HEADER RNA BINDING PROTEIN 03-DEC-14 4X4R
TITLE CRYSTAL STRUCTURE OF THE A.FULGIDUS CCA-ADDING ENZYME IN COMPLEX WITH
TITLE 2 A G70A ARGINYL-TRNA MINIHELIX ENDING IN CCACC AND AMPCPP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CCA-ADDING ENZYME;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: A. FULGIDUS CCA-ADDING ENZYME;
COMPND 5 SYNONYM: CCA TRNA NUCLEOTIDYLTRANSFERASE,TRNA CCA-PYROPHOSPHORYLASE,
COMPND 6 TRNA ADENYLYL-/CYTIDYLYL- TRANSFERASE,TRNA NUCLEOTIDYLTRANSFERASE,
COMPND 7 TRNA-NT;
COMPND 8 EC: 2.7.7.72;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: G70A TRNA MINIHELIX ENDING IN CCACC;
COMPND 12 CHAIN: B, D;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: RNA (5'-D(*CP*G)-3');
COMPND 16 CHAIN: H;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
SOURCE 5 GENE: CCA, AF_2156;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-RNA COMPLEX, TRNA, NON-CODING RNA, CCA-ADDING ENZYME,
KEYWDS 2 NUCLEOTIDYLTRANSFERASE, NCRNA, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-D.KUHN,L.JOSHUA-TOR
REVDAT 6 27-DEC-23 4X4R 1 LINK
REVDAT 5 20-NOV-19 4X4R 1 REMARK
REVDAT 4 22-NOV-17 4X4R 1 SOURCE REMARK
REVDAT 3 25-FEB-15 4X4R 1 REMARK
REVDAT 2 18-FEB-15 4X4R 1 JRNL REMARK
REVDAT 1 11-FEB-15 4X4R 0
JRNL AUTH C.D.KUHN,J.E.WILUSZ,Y.ZHENG,P.A.BEAL,L.JOSHUA-TOR
JRNL TITL ON-ENZYME REFOLDING PERMITS SMALL RNA AND TRNA SURVEILLANCE
JRNL TITL 2 BY THE CCA-ADDING ENZYME.
JRNL REF CELL V. 160 644 2015
JRNL REFN ISSN 1097-4172
JRNL PMID 25640237
JRNL DOI 10.1016/J.CELL.2015.01.005
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 24030
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1230
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 29.9077 - 6.6392 1.00 2708 139 0.1743 0.1708
REMARK 3 2 6.6392 - 5.2792 0.99 2539 168 0.2029 0.2820
REMARK 3 3 5.2792 - 4.6146 1.00 2560 138 0.1826 0.2474
REMARK 3 4 4.6146 - 4.1939 1.00 2505 142 0.1858 0.2539
REMARK 3 5 4.1939 - 3.8940 1.00 2542 126 0.2157 0.2570
REMARK 3 6 3.8940 - 3.6649 1.00 2506 118 0.2178 0.3096
REMARK 3 7 3.6649 - 3.4816 1.00 2501 138 0.2397 0.3087
REMARK 3 8 3.4816 - 3.3303 1.00 2534 124 0.2645 0.3594
REMARK 3 9 3.3303 - 3.2022 0.98 2405 137 0.2790 0.3778
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.45
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 : 0.003 9153
REMARK 3 ANGLE : 0.684 12635
REMARK 3 CHIRALITY : 0.028 1387
REMARK 3 PLANARITY : 0.004 1375
REMARK 3 DIHEDRAL : 13.639 3716
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:89 OR RESSEQ
REMARK 3 100:257 OR RESSEQ 262:437 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 3:89 OR RESSEQ
REMARK 3 100:257 OR RESSEQ 262:437 )
REMARK 3 ATOM PAIRS NUMBER : 3991
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:17 OR RESSEQ 20:25
REMARK 3 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1:17 OR RESSEQ 20:25
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 540
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4X4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000202146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24077
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350, 0.2M NAK TARTRATE, 0.1M
REMARK 280 MES 6.8, PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 55.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 108.68400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 108.68400
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 300 REMARK: ONE CCA-ADDING ENZYME AND ONE TRNA MOLECULE FOR THE
REMARK 300 BIOLOGICALLY FUNCTIONAL UNIT.
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, 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H
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 ASP A 444
REMARK 465 LYS A 445
REMARK 465 LEU A 446
REMARK 465 ALA A 447
REMARK 465 ALA A 448
REMARK 465 ALA A 449
REMARK 465 LEU A 450
REMARK 465 GLU A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 A B 29
REMARK 465 U B 30
REMARK 465 SER C 438
REMARK 465 ASN C 439
REMARK 465 SER C 440
REMARK 465 SER C 441
REMARK 465 SER C 442
REMARK 465 VAL C 443
REMARK 465 ASP C 444
REMARK 465 LYS C 445
REMARK 465 LEU C 446
REMARK 465 ALA C 447
REMARK 465 ALA C 448
REMARK 465 ALA C 449
REMARK 465 LEU C 450
REMARK 465 GLU C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 465 HIS C 456
REMARK 465 HIS C 457
REMARK 465 G D 18
REMARK 465 G D 26
REMARK 465 C D 27
REMARK 465 G D 28
REMARK 465 A D 29
REMARK 465 U D 30
REMARK 465 C D 31
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 O2' A B 17 OP2 U B 19 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS C 269 O2' G H 2 1554 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 G B 1 P G B 1 OP3 -0.127
REMARK 500 G D 1 P G D 1 OP3 -0.125
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 SER A 57 49.84 -109.86
REMARK 500 GLU A 96 -64.22 -136.29
REMARK 500 GLU A 119 116.75 61.46
REMARK 500 ASN A 122 71.21 -104.66
REMARK 500 ILE A 123 150.34 -48.08
REMARK 500 ALA A 248 80.37 -163.02
REMARK 500 MET A 314 74.27 49.44
REMARK 500 LEU A 316 -69.84 -91.62
REMARK 500 GLU A 350 -72.52 -63.81
REMARK 500 HIS A 396 40.82 -99.36
REMARK 500 TYR A 411 138.46 -177.28
REMARK 500 PRO A 424 48.87 -72.48
REMARK 500 LYS C 2 -160.94 -75.97
REMARK 500 SER C 57 49.49 -109.94
REMARK 500 ARG C 93 108.33 -167.16
REMARK 500 GLU C 96 -60.80 -144.07
REMARK 500 GLU C 119 118.11 63.37
REMARK 500 ASN C 122 70.84 -105.25
REMARK 500 ALA C 248 80.44 -163.63
REMARK 500 LEU C 260 67.27 62.40
REMARK 500 MET C 314 74.48 50.92
REMARK 500 LEU C 316 -69.89 -92.50
REMARK 500 GLU C 350 -70.34 -63.84
REMARK 500 HIS C 396 41.06 -99.41
REMARK 500 LEU C 400 30.85 -91.72
REMARK 500 TYR C 411 142.29 -179.48
REMARK 500 PRO C 424 49.73 -72.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD2
REMARK 620 2 APC A 501 O2G 145.9
REMARK 620 3 APC A 501 O1B 86.8 59.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 47 OG
REMARK 620 2 ASP C 61 OD2 137.3
REMARK 620 3 APC C 501 O1B 73.4 100.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue APC A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue APC C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TAR C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X4N RELATED DB: PDB
REMARK 900 RELATED ID: 4X4O RELATED DB: PDB
REMARK 900 RELATED ID: 4X4P RELATED DB: PDB
REMARK 900 RELATED ID: 4X4Q RELATED DB: PDB
REMARK 900 RELATED ID: 4X4S RELATED DB: PDB
REMARK 900 RELATED ID: 4X4T RELATED DB: PDB
REMARK 900 RELATED ID: 4X4U RELATED DB: PDB
REMARK 900 RELATED ID: 4X4V RELATED DB: PDB
REMARK 900 RELATED ID: 4X4W RELATED DB: PDB
REMARK 900 RELATED ID: 4X4X RELATED DB: PDB
DBREF 4X4R A 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 4X4R B 1 37 PDB 4X4R 4X4R 1 37
DBREF 4X4R C 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 4X4R D 1 37 PDB 4X4R 4X4R 1 37
DBREF 4X4R H 1 2 PDB 4X4R 4X4R 1 2
SEQADV 4X4R SER A 438 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ASN A 439 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER A 440 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER A 441 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER A 442 UNP O28126 EXPRESSION TAG
SEQADV 4X4R VAL A 443 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ASP A 444 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LYS A 445 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LEU A 446 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA A 447 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA A 448 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA A 449 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LEU A 450 UNP O28126 EXPRESSION TAG
SEQADV 4X4R GLU A 451 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 452 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 453 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 454 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 455 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 456 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS A 457 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER C 438 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ASN C 439 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER C 440 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER C 441 UNP O28126 EXPRESSION TAG
SEQADV 4X4R SER C 442 UNP O28126 EXPRESSION TAG
SEQADV 4X4R VAL C 443 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ASP C 444 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LYS C 445 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LEU C 446 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA C 447 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA C 448 UNP O28126 EXPRESSION TAG
SEQADV 4X4R ALA C 449 UNP O28126 EXPRESSION TAG
SEQADV 4X4R LEU C 450 UNP O28126 EXPRESSION TAG
SEQADV 4X4R GLU C 451 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 452 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 453 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 454 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 455 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 456 UNP O28126 EXPRESSION TAG
SEQADV 4X4R HIS C 457 UNP O28126 EXPRESSION TAG
SEQRES 1 A 457 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 A 457 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 A 457 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 A 457 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 A 457 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 A 457 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 A 457 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 A 457 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 A 457 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 A 457 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 A 457 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 A 457 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 A 457 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 A 457 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 A 457 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 A 457 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 A 457 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 A 457 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 A 457 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 A 457 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 A 457 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 A 457 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 A 457 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 A 457 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 A 457 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 A 457 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 A 457 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 A 457 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 A 457 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 A 457 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 A 457 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 A 457 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 A 457 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 A 457 CYS GLU MET MET GLY VAL LYS ASP SER ASN SER SER SER
SEQRES 35 A 457 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 36 A 457 HIS HIS
SEQRES 1 B 37 G G C C G C G G C A G G U
SEQRES 2 B 37 U C G A G U C C U G C C G
SEQRES 3 B 37 C G A U C G C C A C C
SEQRES 1 C 457 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 C 457 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 C 457 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 C 457 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 C 457 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 C 457 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 C 457 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 C 457 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 C 457 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 C 457 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 C 457 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 C 457 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 C 457 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 C 457 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 C 457 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 C 457 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 C 457 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 C 457 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 C 457 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 C 457 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 C 457 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 C 457 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 C 457 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 C 457 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 C 457 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 C 457 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 C 457 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 C 457 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 C 457 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 C 457 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 C 457 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 C 457 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 C 457 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 C 457 CYS GLU MET MET GLY VAL LYS ASP SER ASN SER SER SER
SEQRES 35 C 457 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 36 C 457 HIS HIS
SEQRES 1 D 37 G G C C G C G G C A G G U
SEQRES 2 D 37 U C G A G U C C U G C C G
SEQRES 3 D 37 C G A U C G C C A C C
SEQRES 1 H 2 C G
HET APC A 501 45
HET MG A 502 1
HET MES A 503 25
HET GOL A 504 14
HET GOL A 505 14
HET APC C 501 45
HET MG C 502 1
HET GOL C 503 14
HET TAR C 504 14
HET PEG C 505 17
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM MG MAGNESIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM TAR D(-)-TARTARIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 6 APC 2(C11 H18 N5 O12 P3)
FORMUL 7 MG 2(MG 2+)
FORMUL 8 MES C6 H13 N O4 S
FORMUL 9 GOL 3(C3 H8 O3)
FORMUL 14 TAR C4 H6 O6
FORMUL 15 PEG C4 H10 O3
HELIX 1 AA1 LYS A 2 ILE A 15 1 14
HELIX 2 AA2 ASP A 17 LEU A 38 1 22
HELIX 3 AA3 GLY A 46 ARG A 50 1 5
HELIX 4 AA4 SER A 71 LEU A 87 1 17
HELIX 5 AA5 ARG A 129 GLU A 138 1 10
HELIX 6 AA6 LYS A 144 ALA A 157 1 14
HELIX 7 AA7 SER A 171 GLY A 183 1 13
HELIX 8 AA8 SER A 184 ARG A 193 1 10
HELIX 9 AA9 ALA A 204 GLY A 206 5 3
HELIX 10 AB1 SER A 231 ALA A 248 1 18
HELIX 11 AB2 SER A 250 PHE A 254 5 5
HELIX 12 AB3 GLU A 263 GLY A 275 1 13
HELIX 13 AB4 VAL A 289 GLU A 311 1 23
HELIX 14 AB5 ASP A 351 ARG A 361 1 11
HELIX 15 AB6 THR A 384 HIS A 396 1 13
HELIX 16 AB7 TRP A 397 LEU A 400 5 4
HELIX 17 AB8 GLY A 401 TYR A 411 1 11
HELIX 18 AB9 GLY A 417 LYS A 422 1 6
HELIX 19 AC1 VAL A 425 GLY A 434 1 10
HELIX 20 AC2 LYS C 2 ILE C 15 1 14
HELIX 21 AC3 ASP C 17 GLY C 39 1 23
HELIX 22 AC4 GLY C 46 ARG C 50 1 5
HELIX 23 AC5 SER C 71 LEU C 87 1 17
HELIX 24 AC6 ASP C 128 GLU C 138 1 11
HELIX 25 AC7 LYS C 144 ALA C 157 1 14
HELIX 26 AC8 SER C 171 GLY C 183 1 13
HELIX 27 AC9 SER C 184 ARG C 193 1 10
HELIX 28 AD1 ALA C 204 GLY C 206 5 3
HELIX 29 AD2 SER C 231 ALA C 248 1 18
HELIX 30 AD3 SER C 250 LYS C 255 5 6
HELIX 31 AD4 GLU C 263 GLY C 275 1 13
HELIX 32 AD5 VAL C 289 GLU C 311 1 23
HELIX 33 AD6 ASP C 351 ARG C 361 1 11
HELIX 34 AD7 THR C 384 HIS C 396 1 13
HELIX 35 AD8 TRP C 397 LEU C 400 5 4
HELIX 36 AD9 GLY C 401 TYR C 411 1 11
HELIX 37 AE1 GLY C 417 LYS C 422 1 6
HELIX 38 AE2 VAL C 425 GLY C 434 1 10
SHEET 1 AA1 5 TYR A 42 VAL A 45 0
SHEET 2 AA1 5 GLU A 59 PHE A 66 -1 O PHE A 63 N VAL A 43
SHEET 3 AA1 5 VAL A 107 TYR A 115 1 O GLU A 108 N ILE A 60
SHEET 4 AA1 5 VAL A 100 VAL A 104 -1 N VAL A 100 O VAL A 111
SHEET 5 AA1 5 SER A 89 GLU A 91 -1 N SER A 89 O VAL A 103
SHEET 1 AA2 4 GLU A 207 LYS A 210 0
SHEET 2 AA2 4 THR A 199 ASP A 202 -1 N VAL A 200 O ARG A 209
SHEET 3 AA2 4 PHE A 215 ASP A 218 1 O PHE A 215 N ILE A 201
SHEET 4 AA2 4 ASP A 221 ASN A 225 -1 O ARG A 224 N ASP A 218
SHEET 1 AA3 2 HIS A 258 PRO A 259 0
SHEET 2 AA3 2 ASN A 439 SER A 440 -1 O SER A 440 N HIS A 258
SHEET 1 AA4 4 PRO A 315 ALA A 322 0
SHEET 2 AA4 4 PHE A 326 CYS A 333 -1 O GLU A 332 N LEU A 316
SHEET 3 AA4 4 ALA A 277 ARG A 284 -1 N ALA A 277 O CYS A 333
SHEET 4 AA4 4 GLU A 413 SER A 416 -1 O ILE A 415 N ALA A 280
SHEET 1 AA5 3 VAL A 341 GLN A 348 0
SHEET 2 AA5 3 ARG A 373 MET A 379 -1 O TRP A 374 N GLY A 346
SHEET 3 AA5 3 PHE A 368 GLU A 370 -1 N PHE A 368 O TRP A 375
SHEET 1 AA6 5 TYR C 42 VAL C 45 0
SHEET 2 AA6 5 GLU C 59 PHE C 66 -1 O PHE C 63 N VAL C 43
SHEET 3 AA6 5 VAL C 107 TYR C 115 1 O VAL C 112 N LEU C 64
SHEET 4 AA6 5 VAL C 100 VAL C 104 -1 N GLY C 102 O VAL C 109
SHEET 5 AA6 5 SER C 89 GLU C 91 -1 N GLU C 91 O HIS C 101
SHEET 1 AA7 4 GLU C 207 LYS C 210 0
SHEET 2 AA7 4 THR C 199 ASP C 202 -1 N VAL C 200 O ARG C 209
SHEET 3 AA7 4 PHE C 215 ASP C 218 1 O PHE C 215 N ILE C 201
SHEET 4 AA7 4 ASP C 221 ASN C 225 -1 O ARG C 224 N ASP C 218
SHEET 1 AA8 4 PRO C 315 ALA C 322 0
SHEET 2 AA8 4 PHE C 326 CYS C 333 -1 O LEU C 330 N ALA C 319
SHEET 3 AA8 4 ALA C 277 ARG C 284 -1 N ALA C 277 O CYS C 333
SHEET 4 AA8 4 GLU C 413 SER C 416 -1 O GLU C 413 N LYS C 282
SHEET 1 AA9 3 VAL C 341 GLN C 348 0
SHEET 2 AA9 3 ARG C 373 MET C 379 -1 O TRP C 374 N GLY C 346
SHEET 3 AA9 3 PHE C 368 GLU C 370 -1 N PHE C 368 O TRP C 375
LINK OD2 ASP A 61 MG MG A 502 1555 1555 2.65
LINK O2G APC A 501 MG MG A 502 1555 1555 2.91
LINK O1B APC A 501 MG MG A 502 1555 1555 2.63
LINK OG SER C 47 MG MG C 502 1555 1555 2.92
LINK OD2 ASP C 61 MG MG C 502 1555 1555 2.62
LINK O1B APC C 501 MG MG C 502 1555 1555 2.39
SITE 1 AC1 13 SER A 47 ARG A 50 GLU A 59 ASP A 61
SITE 2 AC1 13 THR A 130 HIS A 133 LYS A 152 TYR A 161
SITE 3 AC1 13 ARG A 224 MG A 502 A B 35 C B 36
SITE 4 AC1 13 C B 37
SITE 1 AC2 4 SER A 47 GLU A 59 ASP A 61 APC A 501
SITE 1 AC3 2 ILE A 92 TYR A 94
SITE 1 AC4 3 VAL A 200 ARG A 209 GLU A 222
SITE 1 AC5 3 ARG A 317 SER A 318 GLU C 370
SITE 1 AC6 15 GLY C 46 SER C 47 ARG C 50 GLU C 59
SITE 2 AC6 15 ASP C 61 THR C 130 HIS C 133 LYS C 152
SITE 3 AC6 15 TYR C 161 TYR C 173 ARG C 224 MG C 502
SITE 4 AC6 15 A D 35 C D 36 C D 37
SITE 1 AC7 4 SER C 47 GLU C 59 ASP C 61 APC C 501
SITE 1 AC8 2 GLU C 311 ARG C 344
SITE 1 AC9 7 HIS A 240 ARG A 243 GLU A 244 GLU A 247
SITE 2 AC9 7 GLU C 352 VAL C 355 LYS C 356
SITE 1 AD1 5 PHE A 349 GLU A 352 VAL A 355 HIS C 240
SITE 2 AD1 5 ARG C 243
CRYST1 111.100 217.368 58.562 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 0.009001 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004600 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017076 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
