HEADER CHAPERONE 26-AUG-16 5GU6
TITLE CRYSTAL STRUCTURE OF HUMAN ERP44 FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPLASMIC RETICULUM RESIDENT PROTEIN 44;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 30-402;
COMPND 5 SYNONYM: ERP44,THIOREDOXIN DOMAIN-CONTAINING PROTEIN 4;
COMPND 6 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: ERP44, KIAA0573, TXNDC4, UNQ532/PRO1075;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE, QUALITY CONTROL
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WATANABE,K.INABA
REVDAT 3 08-NOV-23 5GU6 1 REMARK
REVDAT 2 03-MAY-17 5GU6 1 JRNL
REVDAT 1 12-APR-17 5GU6 0
JRNL AUTH S.WATANABE,M.HARAYAMA,S.KANEMURA,R.SITIA,K.INABA
JRNL TITL STRUCTURAL BASIS OF PH-DEPENDENT CLIENT BINDING BY ERP44, A
JRNL TITL 2 KEY REGULATOR OF PROTEIN SECRETION AT THE ER-GOLGI INTERFACE
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E3224 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28373561
JRNL DOI 10.1073/PNAS.1621426114
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 36959
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1782
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 19.6078 - 4.6830 0.99 2856 142 0.1703 0.1947
REMARK 3 2 4.6830 - 3.7253 1.00 2724 178 0.1619 0.1977
REMARK 3 3 3.7253 - 3.2569 1.00 2755 123 0.2051 0.2620
REMARK 3 4 3.2569 - 2.9602 1.00 2721 147 0.2499 0.2985
REMARK 3 5 2.9602 - 2.7486 1.00 2729 121 0.2550 0.3205
REMARK 3 6 2.7486 - 2.5870 1.00 2705 138 0.2551 0.3105
REMARK 3 7 2.5870 - 2.4577 1.00 2675 147 0.2445 0.2505
REMARK 3 8 2.4577 - 2.3509 1.00 2695 121 0.2494 0.2698
REMARK 3 9 2.3509 - 2.2605 1.00 2678 134 0.2535 0.3178
REMARK 3 10 2.2605 - 2.1826 1.00 2663 147 0.2516 0.2952
REMARK 3 11 2.1826 - 2.1144 1.00 2658 136 0.2602 0.3242
REMARK 3 12 2.1144 - 2.0541 1.00 2700 107 0.2772 0.2864
REMARK 3 13 2.0541 - 2.0000 0.99 2618 141 0.3057 0.3342
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.840
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3166
REMARK 3 ANGLE : 0.665 4297
REMARK 3 CHIRALITY : 0.048 459
REMARK 3 PLANARITY : 0.006 576
REMARK 3 DIHEDRAL : 18.845 1187
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -4 THROUGH 112)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1110 3.5946 6.8707
REMARK 3 T TENSOR
REMARK 3 T11: 0.6333 T22: 0.3945
REMARK 3 T33: 0.4656 T12: -0.0233
REMARK 3 T13: -0.2089 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 3.2387 L22: 2.9139
REMARK 3 L33: 1.9729 L12: 0.4491
REMARK 3 L13: -0.1768 L23: -0.5109
REMARK 3 S TENSOR
REMARK 3 S11: 0.1408 S12: -0.4654 S13: -0.2431
REMARK 3 S21: 0.7098 S22: -0.1232 S23: -0.4338
REMARK 3 S31: -0.0280 S32: 0.2640 S33: -0.0437
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0336 22.4500 -3.4393
REMARK 3 T TENSOR
REMARK 3 T11: 0.4822 T22: 0.5747
REMARK 3 T33: 0.6359 T12: -0.0232
REMARK 3 T13: -0.0844 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 3.5637 L22: 4.7412
REMARK 3 L33: 1.8236 L12: -0.3922
REMARK 3 L13: 0.3160 L23: -0.9793
REMARK 3 S TENSOR
REMARK 3 S11: 0.2250 S12: 0.0975 S13: -0.4446
REMARK 3 S21: -0.1706 S22: 0.0125 S23: -0.8667
REMARK 3 S31: 0.2308 S32: 0.4466 S33: -0.1834
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8033 14.4704 -25.5896
REMARK 3 T TENSOR
REMARK 3 T11: 0.5890 T22: 0.2939
REMARK 3 T33: 0.4783 T12: -0.0259
REMARK 3 T13: -0.1508 T23: 0.0618
REMARK 3 L TENSOR
REMARK 3 L11: 1.7701 L22: 1.8801
REMARK 3 L33: 3.9770 L12: 0.3228
REMARK 3 L13: -0.7565 L23: -1.2598
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.2357 S13: 0.3226
REMARK 3 S21: 0.1527 S22: -0.1516 S23: -0.3075
REMARK 3 S31: -0.6826 S32: 0.0642 S33: 0.1787
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 5GU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36963
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 18.20
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.14
REMARK 200 R MERGE FOR SHELL (I) : 1.12500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2R2J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL (PEG) 8000, PH
REMARK 280 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 46.63667
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 93.27333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 93.27333
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 46.63667
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -46.63667
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 HOH A 558 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 GLY A -5
REMARK 465 GLY A 343
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 HIS A -3 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 ASN A 52 CG OD1 ND2
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 GLN A 140 CG CD OE1 NE2
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 TYR A 175 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 PHE A 320 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 344 CG CD OE1 OE2
REMARK 470 ASP A 373 CG OD1 OD2
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 HOH A 527 O HOH A 597 1.87
REMARK 500 O HOH A 544 O HOH A 598 2.08
REMARK 500 NE2 GLN A 345 O HOH A 501 2.10
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 54 32.81 -146.45
REMARK 500 ALA A 341 81.28 -165.53
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 CL A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GU7 RELATED DB: PDB
DBREF 5GU6 A 1 373 UNP Q9BS26 ERP44_HUMAN 30 402
SEQADV 5GU6 GLY A -5 UNP Q9BS26 EXPRESSION TAG
SEQADV 5GU6 SER A -4 UNP Q9BS26 EXPRESSION TAG
SEQADV 5GU6 HIS A -3 UNP Q9BS26 EXPRESSION TAG
SEQADV 5GU6 MET A -2 UNP Q9BS26 EXPRESSION TAG
SEQADV 5GU6 ALA A -1 UNP Q9BS26 EXPRESSION TAG
SEQADV 5GU6 SER A 0 UNP Q9BS26 EXPRESSION TAG
SEQRES 1 A 379 GLY SER HIS MET ALA SER GLU ILE THR SER LEU ASP THR
SEQRES 2 A 379 GLU ASN ILE ASP GLU ILE LEU ASN ASN ALA ASP VAL ALA
SEQRES 3 A 379 LEU VAL ASN PHE TYR ALA ASP TRP CYS ARG PHE SER GLN
SEQRES 4 A 379 MET LEU HIS PRO ILE PHE GLU GLU ALA SER ASP VAL ILE
SEQRES 5 A 379 LYS GLU GLU PHE PRO ASN GLU ASN GLN VAL VAL PHE ALA
SEQRES 6 A 379 ARG VAL ASP CYS ASP GLN HIS SER ASP ILE ALA GLN ARG
SEQRES 7 A 379 TYR ARG ILE SER LYS TYR PRO THR LEU LYS LEU PHE ARG
SEQRES 8 A 379 ASN GLY MET MET MET LYS ARG GLU TYR ARG GLY GLN ARG
SEQRES 9 A 379 SER VAL LYS ALA LEU ALA ASP TYR ILE ARG GLN GLN LYS
SEQRES 10 A 379 SER ASP PRO ILE GLN GLU ILE ARG ASP LEU ALA GLU ILE
SEQRES 11 A 379 THR THR LEU ASP ARG SER LYS ARG ASN ILE ILE GLY TYR
SEQRES 12 A 379 PHE GLU GLN LYS ASP SER ASP ASN TYR ARG VAL PHE GLU
SEQRES 13 A 379 ARG VAL ALA ASN ILE LEU HIS ASP ASP CYS ALA PHE LEU
SEQRES 14 A 379 SER ALA PHE GLY ASP VAL SER LYS PRO GLU ARG TYR SER
SEQRES 15 A 379 GLY ASP ASN ILE ILE TYR LYS PRO PRO GLY HIS SER ALA
SEQRES 16 A 379 PRO ASP MET VAL TYR LEU GLY ALA MET THR ASN PHE ASP
SEQRES 17 A 379 VAL THR TYR ASN TRP ILE GLN ASP LYS CYS VAL PRO LEU
SEQRES 18 A 379 VAL ARG GLU ILE THR PHE GLU ASN GLY GLU GLU LEU THR
SEQRES 19 A 379 GLU GLU GLY LEU PRO PHE LEU ILE LEU PHE HIS MET LYS
SEQRES 20 A 379 GLU ASP THR GLU SER LEU GLU ILE PHE GLN ASN GLU VAL
SEQRES 21 A 379 ALA ARG GLN LEU ILE SER GLU LYS GLY THR ILE ASN PHE
SEQRES 22 A 379 LEU HIS ALA ASP CYS ASP LYS PHE ARG HIS PRO LEU LEU
SEQRES 23 A 379 HIS ILE GLN LYS THR PRO ALA ASP CYS PRO VAL ILE ALA
SEQRES 24 A 379 ILE ASP SER PHE ARG HIS MET TYR VAL PHE GLY ASP PHE
SEQRES 25 A 379 LYS ASP VAL LEU ILE PRO GLY LYS LEU LYS GLN PHE VAL
SEQRES 26 A 379 PHE ASP LEU HIS SER GLY LYS LEU HIS ARG GLU PHE HIS
SEQRES 27 A 379 HIS GLY PRO ASP PRO THR ASP THR ALA PRO GLY GLU GLN
SEQRES 28 A 379 ALA GLN ASP VAL ALA SER SER PRO PRO GLU SER SER PHE
SEQRES 29 A 379 GLN LYS LEU ALA PRO SER GLU TYR ARG TYR THR LEU LEU
SEQRES 30 A 379 ARG ASP
HET CL A 401 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *111(H2 O)
HELIX 1 AA1 ASN A 9 ALA A 17 1 9
HELIX 2 AA2 CYS A 29 PHE A 50 1 22
HELIX 3 AA3 HIS A 66 TYR A 73 1 8
HELIX 4 AA4 SER A 99 SER A 112 1 14
HELIX 5 AA5 LEU A 121 THR A 126 1 6
HELIX 6 AA6 SER A 143 HIS A 157 1 15
HELIX 7 AA7 PHE A 166 LYS A 171 1 6
HELIX 8 AA8 PRO A 172 ARG A 174 5 3
HELIX 9 AA9 ASN A 200 VAL A 213 1 14
HELIX 10 AB1 ASN A 223 GLU A 230 1 8
HELIX 11 AB2 ASP A 243 LEU A 258 1 16
HELIX 12 AB3 ILE A 259 LYS A 262 5 4
HELIX 13 AB4 PHE A 275 ILE A 282 1 8
HELIX 14 AB5 THR A 285 CYS A 289 5 5
HELIX 15 AB6 ASP A 305 ILE A 311 5 7
HELIX 16 AB7 GLY A 313 SER A 324 1 12
HELIX 17 AB8 GLY A 325 GLY A 334 1 10
HELIX 18 AB9 SER A 357 ALA A 362 5 6
SHEET 1 AA1 5 THR A 3 SER A 4 0
SHEET 2 AA1 5 VAL A 57 ASP A 62 1 O ARG A 60 N THR A 3
SHEET 3 AA1 5 ALA A 20 TYR A 25 1 N ASN A 23 O VAL A 61
SHEET 4 AA1 5 THR A 80 ARG A 85 -1 O THR A 80 N PHE A 24
SHEET 5 AA1 5 MET A 88 MET A 89 -1 O MET A 88 N ARG A 85
SHEET 1 AA2 2 LYS A 77 TYR A 78 0
SHEET 2 AA2 2 THR A 369 LEU A 370 -1 O THR A 369 N TYR A 78
SHEET 1 AA3 5 GLN A 116 GLU A 117 0
SHEET 2 AA3 5 ALA A 161 ALA A 165 1 O PHE A 162 N GLN A 116
SHEET 3 AA3 5 ASN A 133 TYR A 137 1 N GLY A 136 O LEU A 163
SHEET 4 AA3 5 ASN A 179 LYS A 183 -1 O LYS A 183 N ASN A 133
SHEET 5 AA3 5 MET A 192 VAL A 193 -1 O MET A 192 N TYR A 182
SHEET 1 AA4 5 ARG A 217 GLU A 218 0
SHEET 2 AA4 5 ASN A 266 ASP A 271 1 O HIS A 269 N ARG A 217
SHEET 3 AA4 5 PHE A 234 HIS A 239 1 N LEU A 235 O ASN A 266
SHEET 4 AA4 5 VAL A 291 ASP A 295 -1 O VAL A 291 N PHE A 238
SHEET 5 AA4 5 MET A 300 VAL A 302 -1 O TYR A 301 N ILE A 294
CISPEP 1 TYR A 78 PRO A 79 0 -7.74
CISPEP 2 CYS A 289 PRO A 290 0 4.94
SITE 1 AC1 2 SER A 296 TYR A 301
CRYST1 81.630 81.630 139.910 90.00 90.00 120.00 P 31 2 1 6
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 0.012250 0.007073 0.000000 0.00000
SCALE2 0.000000 0.014146 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007147 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
