THR A 329 -1 O ILE A 325 N SER A 8
SHEET 3 A 4 LEU A 315 CYS A 318 -1 N PHE A 316 O GLN A 328
SHEET 4 A 4 THR A 306 PHE A 308 -1 N LYS A 307 O ALA A 317
SHEET 1 B 2 LEU A 22 SER A 25 0
SHEET 2 B 2 GLU A 43 SER A 46 -1 O GLU A 43 N SER A 25
SHEET 1 C 4 PHE A 65 TRP A 70 0
SHEET 2 C 4 ILE A 77 LEU A 81 -1 O ALA A 80 N ASN A 66
SHEET 3 C 4 LEU A 86 TYR A 89 -1 O GLU A 87 N GLY A 79
SHEET 4 C 4 SER A 100 ARG A 103 -1 O ALA A 102 N LEU A 88
SHEET 1 D 3 THR A 113 PHE A 116 0
SHEET 2 D 3 LEU A 124 GLY A 127 -1 O ALA A 125 N LYS A 115
SHEET 3 D 3 ILE A 133 PHE A 134 -1 O PHE A 134 N SER A 126
SHEET 1 E 4 SER A 165 TRP A 168 0
SHEET 2 E 4 VAL A 175 ALA A 179 -1 O ALA A 177 N ALA A 167
SHEET 3 E 4 ALA A 185 ASP A 189 -1 O TRP A 188 N PHE A 176
SHEET 4 E 4 LYS A 194 LEU A 199 -1 O VAL A 196 N ILE A 187
SHEET 1 F 3 LEU A 212 TRP A 217 0
SHEET 2 F 3 ARG A 224 THR A 229 -1 O ALA A 226 N GLU A 216
SHEET 3 F 3 ILE A 239 ASP A 241 -1 O TRP A 240 N VAL A 225
SHEET 1 G 4 ILE A 260 TRP A 265 0
SHEET 2 G 4 LEU A 273 GLY A 277 -1 O LEU A 274 N ASP A 264
SHEET 3 G 4 THR A 281 TRP A 285 -1 O LEU A 283 N SER A 275
SHEET 4 G 4 GLN A 292 PRO A 297 -1 O PHE A 296 N VAL A 282
SHEET 1 H 2 HIS A 385 ALA A 387 0
SHEET 2 H 2 LYS A 391 VAL A 393 -1 O VAL A 393 N HIS A 385
SHEET 1 I 4 ILE B 12 ALA B 15 0
SHEET 2 I 4 ALA B 25 SER B 28 -1 O CYS B 27 N HIS B 13
SHEET 3 I 4 THR B 32 GLU B 39 -1 O LYS B 34 N THR B 26
SHEET 4 I 4 THR B 42 THR B 50 -1 N THR B 42 O GLU B 39
SHEET 1 J 4 VAL B 56 TRP B 61 0
SHEET 2 J 4 ILE B 69 SER B 74 -1 O CYS B 73 N TRP B 57
SHEET 3 J 4 VAL B 79 LYS B 83 -1 O MET B 80 N SER B 72
SHEET 4 J 4 SER B 90 HIS B 95 -1 O HIS B 95 N VAL B 79
SHEET 1 K 4 VAL B 102 TRP B 107 0
SHEET 2 K 4 MET B 115 SER B 120 -1 O LEU B 117 N GLN B 106
SHEET 3 K 4 LYS B 124 GLU B 129 -1 O SER B 126 N VAL B 118
SHEET 4 K 4 ILE B 139 ASP B 142 -1 O ILE B 139 N VAL B 127
SHEET 1 L 4 VAL B 148 SER B 150 0
SHEET 2 L 4 LYS B 172 GLY B 177 -1 O GLY B 176 N ASN B 149
SHEET 3 L 4 VAL B 182 LYS B 186 -1 O LYS B 183 N THR B 175
SHEET 4 L 4 VAL B 195 LEU B 196 -1 O VAL B 195 N LYS B 186
SHEET 1 M 3 ASP B 209 TRP B 212 0
SHEET 2 M 3 SER B 220 SER B 226 -1 O VAL B 225 N ASP B 209
SHEET 3 M 3 THR B 230 CYS B 231 -1 O THR B 230 N SER B 226
SHEET 1 N 3 ASP B 209 TRP B 212 0
SHEET 2 N 3 SER B 220 SER B 226 -1 O VAL B 225 N ASP B 209
SHEET 3 N 3 TRP B 234 GLN B 236 -1 O GLN B 236 N SER B 220
SHEET 1 O 3 ARG B 259 TRP B 262 0
SHEET 2 O 3 LEU B 269 SER B 272 -1 O ALA B 270 N SER B 261
SHEET 3 O 3 VAL B 278 TRP B 281 -1 O TRP B 281 N LEU B 269
CRYST1 155.163 155.163 59.866 90.00 90.00 90.00 P 43 4
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 0.006445 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016704 0.00000
(ATOM LINES ARE NOT SHOWN.)
END