HEADER CHAPERONE/PROTEIN TRANSPORT 04-FEB-11 3QML
TITLE THE STRUCTURAL ANALYSIS OF SIL1-BIP COMPLEX REVEALS THE MECHANISM FOR
TITLE 2 SIL1 TO FUNCTION AS A NOVEL NUCLEOTIDE EXCHANGE FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 78 KDA GLUCOSE-REGULATED PROTEIN HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 43-426;
COMPND 5 SYNONYM: GRP-78, IMMUNOGLOBULIN HEAVY CHAIN-BINDING PROTEIN HOMOLOG,
COMPND 6 BIP;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NUCLEOTIDE EXCHANGE FACTOR SIL1;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: UNP RESIDUES 113-421;
COMPND 12 SYNONYM: PROTEIN SLS1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: KAR2, GRP78, SSD1, YJL034W, J1248;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 10 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 11 ORGANISM_TAXID: 4932;
SOURCE 12 GENE: SIL1, PER100, SLS1, YOL031C;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ARMADILLO LIKE REPEATS, CHAPERONE-PROTEIN TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YAN,J.Z.LI,B.D.SHA
REVDAT 3 21-FEB-24 3QML 1 REMARK SEQADV
REVDAT 2 07-SEP-11 3QML 1 JRNL VERSN
REVDAT 1 29-JUN-11 3QML 0
JRNL AUTH M.YAN,J.LI,B.SHA
JRNL TITL STRUCTURAL ANALYSIS OF THE SIL1-BIP COMPLEX REVEALS THE
JRNL TITL 2 MECHANISM FOR SIL1 TO FUNCTION AS A NUCLEOTIDE-EXCHANGE
JRNL TITL 3 FACTOR.
JRNL REF BIOCHEM.J. V. 438 447 2011
JRNL REFN ISSN 0264-6021
JRNL PMID 21675960
JRNL DOI 10.1042/BJ20110500
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_351)
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 60106
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3052
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 46.1385 - 4.9800 1.00 6552 351 0.1878 0.2301
REMARK 3 2 4.9800 - 3.9535 0.99 6282 335 0.1692 0.2176
REMARK 3 3 3.9535 - 3.4539 0.99 6191 325 0.1923 0.2570
REMARK 3 4 3.4539 - 3.1382 0.99 6169 296 0.2340 0.3107
REMARK 3 5 3.1382 - 2.9133 0.96 5933 340 0.2377 0.3170
REMARK 3 6 2.9133 - 2.7416 0.92 5678 322 0.2405 0.3305
REMARK 3 7 2.7416 - 2.6043 0.88 5433 300 0.2483 0.3447
REMARK 3 8 2.6043 - 2.4909 0.84 5221 261 0.2461 0.3112
REMARK 3 9 2.4909 - 2.3950 0.82 5032 260 0.2537 0.3287
REMARK 3 10 2.3950 - 2.3124 0.75 4563 262 0.2858 0.3596
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 : 0.35
REMARK 3 B_SOL : 58.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.21510
REMARK 3 B22 (A**2) : 6.44100
REMARK 3 B33 (A**2) : 1.77420
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 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 : 0.008 10306
REMARK 3 ANGLE : 1.098 13897
REMARK 3 CHIRALITY : 0.072 1594
REMARK 3 PLANARITY : 0.004 1792
REMARK 3 DIHEDRAL : 16.306 3882
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 48:424)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8683 65.9293 62.6351
REMARK 3 T TENSOR
REMARK 3 T11: 0.2064 T22: 0.1880
REMARK 3 T33: 0.1274 T12: -0.0210
REMARK 3 T13: 0.0141 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.8132 L22: 1.1129
REMARK 3 L33: 0.6875 L12: 0.0129
REMARK 3 L13: 0.3879 L23: 0.8714
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: 0.0786 S13: -0.0121
REMARK 3 S21: 0.0539 S22: 0.0397 S23: 0.0145
REMARK 3 S31: 0.0318 S32: 0.0161 S33: -0.0089
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 48:425)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6022 27.7568 35.5221
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.4500
REMARK 3 T33: 0.3606 T12: 0.1489
REMARK 3 T13: -0.0370 T23: -0.1718
REMARK 3 L TENSOR
REMARK 3 L11: 6.7224 L22: 0.3176
REMARK 3 L33: 1.8612 L12: -0.4507
REMARK 3 L13: 3.5445 L23: -0.5058
REMARK 3 S TENSOR
REMARK 3 S11: 0.4922 S12: 1.5482 S13: -0.7450
REMARK 3 S21: -0.0892 S22: -0.0493 S23: 0.1556
REMARK 3 S31: 0.1603 S32: 0.8126 S33: -0.4282
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 122:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9314 97.8481 77.9030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2971 T22: 0.2235
REMARK 3 T33: 0.2858 T12: -0.0000
REMARK 3 T13: -0.0308 T23: -0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 1.6794 L22: 1.1971
REMARK 3 L33: 1.7622 L12: 0.6399
REMARK 3 L13: 1.1332 L23: 0.2111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: -0.0291 S13: 0.1388
REMARK 3 S21: -0.1131 S22: 0.0370 S23: 0.1470
REMARK 3 S31: -0.1657 S32: 0.0485 S33: 0.0073
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 125:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5033 22.5269 48.8011
REMARK 3 T TENSOR
REMARK 3 T11: 0.2955 T22: 0.3095
REMARK 3 T33: 0.1963 T12: 0.0813
REMARK 3 T13: 0.0142 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 3.2508 L22: 2.3077
REMARK 3 L33: 0.8581 L12: -1.6358
REMARK 3 L13: -0.9978 L23: -0.4941
REMARK 3 S TENSOR
REMARK 3 S11: 0.4873 S12: 0.4675 S13: -0.2365
REMARK 3 S21: -0.1123 S22: -0.2941 S23: 0.0694
REMARK 3 S31: -0.0750 S32: -0.1755 S33: -0.0734
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 3QML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9780
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60106
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.71000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES BUFFER, 25% (W/V) PEG4K,
REMARK 280 0.2 M AMMONIUM SULFATE, PH 7.0, EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 113.17650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.29300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 113.17650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.29300
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, 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 37
REMARK 465 MET A 38
REMARK 465 SER A 39
REMARK 465 HIS A 40
REMARK 465 ALA A 41
REMARK 465 SER A 42
REMARK 465 ALA A 43
REMARK 465 ASP A 44
REMARK 465 ASP A 45
REMARK 465 VAL A 46
REMARK 465 GLU A 47
REMARK 465 LEU A 425
REMARK 465 SER A 426
REMARK 465 GLY B 37
REMARK 465 MET B 38
REMARK 465 SER B 39
REMARK 465 HIS B 40
REMARK 465 ALA B 41
REMARK 465 SER B 42
REMARK 465 ALA B 43
REMARK 465 ASP B 44
REMARK 465 ASP B 45
REMARK 465 VAL B 46
REMARK 465 GLU B 47
REMARK 465 ASN B 48
REMARK 465 TYR B 49
REMARK 465 LYS B 233
REMARK 465 SER B 234
REMARK 465 ASP B 235
REMARK 465 LYS B 236
REMARK 465 GLU B 237
REMARK 465 HIS B 238
REMARK 465 SER B 426
REMARK 465 GLY C 107
REMARK 465 MET C 108
REMARK 465 SER C 109
REMARK 465 HIS C 110
REMARK 465 ALA C 111
REMARK 465 SER C 112
REMARK 465 SER C 113
REMARK 465 SER C 114
REMARK 465 GLU C 115
REMARK 465 ASP C 116
REMARK 465 MET C 117
REMARK 465 LYS C 118
REMARK 465 ALA C 119
REMARK 465 SER C 120
REMARK 465 PRO C 121
REMARK 465 ASN C 236
REMARK 465 HIS C 237
REMARK 465 PRO C 262
REMARK 465 ILE C 263
REMARK 465 ASN C 301
REMARK 465 ASP C 302
REMARK 465 ASP C 303
REMARK 465 THR C 304
REMARK 465 ASN C 305
REMARK 465 LEU C 306
REMARK 465 ILE C 307
REMARK 465 LEU C 308
REMARK 465 PHE C 309
REMARK 465 LYS C 310
REMARK 465 ARG C 311
REMARK 465 ASN C 312
REMARK 465 ALA C 313
REMARK 465 GLU C 314
REMARK 465 ASN C 315
REMARK 465 TRP C 316
REMARK 465 SER C 317
REMARK 465 SER C 318
REMARK 465 ASN C 319
REMARK 465 GLY C 407
REMARK 465 ASN C 408
REMARK 465 PRO C 409
REMARK 465 MET C 410
REMARK 465 ALA C 411
REMARK 465 HIS C 412
REMARK 465 ARG C 413
REMARK 465 ILE C 414
REMARK 465 LYS C 415
REMARK 465 ASN C 416
REMARK 465 PHE C 417
REMARK 465 ARG C 418
REMARK 465 ASP C 419
REMARK 465 GLU C 420
REMARK 465 LEU C 421
REMARK 465 GLY D 107
REMARK 465 MET D 108
REMARK 465 SER D 109
REMARK 465 HIS D 110
REMARK 465 ALA D 111
REMARK 465 SER D 112
REMARK 465 SER D 113
REMARK 465 SER D 114
REMARK 465 GLU D 115
REMARK 465 ASP D 116
REMARK 465 MET D 117
REMARK 465 LYS D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 PRO D 121
REMARK 465 GLY D 122
REMARK 465 ASP D 123
REMARK 465 TYR D 124
REMARK 465 ASN D 236
REMARK 465 HIS D 237
REMARK 465 ARG D 238
REMARK 465 TYR D 299
REMARK 465 GLU D 300
REMARK 465 ASN D 301
REMARK 465 ASP D 302
REMARK 465 ASP D 303
REMARK 465 THR D 304
REMARK 465 GLY D 407
REMARK 465 ASN D 408
REMARK 465 PRO D 409
REMARK 465 MET D 410
REMARK 465 ALA D 411
REMARK 465 HIS D 412
REMARK 465 ARG D 413
REMARK 465 ILE D 414
REMARK 465 LYS D 415
REMARK 465 ASN D 416
REMARK 465 PHE D 417
REMARK 465 ARG D 418
REMARK 465 ASP D 419
REMARK 465 GLU D 420
REMARK 465 LEU D 421
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 ND2 ASN D 233 ND2 ASN D 271 2.12
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 ASN A 108 46.17 -144.16
REMARK 500 PRO A 109 2.75 -67.83
REMARK 500 LYS A 154 133.41 -172.12
REMARK 500 LEU A 231 4.85 -68.73
REMARK 500 ASP A 235 64.64 71.67
REMARK 500 LYS A 236 145.44 69.60
REMARK 500 ASN A 259 -12.41 63.51
REMARK 500 PHE A 399 33.05 -97.77
REMARK 500 GLN B 79 9.46 179.43
REMARK 500 THR B 91 -165.85 -124.85
REMARK 500 GLU B 94 -159.15 178.57
REMARK 500 LEU B 213 174.00 156.92
REMARK 500 LEU B 255 93.60 -160.38
REMARK 500 ASN B 259 -94.34 53.17
REMARK 500 SER B 321 -33.93 -156.09
REMARK 500 LEU B 352 -70.77 -59.17
REMARK 500 ASP B 368 27.63 -76.89
REMARK 500 SER B 369 -0.89 -153.03
REMARK 500 LEU B 371 152.69 175.62
REMARK 500 VAL B 376 96.31 -53.35
REMARK 500 SER B 385 -7.13 -55.03
REMARK 500 PHE B 399 39.40 -81.91
REMARK 500 ASP B 400 -21.92 71.09
REMARK 500 ASP C 123 114.80 -14.78
REMARK 500 TYR C 124 111.36 84.37
REMARK 500 SER C 240 -33.59 82.56
REMARK 500 MET C 298 92.11 -170.35
REMARK 500 LYS C 356 -119.11 48.32
REMARK 500 ASN C 382 -157.49 -119.80
REMARK 500 LEU C 384 -147.99 -102.14
REMARK 500 GLU C 386 -80.91 -35.89
REMARK 500 ARG C 387 141.59 66.91
REMARK 500 LEU C 404 -85.07 157.19
REMARK 500 SER D 128 -73.37 -44.98
REMARK 500 ASN D 140 109.83 74.11
REMARK 500 PRO D 141 4.48 -62.16
REMARK 500 SER D 144 -153.34 -90.14
REMARK 500 SER D 154 -36.30 -38.64
REMARK 500 ASN D 185 98.74 -63.92
REMARK 500 ASP D 234 91.79 -62.87
REMARK 500 ARG D 275 5.70 -66.62
REMARK 500 LYS D 356 -115.27 50.30
REMARK 500 ASN D 362 -169.34 -62.34
REMARK 500 LYS D 363 78.83 -172.07
REMARK 500 ASP D 381 66.90 -111.01
REMARK 500 GLU D 386 -66.87 -124.78
REMARK 500 THR D 389 -62.74 45.16
REMARK 500 ILE D 405 -56.27 -124.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 427
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QFU RELATED DB: PDB
REMARK 900 RELATED ID: 3QFP RELATED DB: PDB
DBREF 3QML A 43 426 UNP P16474 GRP78_YEAST 43 426
DBREF 3QML B 43 426 UNP P16474 GRP78_YEAST 43 426
DBREF 3QML C 113 421 UNP Q08199 SIL1_YEAST 113 421
DBREF 3QML D 113 421 UNP Q08199 SIL1_YEAST 113 421
SEQADV 3QML GLY A 37 UNP P16474 EXPRESSION TAG
SEQADV 3QML MET A 38 UNP P16474 EXPRESSION TAG
SEQADV 3QML SER A 39 UNP P16474 EXPRESSION TAG
SEQADV 3QML HIS A 40 UNP P16474 EXPRESSION TAG
SEQADV 3QML ALA A 41 UNP P16474 EXPRESSION TAG
SEQADV 3QML SER A 42 UNP P16474 EXPRESSION TAG
SEQADV 3QML GLY B 37 UNP P16474 EXPRESSION TAG
SEQADV 3QML MET B 38 UNP P16474 EXPRESSION TAG
SEQADV 3QML SER B 39 UNP P16474 EXPRESSION TAG
SEQADV 3QML HIS B 40 UNP P16474 EXPRESSION TAG
SEQADV 3QML ALA B 41 UNP P16474 EXPRESSION TAG
SEQADV 3QML SER B 42 UNP P16474 EXPRESSION TAG
SEQADV 3QML GLY C 107 UNP Q08199 EXPRESSION TAG
SEQADV 3QML MET C 108 UNP Q08199 EXPRESSION TAG
SEQADV 3QML SER C 109 UNP Q08199 EXPRESSION TAG
SEQADV 3QML HIS C 110 UNP Q08199 EXPRESSION TAG
SEQADV 3QML ALA C 111 UNP Q08199 EXPRESSION TAG
SEQADV 3QML SER C 112 UNP Q08199 EXPRESSION TAG
SEQADV 3QML GLY D 107 UNP Q08199 EXPRESSION TAG
SEQADV 3QML MET D 108 UNP Q08199 EXPRESSION TAG
SEQADV 3QML SER D 109 UNP Q08199 EXPRESSION TAG
SEQADV 3QML HIS D 110 UNP Q08199 EXPRESSION TAG
SEQADV 3QML ALA D 111 UNP Q08199 EXPRESSION TAG
SEQADV 3QML SER D 112 UNP Q08199 EXPRESSION TAG
SEQRES 1 A 390 GLY MET SER HIS ALA SER ALA ASP ASP VAL GLU ASN TYR
SEQRES 2 A 390 GLY THR VAL ILE GLY ILE ASP LEU GLY THR THR TYR SER
SEQRES 3 A 390 CYS VAL ALA VAL MET LYS ASN GLY LYS THR GLU ILE LEU
SEQRES 4 A 390 ALA ASN GLU GLN GLY ASN ARG ILE THR PRO SER TYR VAL
SEQRES 5 A 390 ALA PHE THR ASP ASP GLU ARG LEU ILE GLY ASP ALA ALA
SEQRES 6 A 390 LYS ASN GLN VAL ALA ALA ASN PRO GLN ASN THR ILE PHE
SEQRES 7 A 390 ASP ILE LYS ARG LEU ILE GLY LEU LYS TYR ASN ASP ARG
SEQRES 8 A 390 SER VAL GLN LYS ASP ILE LYS HIS LEU PRO PHE ASN VAL
SEQRES 9 A 390 VAL ASN LYS ASP GLY LYS PRO ALA VAL GLU VAL SER VAL
SEQRES 10 A 390 LYS GLY GLU LYS LYS VAL PHE THR PRO GLU GLU ILE SER
SEQRES 11 A 390 GLY MET ILE LEU GLY LYS MET LYS GLN ILE ALA GLU ASP
SEQRES 12 A 390 TYR LEU GLY THR LYS VAL THR HIS ALA VAL VAL THR VAL
SEQRES 13 A 390 PRO ALA TYR PHE ASN ASP ALA GLN ARG GLN ALA THR LYS
SEQRES 14 A 390 ASP ALA GLY THR ILE ALA GLY LEU ASN VAL LEU ARG ILE
SEQRES 15 A 390 VAL ASN GLU PRO THR ALA ALA ALA ILE ALA TYR GLY LEU
SEQRES 16 A 390 ASP LYS SER ASP LYS GLU HIS GLN ILE ILE VAL TYR ASP
SEQRES 17 A 390 LEU GLY GLY GLY THR PHE ASP VAL SER LEU LEU SER ILE
SEQRES 18 A 390 GLU ASN GLY VAL PHE GLU VAL GLN ALA THR SER GLY ASP
SEQRES 19 A 390 THR HIS LEU GLY GLY GLU ASP PHE ASP TYR LYS ILE VAL
SEQRES 20 A 390 ARG GLN LEU ILE LYS ALA PHE LYS LYS LYS HIS GLY ILE
SEQRES 21 A 390 ASP VAL SER ASP ASN ASN LYS ALA LEU ALA LYS LEU LYS
SEQRES 22 A 390 ARG GLU ALA GLU LYS ALA LYS ARG ALA LEU SER SER GLN
SEQRES 23 A 390 MET SER THR ARG ILE GLU ILE ASP SER PHE VAL ASP GLY
SEQRES 24 A 390 ILE ASP LEU SER GLU THR LEU THR ARG ALA LYS PHE GLU
SEQRES 25 A 390 GLU LEU ASN LEU ASP LEU PHE LYS LYS THR LEU LYS PRO
SEQRES 26 A 390 VAL GLU LYS VAL LEU GLN ASP SER GLY LEU GLU LYS LYS
SEQRES 27 A 390 ASP VAL ASP ASP ILE VAL LEU VAL GLY GLY SER THR ARG
SEQRES 28 A 390 ILE PRO LYS VAL GLN GLN LEU LEU GLU SER TYR PHE ASP
SEQRES 29 A 390 GLY LYS LYS ALA SER LYS GLY ILE ASN PRO ASP GLU ALA
SEQRES 30 A 390 VAL ALA TYR GLY ALA ALA VAL GLN ALA GLY VAL LEU SER
SEQRES 1 B 390 GLY MET SER HIS ALA SER ALA ASP ASP VAL GLU ASN TYR
SEQRES 2 B 390 GLY THR VAL ILE GLY ILE ASP LEU GLY THR THR TYR SER
SEQRES 3 B 390 CYS VAL ALA VAL MET LYS ASN GLY LYS THR GLU ILE LEU
SEQRES 4 B 390 ALA ASN GLU GLN GLY ASN ARG ILE THR PRO SER TYR VAL
SEQRES 5 B 390 ALA PHE THR ASP ASP GLU ARG LEU ILE GLY ASP ALA ALA
SEQRES 6 B 390 LYS ASN GLN VAL ALA ALA ASN PRO GLN ASN THR ILE PHE
SEQRES 7 B 390 ASP ILE LYS ARG LEU ILE GLY LEU LYS TYR ASN ASP ARG
SEQRES 8 B 390 SER VAL GLN LYS ASP ILE LYS HIS LEU PRO PHE ASN VAL
SEQRES 9 B 390 VAL ASN LYS ASP GLY LYS PRO ALA VAL GLU VAL SER VAL
SEQRES 10 B 390 LYS GLY GLU LYS LYS VAL PHE THR PRO GLU GLU ILE SER
SEQRES 11 B 390 GLY MET ILE LEU GLY LYS MET LYS GLN ILE ALA GLU ASP
SEQRES 12 B 390 TYR LEU GLY THR LYS VAL THR HIS ALA VAL VAL THR VAL
SEQRES 13 B 390 PRO ALA TYR PHE ASN ASP ALA GLN ARG GLN ALA THR LYS
SEQRES 14 B 390 ASP ALA GLY THR ILE ALA GLY LEU ASN VAL LEU ARG ILE
SEQRES 15 B 390 VAL ASN GLU PRO THR ALA ALA ALA ILE ALA TYR GLY LEU
SEQRES 16 B 390 ASP LYS SER ASP LYS GLU HIS GLN ILE ILE VAL TYR ASP
SEQRES 17 B 390 LEU GLY GLY GLY THR PHE ASP VAL SER LEU LEU SER ILE
SEQRES 18 B 390 GLU ASN GLY VAL PHE GLU VAL GLN ALA THR SER GLY ASP
SEQRES 19 B 390 THR HIS LEU GLY GLY GLU ASP PHE ASP TYR LYS ILE VAL
SEQRES 20 B 390 ARG GLN LEU ILE LYS ALA PHE LYS LYS LYS HIS GLY ILE
SEQRES 21 B 390 ASP VAL SER ASP ASN ASN LYS ALA LEU ALA LYS LEU LYS
SEQRES 22 B 390 ARG GLU ALA GLU LYS ALA LYS ARG ALA LEU SER SER GLN
SEQRES 23 B 390 MET SER THR ARG ILE GLU ILE ASP SER PHE VAL ASP GLY
SEQRES 24 B 390 ILE ASP LEU SER GLU THR LEU THR ARG ALA LYS PHE GLU
SEQRES 25 B 390 GLU LEU ASN LEU ASP LEU PHE LYS LYS THR LEU LYS PRO
SEQRES 26 B 390 VAL GLU LYS VAL LEU GLN ASP SER GLY LEU GLU LYS LYS
SEQRES 27 B 390 ASP VAL ASP ASP ILE VAL LEU VAL GLY GLY SER THR ARG
SEQRES 28 B 390 ILE PRO LYS VAL GLN GLN LEU LEU GLU SER TYR PHE ASP
SEQRES 29 B 390 GLY LYS LYS ALA SER LYS GLY ILE ASN PRO ASP GLU ALA
SEQRES 30 B 390 VAL ALA TYR GLY ALA ALA VAL GLN ALA GLY VAL LEU SER
SEQRES 1 C 315 GLY MET SER HIS ALA SER SER SER GLU ASP MET LYS ALA
SEQRES 2 C 315 SER PRO GLY ASP TYR GLU PHE SER SER ASP PHE LYS GLU
SEQRES 3 C 315 MET ARG ASN ILE ILE ASP SER ASN PRO THR LEU SER SER
SEQRES 4 C 315 GLN ASP ILE ALA ARG LEU GLU ASP SER PHE ASP ARG ILE
SEQRES 5 C 315 MET GLU PHE ALA HIS ASP TYR LYS HIS GLY TYR LYS ILE
SEQRES 6 C 315 ILE THR HIS GLU PHE ALA LEU LEU ALA ASN LEU SER LEU
SEQRES 7 C 315 ASN GLU ASN LEU PRO LEU THR LEU ARG GLU LEU SER THR
SEQRES 8 C 315 ARG VAL ILE THR SER CYS LEU ARG ASN ASN PRO PRO VAL
SEQRES 9 C 315 VAL GLU PHE ILE ASN GLU SER PHE PRO ASN PHE LYS SER
SEQRES 10 C 315 LYS ILE MET ALA ALA LEU SER ASN LEU ASN ASP SER ASN
SEQRES 11 C 315 HIS ARG SER SER ASN ILE LEU ILE LYS ARG TYR LEU SER
SEQRES 12 C 315 ILE LEU ASN GLU LEU PRO VAL THR SER GLU ASP LEU PRO
SEQRES 13 C 315 ILE TYR SER THR VAL VAL LEU GLN ASN VAL TYR GLU ARG
SEQRES 14 C 315 ASN ASN LYS ASP LYS GLN LEU GLN ILE LYS VAL LEU GLU
SEQRES 15 C 315 LEU ILE SER LYS ILE LEU LYS ALA ASP MET TYR GLU ASN
SEQRES 16 C 315 ASP ASP THR ASN LEU ILE LEU PHE LYS ARG ASN ALA GLU
SEQRES 17 C 315 ASN TRP SER SER ASN LEU GLN GLU TRP ALA ASN GLU PHE
SEQRES 18 C 315 GLN GLU MET VAL GLN ASN LYS SER ILE ASP GLU LEU HIS
SEQRES 19 C 315 THR ARG THR PHE PHE ASP THR LEU TYR ASN LEU LYS LYS
SEQRES 20 C 315 ILE PHE LYS SER ASP ILE THR ILE ASN LYS GLY PHE LEU
SEQRES 21 C 315 ASN TRP LEU ALA GLN GLN CYS LYS ALA ARG GLN SER ASN
SEQRES 22 C 315 LEU ASP ASN GLY LEU GLN GLU ARG ASP THR GLU GLN ASP
SEQRES 23 C 315 SER PHE ASP LYS LYS LEU ILE ASP SER ARG HIS LEU ILE
SEQRES 24 C 315 PHE GLY ASN PRO MET ALA HIS ARG ILE LYS ASN PHE ARG
SEQRES 25 C 315 ASP GLU LEU
SEQRES 1 D 315 GLY MET SER HIS ALA SER SER SER GLU ASP MET LYS ALA
SEQRES 2 D 315 SER PRO GLY ASP TYR GLU PHE SER SER ASP PHE LYS GLU
SEQRES 3 D 315 MET ARG ASN ILE ILE ASP SER ASN PRO THR LEU SER SER
SEQRES 4 D 315 GLN ASP ILE ALA ARG LEU GLU ASP SER PHE ASP ARG ILE
SEQRES 5 D 315 MET GLU PHE ALA HIS ASP TYR LYS HIS GLY TYR LYS ILE
SEQRES 6 D 315 ILE THR HIS GLU PHE ALA LEU LEU ALA ASN LEU SER LEU
SEQRES 7 D 315 ASN GLU ASN LEU PRO LEU THR LEU ARG GLU LEU SER THR
SEQRES 8 D 315 ARG VAL ILE THR SER CYS LEU ARG ASN ASN PRO PRO VAL
SEQRES 9 D 315 VAL GLU PHE ILE ASN GLU SER PHE PRO ASN PHE LYS SER
SEQRES 10 D 315 LYS ILE MET ALA ALA LEU SER ASN LEU ASN ASP SER ASN
SEQRES 11 D 315 HIS ARG SER SER ASN ILE LEU ILE LYS ARG TYR LEU SER
SEQRES 12 D 315 ILE LEU ASN GLU LEU PRO VAL THR SER GLU ASP LEU PRO
SEQRES 13 D 315 ILE TYR SER THR VAL VAL LEU GLN ASN VAL TYR GLU ARG
SEQRES 14 D 315 ASN ASN LYS ASP LYS GLN LEU GLN ILE LYS VAL LEU GLU
SEQRES 15 D 315 LEU ILE SER LYS ILE LEU LYS ALA ASP MET TYR GLU ASN
SEQRES 16 D 315 ASP ASP THR ASN LEU ILE LEU PHE LYS ARG ASN ALA GLU
SEQRES 17 D 315 ASN TRP SER SER ASN LEU GLN GLU TRP ALA ASN GLU PHE
SEQRES 18 D 315 GLN GLU MET VAL GLN ASN LYS SER ILE ASP GLU LEU HIS
SEQRES 19 D 315 THR ARG THR PHE PHE ASP THR LEU TYR ASN LEU LYS LYS
SEQRES 20 D 315 ILE PHE LYS SER ASP ILE THR ILE ASN LYS GLY PHE LEU
SEQRES 21 D 315 ASN TRP LEU ALA GLN GLN CYS LYS ALA ARG GLN SER ASN
SEQRES 22 D 315 LEU ASP ASN GLY LEU GLN GLU ARG ASP THR GLU GLN ASP
SEQRES 23 D 315 SER PHE ASP LYS LYS LEU ILE ASP SER ARG HIS LEU ILE
SEQRES 24 D 315 PHE GLY ASN PRO MET ALA HIS ARG ILE LYS ASN PHE ARG
SEQRES 25 D 315 ASP GLU LEU
HET PO4 A 2 5
HET PO4 A 4 5
HET MG A 1 1
HET MG A 427 1
HET PO4 B 1 5
HET PO4 B 3 5
HET PO4 C 5 5
HET PO4 C 6 5
HET MG C 1 1
HET PO4 D 7 5
HET PO4 D 8 5
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
FORMUL 5 PO4 8(O4 P 3-)
FORMUL 7 MG 3(MG 2+)
FORMUL 16 HOH *206(H2 O)
HELIX 1 1 GLY A 98 GLN A 104 1 7
HELIX 2 2 ASP A 115 LEU A 119 5 5
HELIX 3 3 ASP A 126 HIS A 135 1 10
HELIX 4 4 THR A 161 LEU A 181 1 21
HELIX 5 5 ASN A 197 ALA A 211 1 15
HELIX 6 6 GLU A 221 TYR A 229 1 9
HELIX 7 7 GLY A 274 GLY A 295 1 22
HELIX 8 8 ASP A 297 ASP A 300 5 4
HELIX 9 9 ASN A 301 SER A 320 1 20
HELIX 10 10 ARG A 344 THR A 358 1 15
HELIX 11 11 THR A 358 GLY A 370 1 13
HELIX 12 12 GLU A 372 VAL A 376 5 5
HELIX 13 13 GLY A 383 ARG A 387 5 5
HELIX 14 14 ILE A 388 PHE A 399 1 12
HELIX 15 15 GLU A 412 GLY A 423 1 12
HELIX 16 16 GLY B 98 GLN B 104 1 7
HELIX 17 17 ASP B 115 LEU B 119 5 5
HELIX 18 18 ASP B 126 HIS B 135 1 10
HELIX 19 19 THR B 161 ASP B 179 1 19
HELIX 20 20 ASN B 197 ILE B 210 1 14
HELIX 21 21 GLU B 221 TYR B 229 1 9
HELIX 22 22 GLY B 274 GLY B 295 1 22
HELIX 23 23 ASP B 297 ASP B 300 5 4
HELIX 24 24 ASN B 301 LEU B 319 1 19
HELIX 25 25 ARG B 344 ASN B 351 1 8
HELIX 26 26 ASN B 351 LYS B 357 1 7
HELIX 27 27 LEU B 359 ASP B 368 1 10
HELIX 28 28 GLY B 384 ARG B 387 5 4
HELIX 29 29 ILE B 388 PHE B 399 1 12
HELIX 30 30 GLU B 412 VAL B 424 1 13
HELIX 31 31 PHE C 126 ASN C 140 1 15
HELIX 32 32 SER C 144 MET C 159 1 16
HELIX 33 33 GLU C 160 ALA C 162 5 3
HELIX 34 34 ASP C 164 ASN C 185 1 22
HELIX 35 35 PRO C 189 ARG C 205 1 17
HELIX 36 36 ASN C 207 PHE C 218 1 12
HELIX 37 37 ASN C 220 ASP C 234 1 15
HELIX 38 38 SER C 240 LEU C 254 1 15
HELIX 39 39 SER C 265 ASN C 276 1 12
HELIX 40 40 ASP C 279 MET C 298 1 20
HELIX 41 41 LEU C 320 GLN C 332 1 13
HELIX 42 42 ASP C 337 LYS C 356 1 20
HELIX 43 43 SER C 357 ILE C 359 5 3
HELIX 44 44 ASN C 362 ASP C 381 1 20
HELIX 45 45 ASP C 388 HIS C 403 1 16
HELIX 46 46 PHE D 126 ILE D 136 1 11
HELIX 47 47 SER D 144 HIS D 163 1 20
HELIX 48 48 ASP D 164 ASN D 185 1 22
HELIX 49 49 PRO D 189 ARG D 205 1 17
HELIX 50 50 PRO D 209 PHE D 218 1 10
HELIX 51 51 ASN D 220 ASP D 234 1 15
HELIX 52 52 SER D 240 LEU D 254 1 15
HELIX 53 53 THR D 257 TYR D 264 5 8
HELIX 54 54 SER D 265 ARG D 275 1 11
HELIX 55 55 ASP D 279 LYS D 295 1 17
HELIX 56 56 ASN D 305 SER D 317 1 13
HELIX 57 57 LEU D 320 VAL D 331 1 12
HELIX 58 58 ASP D 337 LYS D 356 1 20
HELIX 59 59 SER D 357 ILE D 359 5 3
HELIX 60 60 GLY D 364 ASP D 381 1 18
HELIX 61 61 THR D 389 ILE D 405 1 17
SHEET 1 A 3 LYS A 71 ILE A 74 0
SHEET 2 A 3 TYR A 61 LYS A 68 -1 N LYS A 68 O LYS A 71
SHEET 3 A 3 THR A 84 PRO A 85 -1 O THR A 84 N SER A 62
SHEET 1 B 5 LYS A 71 ILE A 74 0
SHEET 2 B 5 TYR A 61 LYS A 68 -1 N LYS A 68 O LYS A 71
SHEET 3 B 5 ILE A 53 LEU A 57 -1 N ASP A 56 O CYS A 63
SHEET 4 B 5 HIS A 187 VAL A 192 1 O VAL A 189 N ILE A 53
SHEET 5 B 5 ASN A 214 ASN A 220 1 O VAL A 219 N VAL A 192
SHEET 1 C 3 ARG A 95 ILE A 97 0
SHEET 2 C 3 VAL A 88 PHE A 90 -1 N ALA A 89 O LEU A 96
SHEET 3 C 3 THR A 112 ILE A 113 -1 O ILE A 113 N VAL A 88
SHEET 1 D 3 ASN A 139 LYS A 143 0
SHEET 2 D 3 LYS A 146 SER A 152 -1 O LYS A 146 N LYS A 143
SHEET 3 D 3 LYS A 157 PHE A 160 -1 O LYS A 158 N VAL A 151
SHEET 1 E 4 VAL A 261 ASP A 270 0
SHEET 2 E 4 PHE A 250 GLU A 258 -1 N LEU A 254 O GLN A 265
SHEET 3 E 4 HIS A 238 LEU A 245 -1 N ASP A 244 O ASP A 251
SHEET 4 E 4 ASP A 378 VAL A 382 1 O VAL A 380 N TYR A 243
SHEET 1 F 2 SER A 324 VAL A 333 0
SHEET 2 F 2 ILE A 336 THR A 343 -1 O GLU A 340 N ILE A 327
SHEET 1 G 3 LYS B 71 ILE B 74 0
SHEET 2 G 3 TYR B 61 LYS B 68 -1 N VAL B 66 O GLU B 73
SHEET 3 G 3 THR B 84 PRO B 85 -1 O THR B 84 N SER B 62
SHEET 1 H 5 LYS B 71 ILE B 74 0
SHEET 2 H 5 TYR B 61 LYS B 68 -1 N VAL B 66 O GLU B 73
SHEET 3 H 5 ILE B 53 LEU B 57 -1 N GLY B 54 O ALA B 65
SHEET 4 H 5 ALA B 188 VAL B 192 1 O VAL B 189 N ILE B 53
SHEET 5 H 5 VAL B 219 ASN B 220 1 O VAL B 219 N VAL B 192
SHEET 1 I 3 ARG B 95 ILE B 97 0
SHEET 2 I 3 VAL B 88 PHE B 90 -1 N ALA B 89 O LEU B 96
SHEET 3 I 3 THR B 112 ILE B 113 -1 O ILE B 113 N VAL B 88
SHEET 1 J 3 ASN B 139 LYS B 143 0
SHEET 2 J 3 LYS B 146 SER B 152 -1 O LYS B 146 N LYS B 143
SHEET 3 J 3 LYS B 157 PHE B 160 -1 O PHE B 160 N VAL B 149
SHEET 1 K 3 PHE B 262 GLU B 263 0
SHEET 2 K 3 PHE B 250 ILE B 257 -1 N SER B 256 O GLU B 263
SHEET 3 K 3 THR B 267 ASP B 270 -1 O SER B 268 N VAL B 252
SHEET 1 L 4 PHE B 262 GLU B 263 0
SHEET 2 L 4 PHE B 250 ILE B 257 -1 N SER B 256 O GLU B 263
SHEET 3 L 4 ILE B 240 LEU B 245 -1 N ASP B 244 O ASP B 251
SHEET 4 L 4 ASP B 378 VAL B 382 1 O VAL B 382 N TYR B 243
SHEET 1 M 2 SER B 324 VAL B 333 0
SHEET 2 M 2 ILE B 336 THR B 343 -1 O LEU B 338 N ILE B 329
LINK MG MG A 1 O HOH A 477 1555 1555 2.54
CISPEP 1 VAL A 153 LYS A 154 0 -3.84
CISPEP 2 LYS A 154 GLY A 155 0 -7.69
CISPEP 3 SER A 234 ASP A 235 0 11.15
CISPEP 4 VAL B 153 LYS B 154 0 -6.86
CISPEP 5 LYS B 154 GLY B 155 0 -1.79
CISPEP 6 ILE B 210 ALA B 211 0 -6.82
CISPEP 7 GLY B 370 LEU B 371 0 -2.36
CISPEP 8 ASP C 123 TYR C 124 0 -10.89
CISPEP 9 SER C 239 SER C 240 0 -3.19
CISPEP 10 MET C 298 TYR C 299 0 -7.36
CISPEP 11 GLY C 383 LEU C 384 0 -7.47
CISPEP 12 PRO D 208 PRO D 209 0 11.53
CISPEP 13 ALA D 296 ASP D 297 0 8.86
CISPEP 14 LYS D 363 GLY D 364 0 -8.50
CISPEP 15 GLU D 386 ARG D 387 0 -3.88
SITE 1 AC1 6 GLY B 58 THR B 59 THR B 60 TYR B 61
SITE 2 AC1 6 GLY B 246 GLY B 247
SITE 1 AC2 7 THR A 59 THR A 60 TYR A 61 GLY A 246
SITE 2 AC2 7 GLY A 247 HOH A 444 HOH A 452
SITE 1 AC3 4 GLU B 276 ASP B 279 GLU B 313 LYS B 316
SITE 1 AC4 4 GLU A 276 ASP A 279 GLU A 313 LYS A 316
SITE 1 AC5 6 HOH C 60 PHE C 218 PRO C 219 ASN C 220
SITE 2 AC5 6 PHE C 221 LYS C 224
SITE 1 AC6 3 GLU C 326 HOH C 434 HOH C 436
SITE 1 AC7 4 PHE D 218 PRO D 219 ASN D 220 LYS D 224
SITE 1 AC8 4 GLU D 274 ASN D 277 GLU D 326 HOH D 434
SITE 1 AC9 1 HOH A 477
SITE 1 BC1 3 LYS A 68 ASN A 69 GLN A 285
SITE 1 BC2 1 LYS C 363
CRYST1 226.353 116.586 55.844 90.00 90.00 90.00 P 21 21 2 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 0.004418 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017907 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
