HEADER PROTEIN BINDING 21-JAN-15 4XRU
TITLE STRUCTURE OF PNKP1/RNL/HEN1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PNKP1;
COMPND 3 CHAIN: A, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: RNL;
COMPND 7 CHAIN: B, E;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HEN1;
COMPND 11 CHAIN: C, F;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAPNOCYTOPHAGA GINGIVALIS;
SOURCE 3 ORGANISM_TAXID: 553178;
SOURCE 4 STRAIN: ATCC 33624;
SOURCE 5 GENE: CAPGI0001_2485;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CAPNOCYTOPHAGA GINGIVALIS;
SOURCE 10 ORGANISM_TAXID: 553178;
SOURCE 11 STRAIN: ATCC 33624;
SOURCE 12 GENE: CAPGI0001_2487;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: CAPNOCYTOPHAGA GINGIVALIS;
SOURCE 17 ORGANISM_TAXID: 553178;
SOURCE 18 STRAIN: ATCC 33624;
SOURCE 19 GENE: CAPGI0001_1566;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RNA REPAIR, KINASE, PHOSPHATASE, METHYLTRANSFERASE, LIGASE, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR P.WANG
REVDAT 2 29-APR-15 4XRU 1 JRNL
REVDAT 1 22-APR-15 4XRU 0
JRNL AUTH P.WANG,K.SELVADURAI,R.H.HUANG
JRNL TITL RECONSTITUTION AND STRUCTURE OF A BACTERIAL PNKP1-RNL-HEN1
JRNL TITL 2 RNA REPAIR COMPLEX.
JRNL REF NAT COMMUN V. 6 6876 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25882814
JRNL DOI 10.1038/NCOMMS7876
REMARK 2
REMARK 2 RESOLUTION. 3.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 3.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 56120
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.780
REMARK 3 FREE R VALUE TEST SET COUNT : 4285
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.38
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2319 4.9190 -23.1882
REMARK 3 T TENSOR
REMARK 3 T11: 0.5456 T22: 0.4341
REMARK 3 T33: 0.5095 T12: -0.1253
REMARK 3 T13: -0.0453 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.4561 L22: 0.6156
REMARK 3 L33: 0.0456 L12: -0.5367
REMARK 3 L13: -0.0923 L23: 0.0821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0821 S12: 0.1088 S13: -0.0424
REMARK 3 S21: 0.0013 S22: -0.0897 S23: -0.0150
REMARK 3 S31: 0.0006 S32: -0.0218 S33: 0.0089
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 4XRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65456
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
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 (%): 74.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, PH 6.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 93.62250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 97150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 MSE A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 ASP A 124
REMARK 465 LYS A 125
REMARK 465 ARG A 126
REMARK 465 CYS A 127
REMARK 465 GLU A 128
REMARK 465 GLN A 129
REMARK 465 THR A 130
REMARK 465 GLY A 131
REMARK 465 LYS A 132
REMARK 465 PHE A 133
REMARK 465 ILE A 134
REMARK 465 PRO A 135
REMARK 465 LYS A 136
REMARK 465 SER A 137
REMARK 465 ALA A 138
REMARK 465 ILE A 139
REMARK 465 GLU A 140
REMARK 465 LYS A 141
REMARK 465 ASP C 378
REMARK 465 GLU C 379
REMARK 465 ASP C 380
REMARK 465 PRO C 381
REMARK 465 GLU C 382
REMARK 465 SER C 383
REMARK 465 LEU C 384
REMARK 465 ARG C 385
REMARK 465 HIS C 386
REMARK 465 GLU C 387
REMARK 465 ASP C 388
REMARK 465 HIS C 389
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 ALA D 3
REMARK 465 CYS D 123
REMARK 465 ASP D 124
REMARK 465 LYS D 125
REMARK 465 ARG D 126
REMARK 465 CYS D 127
REMARK 465 GLU D 128
REMARK 465 GLN D 129
REMARK 465 THR D 130
REMARK 465 GLY D 131
REMARK 465 LYS D 132
REMARK 465 PHE D 133
REMARK 465 ILE D 134
REMARK 465 PRO D 135
REMARK 465 LYS D 136
REMARK 465 SER D 137
REMARK 465 ALA D 138
REMARK 465 ILE D 139
REMARK 465 GLU D 140
REMARK 465 LYS D 141
REMARK 465 HIS D 142
REMARK 465 VAL D 143
REMARK 465 THR D 144
REMARK 465 MET E 1
REMARK 465 ASP F 378
REMARK 465 GLU F 379
REMARK 465 ASP F 380
REMARK 465 PRO F 381
REMARK 465 GLU F 382
REMARK 465 SER F 383
REMARK 465 LEU F 384
REMARK 465 ARG F 385
REMARK 465 HIS F 386
REMARK 465 GLU F 387
REMARK 465 ASP F 388
REMARK 465 HIS F 389
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 OD2 ASP D 173 OG SER D 175 1.99
REMARK 500 OG1 THR E 25 OE2 GLU E 387 2.03
REMARK 500 O ASN C 33 OG1 THR C 53 2.06
REMARK 500 O HOH B 601 O HOH B 609 2.07
REMARK 500 O PRO E 30 OG SER E 40 2.07
REMARK 500 O ALA A 19 OG SER A 22 2.14
REMARK 500 O VAL D 98 OG1 THR D 102 2.16
REMARK 500 OE1 GLU B 55 OH TYR B 266 2.17
REMARK 500 O HIS C 354 OG SER C 357 2.17
REMARK 500 OE2 GLU E 43 O HOH E 611 2.18
REMARK 500 OE2 GLU C 338 O HOH C 616 2.19
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 C 203 C - N - CA ANGL. DEV. = -11.6 DEGREES
REMARK 500 PRO D 20 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 LEU D 91 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 GLY F 273 N - CA - C ANGL. DEV. = -15.2 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 ASN A 5 -27.38 83.66
REMARK 500 ARG A 47 38.11 -71.12
REMARK 500 SER A 54 42.58 -72.65
REMARK 500 ALA A 86 91.36 -54.60
REMARK 500 ASN A 88 -82.37 -38.58
REMARK 500 SER A 89 95.06 53.21
REMARK 500 SER A 90 -95.91 -163.53
REMARK 500 LEU A 91 -49.73 179.41
REMARK 500 THR A 102 104.43 -59.76
REMARK 500 GLU A 103 -16.78 160.08
REMARK 500 LEU A 114 119.94 -168.46
REMARK 500 PRO A 115 127.48 -35.36
REMARK 500 ARG A 122 43.20 -107.01
REMARK 500 THR A 144 92.35 -54.10
REMARK 500 TYR A 148 39.54 -61.29
REMARK 500 LYS A 150 69.32 -115.87
REMARK 500 GLU A 151 79.14 -18.07
REMARK 500 PHE A 153 -28.99 68.01
REMARK 500 ASP A 154 116.46 53.60
REMARK 500 PHE A 155 33.15 -81.87
REMARK 500 LYS A 163 -43.57 76.12
REMARK 500 SER A 166 63.03 -103.67
REMARK 500 TYR A 169 -139.40 -76.74
REMARK 500 ASP A 173 105.46 -52.23
REMARK 500 LEU A 184 -72.02 -95.70
REMARK 500 ASP A 185 107.51 -52.24
REMARK 500 THR A 187 -51.42 -139.83
REMARK 500 SER A 189 88.95 -152.75
REMARK 500 ARG A 194 150.11 -46.73
REMARK 500 ASN A 198 77.62 -110.09
REMARK 500 ALA A 199 41.41 -83.00
REMARK 500 THR A 201 25.89 -73.00
REMARK 500 ASP A 205 154.30 -46.65
REMARK 500 ASP A 260 -70.78 -81.17
REMARK 500 TYR A 261 -3.04 74.33
REMARK 500 GLU A 275 -93.64 -82.92
REMARK 500 ASN A 308 -148.63 -111.82
REMARK 500 PHE B 22 -96.39 -107.59
REMARK 500 SER B 23 159.05 172.83
REMARK 500 ASN B 84 -154.47 -85.26
REMARK 500 HIS B 90 25.72 -155.91
REMARK 500 GLN B 95 -34.38 -32.65
REMARK 500 GLU B 135 -74.49 -103.59
REMARK 500 GLU B 165 152.62 -44.65
REMARK 500 LEU B 169 -47.67 81.83
REMARK 500 ASP B 174 32.23 -74.92
REMARK 500 LYS B 181 8.92 -69.78
REMARK 500 GLU B 182 65.79 -160.82
REMARK 500 LYS B 184 173.60 33.06
REMARK 500 LYS B 186 87.70 -36.50
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER C 129 LYS C 130 -147.78
REMARK 500 HIS C 342 ASN C 343 136.13
REMARK 500 ARG D 92 SER D 93 148.57
REMARK 500 LYS E 181 GLU E 182 148.94
REMARK 500 ASP E 185 LYS E 186 149.66
REMARK 500 TRP F 101 LEU F 102 -146.06
REMARK 500 CYS F 272 GLY F 273 145.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 SAH F 501
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 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 183 OD2
REMARK 620 2 ASP A 185 O 77.5
REMARK 620 3 ASP A 288 OD1 111.0 79.3
REMARK 620 4 ASP A 288 OD2 61.4 79.2 50.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 183 OD2
REMARK 620 2 ASP D 185 O 88.2
REMARK 620 3 ASP D 288 OD2 118.5 77.1
REMARK 620 4 HOH D 507 O 91.6 129.3 142.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B 501 O2A
REMARK 620 2 HOH B 606 O 94.2
REMARK 620 3 HOH B 608 O 57.3 81.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP E 501 O2A
REMARK 620 2 HOH E 607 O 91.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XRP RELATED DB: PDB
DBREF 4XRU A 1 312 UNP C2M8N3 C2M8N3_CAPGI 1 312
DBREF 4XRU B 1 394 UNP C2M8N4 C2M8N4_CAPGI 1 394
DBREF 4XRU C 1 436 UNP C2M7I7 C2M7I7_CAPGI 1 436
DBREF 4XRU D 1 312 UNP C2M8N3 C2M8N3_CAPGI 1 312
DBREF 4XRU E 1 394 UNP C2M8N4 C2M8N4_CAPGI 1 394
DBREF 4XRU F 1 436 UNP C2M7I7 C2M7I7_CAPGI 1 436
SEQADV 4XRU THR B 269 UNP C2M8N4 ALA 269 CONFLICT
SEQADV 4XRU GLU B 329 UNP C2M8N4 GLN 329 CONFLICT
SEQADV 4XRU THR E 269 UNP C2M8N4 ALA 269 CONFLICT
SEQADV 4XRU GLU E 329 UNP C2M8N4 GLN 329 CONFLICT
SEQRES 1 A 312 MSE SER ALA LYS ASN ASN THR HIS HIS PHE PRO LYS LEU
SEQRES 2 A 312 LEU ILE LEU VAL GLY ALA PRO GLY SER GLY LYS SER THR
SEQRES 3 A 312 PHE ALA ARG TYR PHE ILE ARG THR GLU ASP ASN TRP VAL
SEQRES 4 A 312 ARG VAL ASN ARG ASP ASP PHE ARG LEU MSE GLN PHE GLY
SEQRES 5 A 312 ASP SER LEU MSE SER PRO PHE TYR GLU GLU ARG ILE THR
SEQRES 6 A 312 LYS MSE VAL GLU ALA SER VAL ILE ALA LEU LEU LYS ASN
SEQRES 7 A 312 ARG THR ASN VAL ILE ILE ASP ALA THR ASN SER SER LEU
SEQRES 8 A 312 ARG SER LEU GLN ASP MSE VAL HIS THR TYR THR GLU TYR
SEQRES 9 A 312 ALA ASP ILE SER PHE LYS VAL PHE ASP LEU PRO VAL GLU
SEQRES 10 A 312 GLU LEU VAL LYS ARG CYS ASP LYS ARG CYS GLU GLN THR
SEQRES 11 A 312 GLY LYS PHE ILE PRO LYS SER ALA ILE GLU LYS HIS VAL
SEQRES 12 A 312 THR GLN LEU GLN TYR THR LYS GLU LYS PHE ASP PHE LYS
SEQRES 13 A 312 PRO ILE PRO ARG ALA LEU LYS GLU THR SER LEU THR TYR
SEQRES 14 A 312 ALA ASP GLN ASP THR SER LEU PRO LYS ALA VAL ILE CYS
SEQRES 15 A 312 ASP LEU ASP GLY THR LEU SER LEU LEU ASN GLY ARG ASP
SEQRES 16 A 312 PRO TYR ASN ALA SER THR ALA ASP GLN ASP LEU LEU ASN
SEQRES 17 A 312 THR PRO VAL ALA MSE VAL LEU LYS MSE ALA LYS GLN GLN
SEQRES 18 A 312 GLY TYR LYS VAL ILE LEU LEU SER GLY ARG GLU ASN ALA
SEQRES 19 A 312 TYR ARG GLU PRO THR GLU ARG PHE LEU ALA LYS TYR GLN
SEQRES 20 A 312 ILE ASP TYR ASP LEU LEU LEU MSE ARG ASP THR ASN ASP
SEQRES 21 A 312 TYR ARG LYS ASP ASN ILE ILE LYS LYS GLU LEU PHE LEU
SEQRES 22 A 312 GLU GLU ILE GLN GLY LYS TYR PHE VAL GLU PHE LEU LEU
SEQRES 23 A 312 ASP ASP ARG ASN GLN VAL VAL ASP MSE TRP ARG ARG GLU
SEQRES 24 A 312 LEU ALA LEU PRO CYS PHE GLN VAL ASN TYR GLY ASP PHE
SEQRES 1 B 394 MET GLU ASP LYS THR LEU ILE LYS LYS ARG ILE ASP TRP
SEQRES 2 B 394 PHE CYS LYS ASN LYS ILE ASN ALA PHE SER PRO THR ILE
SEQRES 3 B 394 SER PRO ALA PRO LYS SER VAL GLU ARG ASN GLU ILE GLU
SEQRES 4 B 394 SER LEU TYR GLU GLY ILE LEU TRP PHE VAL LEU ASN GLY
SEQRES 5 B 394 VAL LYS GLU ILE VAL ILE GLU LYS LYS TYR MET GLY SER
SEQRES 6 B 394 TYR CYS ASP ILE TYR LEU HIS ARG ARG LEU GLU ASP THR
SEQRES 7 B 394 TYR LEU VAL SER ARG ASN GLY TYR LYS ILE ASN HIS LEU
SEQRES 8 B 394 ASP GLN GLU GLN CYS LEU ARG ALA LEU GLN GLY LEU HIS
SEQRES 9 B 394 ASP ARG PHE SER TRP ASP GLY VAL GLU LEU ARG ILE ILE
SEQRES 10 B 394 GLN SER GLU LEU MET PRO TRP SER ILE LEU GLY LYS GLY
SEQRES 11 B 394 LEU ILE ASN ASN GLU PHE SER ALA TYR TYR ILE SER HIS
SEQRES 12 B 394 GLU ILE HIS ALA GLU TYR LEU VAL GLN SER SER LEU TYR
SEQRES 13 B 394 GLU LYS LEU GLN LYS ILE GLN GLN GLU PRO ALA TYR LEU
SEQRES 14 B 394 SER PHE VAL ALA ASP ALA LYS VAL LEU SER ALA LYS GLU
SEQRES 15 B 394 LEU LYS ASP LYS TYR PRO MET HIS ILE ILE ARG GLN TYR
SEQRES 16 B 394 GLN SER ILE ARG ASP PHE LYS PHE LEU ASP LEU PRO HIS
SEQRES 17 B 394 TYR GLN GLN ASN ILE GLN LEU PHE LYS ARG GLN LEU ASP
SEQRES 18 B 394 ILE PHE GLY LYS GLU ALA ALA PRO PHE PHE LYS PRO PHE
SEQRES 19 B 394 ASN ILE LEU LYS GLU VAL TYR THR ASP GLY ARG GLU HIS
SEQRES 20 B 394 PHE VAL ASN ASP ASN LEU SER PHE GLN GLN ILE ASN ASP
SEQRES 21 B 394 ASP ASP PHE LEU HIS TYR GLN PHE THR ASP ARG GLU ASP
SEQRES 22 B 394 PHE GLU ALA LYS TYR PRO GLN ILE ARG ALA TRP VAL ASP
SEQRES 23 B 394 GLN VAL ASN GLN SER ASP GLU GLU GLY VAL VAL ILE LYS
SEQRES 24 B 394 PRO ARG THR ALA PHE LEU PRO GLY MET PRO PRO ALA PHE
SEQRES 25 B 394 LYS VAL ARG ASN ASN ASP TYR LEU THR LEU VAL TYR GLY
SEQRES 26 B 394 VAL ASP PHE GLU ASP ARG LEU GLN GLU GLN ILE ALA LYS
SEQRES 27 B 394 ARG ASN ILE LYS GLY LYS LEU ARG CYS SER ILE ASN ASP
SEQRES 28 B 394 TRP ALA ILE ASN ALA LYS LEU LEU ALA ILE PRO TYR SER
SEQRES 29 B 394 GLU LEU GLY GLU GLU ASN TYR GLU LEU LYS ASN LEU VAL
SEQRES 30 B 394 LEU ASP ARG ILE LEU GLY GLU GLU ILE GLU ASN GLN LEU
SEQRES 31 B 394 ASP SER ARG LEU
SEQRES 1 C 436 MET ILE LEU GLN ILE HIS SER GLN ASN PRO HIS LEU LEU
SEQRES 2 C 436 ASP LEU LEU ASN LYS ASN PRO HIS THR ASP LEU GLY ILE
SEQRES 3 C 436 TYR ALA LYS SER LEU ARG ASN GLY GLN LEU ILE GLY ASN
SEQRES 4 C 436 ALA VAL SER ALA TYR GLN TYR ASP VAL VAL PHE GLN ASP
SEQRES 5 C 436 THR ARG TYR SER TYR LEU PRO GLU GLU SER ASN GLN ILE
SEQRES 6 C 436 ASP PHE GLN SER TYR CYS SER PRO LEU VAL ILE LEU HIS
SEQRES 7 C 436 ILE CYS ASN GLU PHE PHE LYS GLU LEU LEU GLN GLU LYS
SEQRES 8 C 436 GLN THR TYR TRP SER GLN GLN ILE LYS TRP LEU GLU ARG
SEQRES 9 C 436 THR ARG ALA GLU VAL ASP THR TYR PRO CYS THR ILE GLU
SEQRES 10 C 436 VAL LYS ASN LEU TYR ALA ASN SER THR TRP TYR SER LYS
SEQRES 11 C 436 GLY HIS PHE MET MET GLU ARG TYR PHE LYS ASN ILE HIS
SEQRES 12 C 436 ILE THR PRO ILE VAL GLY ASN ASN LEU SER LEU ARG VAL
SEQRES 13 C 436 GLU GLY LYS SER VAL PHE GLU ALA MET ASN LEU LEU SER
SEQRES 14 C 436 PHE ILE ALA VAL THR THR HIS ILE THR ASN THR TYR GLY
SEQRES 15 C 436 GLU TYR THR TYR ILE ASP ASP HIS PHE ALA GLN LYS TYR
SEQRES 16 C 436 ALA ARG ILE LEU THR ASN ILE PRO GLN VAL PRO TYR PHE
SEQRES 17 C 436 VAL PHE TYR LEU PHE ILE LYS ARG ALA ILE LYS SER GLU
SEQRES 18 C 436 ARG GLN PHE ALA GLU ILE LYS PRO MET PHE GLU ALA TYR
SEQRES 19 C 436 PHE LYS GLU GLU GLY LEU ASP ILE ASP PHE GLN PHE THR
SEQRES 20 C 436 ASP THR HIS GLY SER ARG MET ASP PHE ILE VAL LYS GLU
SEQRES 21 C 436 LEU GLY MET GLU TYR PRO ILE LEU ASP ILE GLY CYS GLY
SEQRES 22 C 436 GLU LEU LYS TYR TYR ARG ARG PHE MET ARG ARG ASN TYR
SEQRES 23 C 436 ASN TYR SER HIS PRO TYR PHE ALA THR ASP THR ASP LYS
SEQRES 24 C 436 SER VAL GLY ASP TYR ALA ALA LEU LEU LYS GLU ARG MET
SEQRES 25 C 436 GLU ALA ASP ASN LEU TYR PHE PHE SER ASP TRP THR ASP
SEQRES 26 C 436 TYR GLU TYR LYS ASN PRO VAL ASN ILE ILE LEU THR GLU
SEQRES 27 C 436 VAL ILE GLU HIS ASN THR PRO GLU ALA ALA GLU ALA LEU
SEQRES 28 C 436 VAL LYS HIS CYS LEU SER LEU ASN PHE HIS LYS MET ILE
SEQRES 29 C 436 ILE THR THR PRO ASN SER LEU PHE ASN LYS TYR TYR PHE
SEQRES 30 C 436 ASP GLU ASP PRO GLU SER LEU ARG HIS GLU ASP HIS HIS
SEQRES 31 C 436 PHE GLU TRP THR PRO GLN GLU PHE GLN ASP PHE ILE ARG
SEQRES 32 C 436 HIS CYS VAL GLY ASP THR SER LEU GLU VAL THR TYR CYS
SEQRES 33 C 436 GLY ILE GLY ASP ARG ILE ASN GLY GLU THR PRO THR GLN
SEQRES 34 C 436 ALA VAL VAL ILE THR ARG LYS
SEQRES 1 D 312 MSE SER ALA LYS ASN ASN THR HIS HIS PHE PRO LYS LEU
SEQRES 2 D 312 LEU ILE LEU VAL GLY ALA PRO GLY SER GLY LYS SER THR
SEQRES 3 D 312 PHE ALA ARG TYR PHE ILE ARG THR GLU ASP ASN TRP VAL
SEQRES 4 D 312 ARG VAL ASN ARG ASP ASP PHE ARG LEU MSE GLN PHE GLY
SEQRES 5 D 312 ASP SER LEU MSE SER PRO PHE TYR GLU GLU ARG ILE THR
SEQRES 6 D 312 LYS MSE VAL GLU ALA SER VAL ILE ALA LEU LEU LYS ASN
SEQRES 7 D 312 ARG THR ASN VAL ILE ILE ASP ALA THR ASN SER SER LEU
SEQRES 8 D 312 ARG SER LEU GLN ASP MSE VAL HIS THR TYR THR GLU TYR
SEQRES 9 D 312 ALA ASP ILE SER PHE LYS VAL PHE ASP LEU PRO VAL GLU
SEQRES 10 D 312 GLU LEU VAL LYS ARG CYS ASP LYS ARG CYS GLU GLN THR
SEQRES 11 D 312 GLY LYS PHE ILE PRO LYS SER ALA ILE GLU LYS HIS VAL
SEQRES 12 D 312 THR GLN LEU GLN TYR THR LYS GLU LYS PHE ASP PHE LYS
SEQRES 13 D 312 PRO ILE PRO ARG ALA LEU LYS GLU THR SER LEU THR TYR
SEQRES 14 D 312 ALA ASP GLN ASP THR SER LEU PRO LYS ALA VAL ILE CYS
SEQRES 15 D 312 ASP LEU ASP GLY THR LEU SER LEU LEU ASN GLY ARG ASP
SEQRES 16 D 312 PRO TYR ASN ALA SER THR ALA ASP GLN ASP LEU LEU ASN
SEQRES 17 D 312 THR PRO VAL ALA MSE VAL LEU LYS MSE ALA LYS GLN GLN
SEQRES 18 D 312 GLY TYR LYS VAL ILE LEU LEU SER GLY ARG GLU ASN ALA
SEQRES 19 D 312 TYR ARG GLU PRO THR GLU ARG PHE LEU ALA LYS TYR GLN
SEQRES 20 D 312 ILE ASP TYR ASP LEU LEU LEU MSE ARG ASP THR ASN ASP
SEQRES 21 D 312 TYR ARG LYS ASP ASN ILE ILE LYS LYS GLU LEU PHE LEU
SEQRES 22 D 312 GLU GLU ILE GLN GLY LYS TYR PHE VAL GLU PHE LEU LEU
SEQRES 23 D 312 ASP ASP ARG ASN GLN VAL VAL ASP MSE TRP ARG ARG GLU
SEQRES 24 D 312 LEU ALA LEU PRO CYS PHE GLN VAL ASN TYR GLY ASP PHE
SEQRES 1 E 394 MET GLU ASP LYS THR LEU ILE LYS LYS ARG ILE ASP TRP
SEQRES 2 E 394 PHE CYS LYS ASN LYS ILE ASN ALA PHE SER PRO THR ILE
SEQRES 3 E 394 SER PRO ALA PRO LYS SER VAL GLU ARG ASN GLU ILE GLU
SEQRES 4 E 394 SER LEU TYR GLU GLY ILE LEU TRP PHE VAL LEU ASN GLY
SEQRES 5 E 394 VAL LYS GLU ILE VAL ILE GLU LYS LYS TYR MET GLY SER
SEQRES 6 E 394 TYR CYS ASP ILE TYR LEU HIS ARG ARG LEU GLU ASP THR
SEQRES 7 E 394 TYR LEU VAL SER ARG ASN GLY TYR LYS ILE ASN HIS LEU
SEQRES 8 E 394 ASP GLN GLU GLN CYS LEU ARG ALA LEU GLN GLY LEU HIS
SEQRES 9 E 394 ASP ARG PHE SER TRP ASP GLY VAL GLU LEU ARG ILE ILE
SEQRES 10 E 394 GLN SER GLU LEU MET PRO TRP SER ILE LEU GLY LYS GLY
SEQRES 11 E 394 LEU ILE ASN ASN GLU PHE SER ALA TYR TYR ILE SER HIS
SEQRES 12 E 394 GLU ILE HIS ALA GLU TYR LEU VAL GLN SER SER LEU TYR
SEQRES 13 E 394 GLU LYS LEU GLN LYS ILE GLN GLN GLU PRO ALA TYR LEU
SEQRES 14 E 394 SER PHE VAL ALA ASP ALA LYS VAL LEU SER ALA LYS GLU
SEQRES 15 E 394 LEU LYS ASP LYS TYR PRO MET HIS ILE ILE ARG GLN TYR
SEQRES 16 E 394 GLN SER ILE ARG ASP PHE LYS PHE LEU ASP LEU PRO HIS
SEQRES 17 E 394 TYR GLN GLN ASN ILE GLN LEU PHE LYS ARG GLN LEU ASP
SEQRES 18 E 394 ILE PHE GLY LYS GLU ALA ALA PRO PHE PHE LYS PRO PHE
SEQRES 19 E 394 ASN ILE LEU LYS GLU VAL TYR THR ASP GLY ARG GLU HIS
SEQRES 20 E 394 PHE VAL ASN ASP ASN LEU SER PHE GLN GLN ILE ASN ASP
SEQRES 21 E 394 ASP ASP PHE LEU HIS TYR GLN PHE THR ASP ARG GLU ASP
SEQRES 22 E 394 PHE GLU ALA LYS TYR PRO GLN ILE ARG ALA TRP VAL ASP
SEQRES 23 E 394 GLN VAL ASN GLN SER ASP GLU GLU GLY VAL VAL ILE LYS
SEQRES 24 E 394 PRO ARG THR ALA PHE LEU PRO GLY MET PRO PRO ALA PHE
SEQRES 25 E 394 LYS VAL ARG ASN ASN ASP TYR LEU THR LEU VAL TYR GLY
SEQRES 26 E 394 VAL ASP PHE GLU ASP ARG LEU GLN GLU GLN ILE ALA LYS
SEQRES 27 E 394 ARG ASN ILE LYS GLY LYS LEU ARG CYS SER ILE ASN ASP
SEQRES 28 E 394 TRP ALA ILE ASN ALA LYS LEU LEU ALA ILE PRO TYR SER
SEQRES 29 E 394 GLU LEU GLY GLU GLU ASN TYR GLU LEU LYS ASN LEU VAL
SEQRES 30 E 394 LEU ASP ARG ILE LEU GLY GLU GLU ILE GLU ASN GLN LEU
SEQRES 31 E 394 ASP SER ARG LEU
SEQRES 1 F 436 MET ILE LEU GLN ILE HIS SER GLN ASN PRO HIS LEU LEU
SEQRES 2 F 436 ASP LEU LEU ASN LYS ASN PRO HIS THR ASP LEU GLY ILE
SEQRES 3 F 436 TYR ALA LYS SER LEU ARG ASN GLY GLN LEU ILE GLY ASN
SEQRES 4 F 436 ALA VAL SER ALA TYR GLN TYR ASP VAL VAL PHE GLN ASP
SEQRES 5 F 436 THR ARG TYR SER TYR LEU PRO GLU GLU SER ASN GLN ILE
SEQRES 6 F 436 ASP PHE GLN SER TYR CYS SER PRO LEU VAL ILE LEU HIS
SEQRES 7 F 436 ILE CYS ASN GLU PHE PHE LYS GLU LEU LEU GLN GLU LYS
SEQRES 8 F 436 GLN THR TYR TRP SER GLN GLN ILE LYS TRP LEU GLU ARG
SEQRES 9 F 436 THR ARG ALA GLU VAL ASP THR TYR PRO CYS THR ILE GLU
SEQRES 10 F 436 VAL LYS ASN LEU TYR ALA ASN SER THR TRP TYR SER LYS
SEQRES 11 F 436 GLY HIS PHE MET MET GLU ARG TYR PHE LYS ASN ILE HIS
SEQRES 12 F 436 ILE THR PRO ILE VAL GLY ASN ASN LEU SER LEU ARG VAL
SEQRES 13 F 436 GLU GLY LYS SER VAL PHE GLU ALA MET ASN LEU LEU SER
SEQRES 14 F 436 PHE ILE ALA VAL THR THR HIS ILE THR ASN THR TYR GLY
SEQRES 15 F 436 GLU TYR THR TYR ILE ASP ASP HIS PHE ALA GLN LYS TYR
SEQRES 16 F 436 ALA ARG ILE LEU THR ASN ILE PRO GLN VAL PRO TYR PHE
SEQRES 17 F 436 VAL PHE TYR LEU PHE ILE LYS ARG ALA ILE LYS SER GLU
SEQRES 18 F 436 ARG GLN PHE ALA GLU ILE LYS PRO MET PHE GLU ALA TYR
SEQRES 19 F 436 PHE LYS GLU GLU GLY LEU ASP ILE ASP PHE GLN PHE THR
SEQRES 20 F 436 ASP THR HIS GLY SER ARG MET ASP PHE ILE VAL LYS GLU
SEQRES 21 F 436 LEU GLY MET GLU TYR PRO ILE LEU ASP ILE GLY CYS GLY
SEQRES 22 F 436 GLU LEU LYS TYR TYR ARG ARG PHE MET ARG ARG ASN TYR
SEQRES 23 F 436 ASN TYR SER HIS PRO TYR PHE ALA THR ASP THR ASP LYS
SEQRES 24 F 436 SER VAL GLY ASP TYR ALA ALA LEU LEU LYS GLU ARG MET
SEQRES 25 F 436 GLU ALA ASP ASN LEU TYR PHE PHE SER ASP TRP THR ASP
SEQRES 26 F 436 TYR GLU TYR LYS ASN PRO VAL ASN ILE ILE LEU THR GLU
SEQRES 27 F 436 VAL ILE GLU HIS ASN THR PRO GLU ALA ALA GLU ALA LEU
SEQRES 28 F 436 VAL LYS HIS CYS LEU SER LEU ASN PHE HIS LYS MET ILE
SEQRES 29 F 436 ILE THR THR PRO ASN SER LEU PHE ASN LYS TYR TYR PHE
SEQRES 30 F 436 ASP GLU ASP PRO GLU SER LEU ARG HIS GLU ASP HIS HIS
SEQRES 31 F 436 PHE GLU TRP THR PRO GLN GLU PHE GLN ASP PHE ILE ARG
SEQRES 32 F 436 HIS CYS VAL GLY ASP THR SER LEU GLU VAL THR TYR CYS
SEQRES 33 F 436 GLY ILE GLY ASP ARG ILE ASN GLY GLU THR PRO THR GLN
SEQRES 34 F 436 ALA VAL VAL ILE THR ARG LYS
MODRES 4XRU MSE A 49 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 56 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 67 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 97 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 213 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 217 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 255 MET MODIFIED RESIDUE
MODRES 4XRU MSE A 295 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 49 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 56 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 67 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 97 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 213 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 217 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 255 MET MODIFIED RESIDUE
MODRES 4XRU MSE D 295 MET MODIFIED RESIDUE
HET MSE A 49 8
HET MSE A 56 8
HET MSE A 67 8
HET MSE A 97 8
HET MSE A 213 8
HET MSE A 217 8
HET MSE A 255 8
HET MSE A 295 8
HET MSE D 49 8
HET MSE D 56 8
HET MSE D 67 8
HET MSE D 97 8
HET MSE D 213 8
HET MSE D 217 8
HET MSE D 255 8
HET MSE D 295 8
HET MG A 401 1
HET ATP A 402 31
HET ATP B 501 31
HET MES B 502 12
HET GOL B 503 6
HET GOL B 504 6
HET MG B 505 1
HET PO4 B 506 5
HET SAH C 501 26
HET MG C 502 1
HET PO4 C 503 5
HET MG D 401 1
HET ATP D 402 31
HET ATP E 501 31
HET MG E 502 1
HET PO4 E 503 5
HET SAH F 501 26
HET MG F 502 1
HET PO4 F 503 5
HET PO4 F 504 5
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 7 MG 6(MG 2+)
FORMUL 8 ATP 4(C10 H16 N5 O13 P3)
FORMUL 10 MES C6 H13 N O4 S
FORMUL 11 GOL 2(C3 H8 O3)
FORMUL 14 PO4 5(O4 P 3-)
FORMUL 15 SAH 2(C14 H20 N6 O5 S)
FORMUL 27 HOH *92(H2 O)
HELIX 1 AA1 GLY A 23 GLU A 35 1 13
HELIX 2 AA2 ASN A 42 ARG A 47 1 6
HELIX 3 AA3 SER A 57 ASN A 78 1 22
HELIX 4 AA4 LEU A 91 THR A 102 1 12
HELIX 5 AA5 PRO A 115 VAL A 120 1 6
HELIX 6 AA6 ASN A 208 GLN A 221 1 14
HELIX 7 AA7 TYR A 235 TYR A 246 1 12
HELIX 8 AA8 LYS A 263 GLU A 275 1 13
HELIX 9 AA9 ARG A 289 GLU A 299 1 11
HELIX 10 AB1 ASP B 3 ASN B 17 1 15
HELIX 11 AB2 SER B 40 LEU B 50 1 11
HELIX 12 AB3 ARG B 74 THR B 78 5 5
HELIX 13 AB4 ASP B 92 LEU B 100 1 9
HELIX 14 AB5 LEU B 100 ASP B 105 1 6
HELIX 15 AB6 TRP B 124 LYS B 129 1 6
HELIX 16 AB7 GLY B 130 GLU B 135 1 6
HELIX 17 AB8 GLU B 135 SER B 153 1 19
HELIX 18 AB9 SER B 154 GLN B 163 1 10
HELIX 19 AC1 PRO B 166 VAL B 177 1 12
HELIX 20 AC2 MET B 189 ILE B 198 1 10
HELIX 21 AC3 ASP B 205 GLY B 224 1 20
HELIX 22 AC4 LYS B 277 SER B 291 1 15
HELIX 23 AC5 ASN B 316 THR B 321 1 6
HELIX 24 AC6 GLY B 325 ASP B 330 5 6
HELIX 25 AC7 ARG B 331 LYS B 338 1 8
HELIX 26 AC8 GLY B 343 ALA B 360 1 18
HELIX 27 AC9 PRO B 362 LEU B 366 5 5
HELIX 28 AD1 ASN B 370 ASN B 388 1 19
HELIX 29 AD2 HIS C 11 LEU C 16 1 6
HELIX 30 AD3 HIS C 21 LEU C 24 5 4
HELIX 31 AD4 PHE C 67 CYS C 71 5 5
HELIX 32 AD5 SER C 72 PHE C 84 1 13
HELIX 33 AD6 LYS C 85 GLN C 89 5 5
HELIX 34 AD7 GLU C 90 SER C 96 1 7
HELIX 35 AD8 THR C 105 ASP C 110 1 6
HELIX 36 AD9 MET C 135 TYR C 138 5 4
HELIX 37 AE1 SER C 160 THR C 178 1 19
HELIX 38 AE2 ARG C 197 ASN C 201 5 5
HELIX 39 AE3 PRO C 206 ILE C 218 1 13
HELIX 40 AE4 SER C 220 GLU C 238 1 19
HELIX 41 AE5 GLY C 251 GLY C 262 1 12
HELIX 42 AE6 GLU C 274 ARG C 280 1 7
HELIX 43 AE7 PHE C 281 TYR C 286 5 6
HELIX 44 AE8 ASP C 298 LEU C 308 1 11
HELIX 45 AE9 GLU C 346 LEU C 358 1 13
HELIX 46 AF1 PHE C 372 TYR C 376 5 5
HELIX 47 AF2 THR C 394 GLY C 407 1 14
HELIX 48 AF3 GLY D 23 GLU D 35 1 13
HELIX 49 AF4 ASN D 42 LEU D 48 1 7
HELIX 50 AF5 MSE D 49 PHE D 51 5 3
HELIX 51 AF6 SER D 57 ASN D 78 1 22
HELIX 52 AF7 SER D 93 THR D 102 1 10
HELIX 53 AF8 PRO D 115 VAL D 120 1 6
HELIX 54 AF9 ASN D 198 ALA D 202 5 5
HELIX 55 AG1 ASN D 208 GLN D 220 1 13
HELIX 56 AG2 TYR D 235 TYR D 246 1 12
HELIX 57 AG3 LYS D 263 ILE D 276 1 14
HELIX 58 AG4 ARG D 289 GLU D 299 1 11
HELIX 59 AG5 ASP E 3 ASN E 17 1 15
HELIX 60 AG6 SER E 40 LEU E 50 1 11
HELIX 61 AG7 ARG E 74 THR E 78 5 5
HELIX 62 AG8 ASP E 92 ASP E 105 1 14
HELIX 63 AG9 TRP E 124 LYS E 129 1 6
HELIX 64 AH1 GLY E 130 GLU E 135 1 6
HELIX 65 AH2 GLU E 135 SER E 153 1 19
HELIX 66 AH3 SER E 154 GLN E 163 1 10
HELIX 67 AH4 PRO E 166 ASP E 174 1 9
HELIX 68 AH5 HIS E 190 ILE E 198 1 9
HELIX 69 AH6 ASP E 205 GLY E 224 1 20
HELIX 70 AH7 ASP E 251 GLN E 257 5 7
HELIX 71 AH8 LYS E 277 SER E 291 1 15
HELIX 72 AH9 ASN E 316 TYR E 324 1 9
HELIX 73 AI1 ARG E 331 ARG E 339 1 9
HELIX 74 AI2 GLY E 343 ALA E 360 1 18
HELIX 75 AI3 PRO E 362 LEU E 366 5 5
HELIX 76 AI4 ASN E 370 ASN E 388 1 19
HELIX 77 AI5 HIS F 11 LEU F 16 1 6
HELIX 78 AI6 HIS F 21 LEU F 24 5 4
HELIX 79 AI7 PHE F 67 CYS F 71 5 5
HELIX 80 AI8 SER F 72 ASN F 81 1 10
HELIX 81 AI9 PHE F 84 GLN F 89 5 6
HELIX 82 AJ1 GLU F 90 TRP F 95 1 6
HELIX 83 AJ2 THR F 105 ASP F 110 1 6
HELIX 84 AJ3 SER F 125 SER F 129 5 5
HELIX 85 AJ4 SER F 160 THR F 178 1 19
HELIX 86 AJ5 TYR F 195 THR F 200 5 6
HELIX 87 AJ6 PRO F 206 ILE F 218 1 13
HELIX 88 AJ7 SER F 220 GLU F 237 1 18
HELIX 89 AJ8 GLY F 251 GLY F 262 1 12
HELIX 90 AJ9 GLU F 274 ARG F 279 1 6
HELIX 91 AK1 ARG F 280 ASN F 285 5 6
HELIX 92 AK2 ASP F 298 LYS F 309 1 12
HELIX 93 AK3 ASP F 322 TYR F 326 5 5
HELIX 94 AK4 ALA F 347 LEU F 358 1 12
HELIX 95 AK5 PHE F 372 TYR F 376 5 5
HELIX 96 AK6 GLN F 396 GLY F 407 1 12
SHEET 1 AA1 4 TRP A 38 VAL A 41 0
SHEET 2 AA1 4 ASN A 81 ILE A 84 1 O ILE A 83 N VAL A 39
SHEET 3 AA1 4 LYS A 12 GLY A 18 1 N LEU A 14 O ILE A 84
SHEET 4 AA1 4 ASP A 106 PHE A 112 1 O SER A 108 N ILE A 15
SHEET 1 AA210 LEU A 252 ARG A 256 0
SHEET 2 AA210 LYS A 224 GLU A 232 1 N LEU A 227 O LEU A 254
SHEET 3 AA210 LYS A 178 CYS A 182 1 N VAL A 180 O LYS A 224
SHEET 4 AA210 PHE A 281 ASP A 287 1 O GLU A 283 N ALA A 179
SHEET 5 AA210 CYS A 304 GLN A 306 1 O PHE A 305 N LEU A 285
SHEET 6 AA210 CYS D 304 VAL D 307 -1 O GLN D 306 N GLN A 306
SHEET 7 AA210 PHE D 281 ASP D 287 1 N ASP D 287 O PHE D 305
SHEET 8 AA210 LYS D 178 CYS D 182 1 N ILE D 181 O LEU D 286
SHEET 9 AA210 LYS D 224 GLU D 232 1 O ILE D 226 N VAL D 180
SHEET 10 AA210 LEU D 252 ARG D 256 1 O LEU D 254 N SER D 229
SHEET 1 AA3 2 SER A 189 LEU A 190 0
SHEET 2 AA3 2 LEU A 206 LEU A 207 -1 O LEU A 206 N LEU A 190
SHEET 1 AA4 5 SER B 27 PRO B 28 0
SHEET 2 AA4 5 PHE B 312 ARG B 315 1 O LYS B 313 N SER B 27
SHEET 3 AA4 5 GLY B 295 PRO B 300 -1 N ILE B 298 O PHE B 312
SHEET 4 AA4 5 ILE B 56 LYS B 61 -1 N VAL B 57 O LYS B 299
SHEET 5 AA4 5 TYR B 266 GLN B 267 -1 O GLN B 267 N ILE B 56
SHEET 1 AA5 5 TYR B 79 VAL B 81 0
SHEET 2 AA5 5 SER B 65 HIS B 72 -1 N TYR B 70 O TYR B 79
SHEET 3 AA5 5 VAL B 112 MET B 122 -1 O ARG B 115 N LEU B 71
SHEET 4 AA5 5 PHE B 230 TYR B 241 -1 O LYS B 232 N GLU B 120
SHEET 5 AA5 5 GLU B 246 PHE B 248 -1 O HIS B 247 N GLU B 239
SHEET 1 AA6 7 ILE C 26 LYS C 29 0
SHEET 2 AA6 7 LEU C 36 ASN C 39 -1 O GLY C 38 N TYR C 27
SHEET 3 AA6 7 GLN C 45 PHE C 50 -1 O ASP C 47 N ASN C 39
SHEET 4 AA6 7 ILE C 2 SER C 7 -1 N ILE C 5 O TYR C 46
SHEET 5 AA6 7 CYS C 114 TYR C 122 -1 O THR C 115 N HIS C 6
SHEET 6 AA6 7 ASN C 151 GLY C 158 -1 O VAL C 156 N ILE C 116
SHEET 7 AA6 7 ILE C 142 VAL C 148 -1 N VAL C 148 O ASN C 151
SHEET 1 AA7 2 TYR C 128 SER C 129 0
SHEET 2 AA7 2 HIS C 132 PHE C 133 -1 O HIS C 132 N SER C 129
SHEET 1 AA8 7 LEU C 317 PHE C 320 0
SHEET 2 AA8 7 TYR C 292 THR C 295 1 N TYR C 292 O TYR C 318
SHEET 3 AA8 7 ILE C 267 ASP C 269 1 N ASP C 269 O PHE C 293
SHEET 4 AA8 7 VAL C 332 LEU C 336 1 O ASN C 333 N LEU C 268
SHEET 5 AA8 7 PHE C 360 PRO C 368 1 O LYS C 362 N ILE C 334
SHEET 6 AA8 7 THR C 428 ARG C 435 -1 O GLN C 429 N THR C 367
SHEET 7 AA8 7 LEU C 411 ILE C 418 -1 N GLU C 412 O THR C 434
SHEET 1 AA9 4 TRP D 38 VAL D 41 0
SHEET 2 AA9 4 ASN D 81 ILE D 84 1 O ILE D 83 N VAL D 39
SHEET 3 AA9 4 LYS D 12 ILE D 15 1 N LEU D 14 O ILE D 84
SHEET 4 AA9 4 ASP D 106 PHE D 109 1 O SER D 108 N LEU D 13
SHEET 1 AB1 2 SER D 189 LEU D 190 0
SHEET 2 AB1 2 LEU D 206 LEU D 207 -1 O LEU D 206 N LEU D 190
SHEET 1 AB2 5 SER E 27 PRO E 28 0
SHEET 2 AB2 5 PHE E 312 ARG E 315 1 O LYS E 313 N SER E 27
SHEET 3 AB2 5 GLY E 295 PRO E 300 -1 N VAL E 296 O VAL E 314
SHEET 4 AB2 5 ILE E 56 LYS E 61 -1 N GLU E 59 O VAL E 297
SHEET 5 AB2 5 HIS E 265 GLN E 267 -1 O HIS E 265 N ILE E 58
SHEET 1 AB3 5 TYR E 79 VAL E 81 0
SHEET 2 AB3 5 SER E 65 HIS E 72 -1 N TYR E 70 O TYR E 79
SHEET 3 AB3 5 VAL E 112 MET E 122 -1 O ILE E 117 N ILE E 69
SHEET 4 AB3 5 PHE E 230 TYR E 241 -1 O VAL E 240 N LEU E 114
SHEET 5 AB3 5 GLU E 246 PHE E 248 -1 O HIS E 247 N GLU E 239
SHEET 1 AB4 7 ILE F 26 SER F 30 0
SHEET 2 AB4 7 GLN F 35 SER F 42 -1 O LEU F 36 N LYS F 29
SHEET 3 AB4 7 GLN F 45 PHE F 50 -1 O VAL F 49 N ILE F 37
SHEET 4 AB4 7 ILE F 2 SER F 7 -1 N ILE F 5 O TYR F 46
SHEET 5 AB4 7 CYS F 114 VAL F 118 -1 O THR F 115 N HIS F 6
SHEET 6 AB4 7 ASN F 151 GLY F 158 -1 O GLY F 158 N CYS F 114
SHEET 7 AB4 7 THR F 145 VAL F 148 -1 N THR F 145 O SER F 153
SHEET 1 AB5 2 ILE F 242 ASP F 243 0
SHEET 2 AB5 2 ARG F 421 ILE F 422 -1 O ARG F 421 N ASP F 243
SHEET 1 AB6 7 LEU F 317 PHE F 320 0
SHEET 2 AB6 7 TYR F 292 THR F 295 1 N TYR F 292 O TYR F 318
SHEET 3 AB6 7 ILE F 267 ILE F 270 1 N ASP F 269 O PHE F 293
SHEET 4 AB6 7 VAL F 332 LEU F 336 1 O ILE F 335 N LEU F 268
SHEET 5 AB6 7 PHE F 360 PRO F 368 1 O LYS F 362 N ILE F 334
SHEET 6 AB6 7 THR F 428 ARG F 435 -1 O GLN F 429 N THR F 367
SHEET 7 AB6 7 LEU F 411 ILE F 418 -1 N THR F 414 O VAL F 432
LINK C LEU A 48 N MSE A 49 1555 1555 1.33
LINK C MSE A 49 N GLN A 50 1555 1555 1.33
LINK C LEU A 55 N MSE A 56 1555 1555 1.33
LINK C MSE A 56 N SER A 57 1555 1555 1.33
LINK C LYS A 66 N MSE A 67 1555 1555 1.34
LINK C MSE A 67 N VAL A 68 1555 1555 1.33
LINK C ASP A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N VAL A 98 1555 1555 1.33
LINK OD2 ASP A 183 MG MG A 401 1555 1555 2.32
LINK O ASP A 185 MG MG A 401 1555 1555 2.33
LINK C ALA A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N VAL A 214 1555 1555 1.33
LINK C LYS A 216 N MSE A 217 1555 1555 1.33
LINK C MSE A 217 N ALA A 218 1555 1555 1.33
LINK C LEU A 254 N MSE A 255 1555 1555 1.34
LINK C MSE A 255 N ARG A 256 1555 1555 1.33
LINK OD1 ASP A 288 MG MG A 401 1555 1555 2.75
LINK OD2 ASP A 288 MG MG A 401 1555 1555 2.20
LINK C ASP A 294 N MSE A 295 1555 1555 1.33
LINK C MSE A 295 N TRP A 296 1555 1555 1.33
LINK C LEU D 48 N MSE D 49 1555 1555 1.32
LINK C MSE D 49 N GLN D 50 1555 1555 1.33
LINK C LEU D 55 N MSE D 56 1555 1555 1.33
LINK C MSE D 56 N SER D 57 1555 1555 1.33
LINK C LYS D 66 N MSE D 67 1555 1555 1.33
LINK C MSE D 67 N VAL D 68 1555 1555 1.33
LINK C ASP D 96 N MSE D 97 1555 1555 1.33
LINK C MSE D 97 N VAL D 98 1555 1555 1.33
LINK OD2 ASP D 183 MG MG D 401 1555 1555 1.75
LINK O ASP D 185 MG MG D 401 1555 1555 2.30
LINK C ALA D 212 N MSE D 213 1555 1555 1.32
LINK C MSE D 213 N VAL D 214 1555 1555 1.33
LINK C LYS D 216 N MSE D 217 1555 1555 1.33
LINK C MSE D 217 N ALA D 218 1555 1555 1.33
LINK C LEU D 254 N MSE D 255 1555 1555 1.32
LINK C MSE D 255 N ARG D 256 1555 1555 1.33
LINK OD2 ASP D 288 MG MG D 401 1555 1555 2.46
LINK C ASP D 294 N MSE D 295 1555 1555 1.33
LINK C MSE D 295 N TRP D 296 1555 1555 1.33
LINK O2A ATP B 501 MG MG B 505 1555 1555 2.62
LINK MG MG B 505 O HOH B 606 1555 1555 2.27
LINK MG MG B 505 O HOH B 608 1555 1555 1.90
LINK MG MG D 401 O HOH D 507 1555 1555 2.97
LINK O2A ATP E 501 MG MG E 502 1555 1555 2.31
LINK MG MG E 502 O HOH E 607 1555 1555 2.72
CISPEP 1 MET B 122 PRO B 123 0 -10.93
CISPEP 2 GLU B 226 ALA B 227 0 -27.90
CISPEP 3 ASN C 33 GLY C 34 0 3.14
CISPEP 4 GLU C 310 ARG C 311 0 1.17
CISPEP 5 THR D 149 LYS D 150 0 -10.18
CISPEP 6 MET E 122 PRO E 123 0 -10.03
CISPEP 7 GLU E 182 LEU E 183 0 16.86
CISPEP 8 PRO E 188 MET E 189 0 -16.66
CISPEP 9 GLU E 226 ALA E 227 0 -14.62
CISPEP 10 PRO F 59 GLU F 60 0 -2.78
SITE 1 AC1 4 ASP A 183 ASP A 185 ASP A 288 HOH A 506
SITE 1 AC2 12 ALA A 19 PRO A 20 GLY A 21 SER A 22
SITE 2 AC2 12 GLY A 23 LYS A 24 SER A 25 THR A 26
SITE 3 AC2 12 THR A 87 ARG A 122 ASN B 370 GLU B 372
SITE 1 AC3 19 THR B 25 ILE B 26 GLU B 59 LYS B 60
SITE 2 AC3 19 LYS B 61 TYR B 62 TYR B 66 ARG B 83
SITE 3 AC3 19 GLU B 120 PHE B 234 GLU B 294 LYS B 299
SITE 4 AC3 19 LYS B 313 ARG B 315 LYS B 344 LEU B 394
SITE 5 AC3 19 MG B 505 HOH B 608 HOH B 620
SITE 1 AC4 4 SER B 32 VAL B 33 GLU B 34 GLU B 43
SITE 1 AC5 4 GLU B 39 ARG B 315 ASN B 317 HOH B 618
SITE 1 AC6 6 THR B 78 ILE B 88 ASN B 89 LEU B 91
SITE 2 AC6 6 GLN B 93 LEU B 97
SITE 1 AC7 5 GLY B 64 GLU B 120 ATP B 501 HOH B 606
SITE 2 AC7 5 HOH B 608
SITE 1 AC8 4 ASN B 250 ASP B 251 ARG B 301 THR B 302
SITE 1 AC9 9 ARG C 253 GLY C 271 ASP C 296 THR C 297
SITE 2 AC9 9 THR C 337 GLU C 338 HIS C 342 THR C 344
SITE 3 AC9 9 LEU C 351
SITE 1 AD1 2 GLN C 64 TYR C 122
SITE 1 AD2 5 ASN C 369 GLY C 417 GLY C 424 GLU C 425
SITE 2 AD2 5 THR C 426
SITE 1 AD3 4 ASP D 183 ASP D 185 ASP D 288 HOH D 507
SITE 1 AD4 8 PRO D 20 GLY D 21 GLY D 23 LYS D 24
SITE 2 AD4 8 SER D 25 THR D 26 ASN E 370 GLU E 372
SITE 1 AD5 15 THR E 25 ILE E 26 LYS E 60 LYS E 61
SITE 2 AD5 15 TYR E 62 TYR E 66 ARG E 83 GLU E 120
SITE 3 AD5 15 PHE E 234 GLU E 294 LYS E 313 ARG E 315
SITE 4 AD5 15 LEU E 394 MG E 502 HOH E 613
SITE 1 AD6 5 TYR E 62 GLU E 120 GLU E 294 ATP E 501
SITE 2 AD6 5 HOH E 607
SITE 1 AD7 3 ASP E 110 TYR E 241 ARG E 245
SITE 1 AD8 10 HIS F 250 GLY F 271 GLY F 273 ASP F 296
SITE 2 AD8 10 THR F 297 THR F 337 VAL F 339 ASN F 343
SITE 3 AD8 10 THR F 344 LEU F 351
SITE 1 AD9 3 GLN F 64 TYR F 122 TYR F 181
SITE 1 AE1 4 TYR F 57 HIS F 176 TYR F 181 TYR F 184
SITE 1 AE2 5 ASN F 369 PRO F 395 GLY F 424 GLU F 425
SITE 2 AE2 5 THR F 426
CRYST1 108.483 187.245 111.999 90.00 106.04 90.00 P 1 21 1 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 0.009218 0.000000 0.002650 0.00000
SCALE2 0.000000 0.005341 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009290 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
