HEADER PROTEIN BINDING 21-JAN-15 4XRP
TITLE STRUCTURE OF THE PNKP1/RNL/HEN1 RNA REPAIR 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 R.H.HUANG,P.WANG
REVDAT 3 28-FEB-24 4XRP 1 SOURCE REMARK
REVDAT 2 29-APR-15 4XRP 1 JRNL
REVDAT 1 22-APR-15 4XRP 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. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1624)
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) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 65439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
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 : 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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.67
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: ( CHAIN A AND ( RESID 2:312 OR RESID 401:404 OR
REMARK 3 RESID 501:507 ) ) OR ( CHAIN C AND ( RESID 1:435 OR
REMARK 3 RESID 501:504 OR RESID 601:622 ) ) OR ( CHAIN B AND
REMARK 3 ( RESID 1:394 OR RESID 401:404 OR RESID 501:518 ) )
REMARK 3 OR ( CHAIN E AND ( RESID 2:394 OR RESID 401:402 OR
REMARK 3 RESID 501:517 ) ) OR ( CHAIN D AND ( RESID 2:312 OR
REMARK 3 RESID 401:402 OR RESID 501:509 ) ) OR ( CHAIN F AND
REMARK 3 ( RESID 1:435 OR RESID 501:503 OR RESID 601:620 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.2875 5.5196 142.3371
REMARK 3 T TENSOR
REMARK 3 T11: 0.4694 T22: 0.2737
REMARK 3 T33: 0.4333 T12: -0.0628
REMARK 3 T13: -0.0428 T23: 0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 0.9007 L22: 0.2059
REMARK 3 L33: 0.0616 L12: -0.2234
REMARK 3 L13: -0.0187 L23: -0.0290
REMARK 3 S TENSOR
REMARK 3 S11: 0.1172 S12: -0.0152 S13: -0.1360
REMARK 3 S21: -0.0318 S22: -0.0990 S23: 0.0076
REMARK 3 S31: -0.0033 S32: 0.0113 S33: -0.0209
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 2864
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN E
REMARK 3 ATOM PAIRS NUMBER : 3650
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN F
REMARK 3 ATOM PAIRS NUMBER : 3878
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XRP 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_1000206215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-14
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) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
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 : 65439
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, PH 6.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 278K
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 89.60050
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: 22400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 100540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -226.0 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 MET A 1
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 LYS C 436
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 PHE F 377
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 465 LYS F 436
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 ARG A 126 N GLU A 128 1.96
REMARK 500 ND2 ASN D 5 OH TYR F 318 2.05
REMARK 500 O LYS E 225 O HOH E 516 2.07
REMARK 500 NH1 ARG F 216 O2 GOL F 503 2.08
REMARK 500 OH TYR B 324 NH1 ARG B 339 2.09
REMARK 500 OE2 GLU B 2 O HOH B 503 2.12
REMARK 500 OD2 ASP A 203 NH2 ARG A 241 2.12
REMARK 500 NZ LYS A 269 OE1 GLU A 299 2.13
REMARK 500 NE2 GLN A 221 OE1 GLN D 220 2.15
REMARK 500 NE2 GLN E 93 O HOH E 514 2.18
REMARK 500 OE2 GLU E 43 O HOH E 509 2.18
REMARK 500 OG1 THR D 130 NZ LYS D 132 2.18
REMARK 500 O ALA D 19 OG SER D 22 2.19
REMARK 500 OG1 THR B 25 OE2 GLU B 387 2.19
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 GLN A 129 CG GLN A 129 CD 0.150
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 ARG A 126 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 CYS A 127 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 GLN A 129 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 PRO A 238 C - N - CA ANGL. DEV. = -11.5 DEGREES
REMARK 500 LEU B 183 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LYS B 299 CD - CE - NZ ANGL. DEV. = 15.1 DEGREES
REMARK 500 LEU C 308 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LYS C 309 CD - CE - NZ ANGL. DEV. = 17.8 DEGREES
REMARK 500 LEU D 114 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 PRO D 115 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG D 126 CG - CD - NE ANGL. DEV. = 15.1 DEGREES
REMARK 500 LEU D 162 CA - CB - CG ANGL. DEV. = 15.7 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 THR A 7 139.86 -39.81
REMARK 500 ASN A 37 59.42 -104.99
REMARK 500 LEU A 55 111.44 14.07
REMARK 500 SER A 57 143.69 -35.13
REMARK 500 PHE A 59 -74.78 -57.64
REMARK 500 ASN A 88 -144.35 -163.67
REMARK 500 SER A 89 -22.53 -141.39
REMARK 500 SER A 90 105.64 -45.96
REMARK 500 LEU A 91 -48.31 -27.66
REMARK 500 ASP A 124 62.35 -101.38
REMARK 500 LYS A 125 -26.84 -169.84
REMARK 500 ARG A 126 -88.82 -75.27
REMARK 500 CYS A 127 29.66 -40.91
REMARK 500 THR A 130 -166.08 -112.91
REMARK 500 LYS A 132 159.95 -36.10
REMARK 500 SER A 137 -68.44 -91.65
REMARK 500 LYS A 152 54.95 -117.84
REMARK 500 PHE A 153 126.13 175.95
REMARK 500 LEU A 184 -76.41 -99.58
REMARK 500 ASP A 185 104.23 -55.64
REMARK 500 THR A 187 -65.98 -130.58
REMARK 500 ASN A 198 68.75 -103.15
REMARK 500 ALA A 199 30.36 -76.90
REMARK 500 ASN A 208 90.33 -66.56
REMARK 500 GLN A 221 -176.96 177.97
REMARK 500 TYR A 235 40.40 -87.13
REMARK 500 LEU A 252 117.72 -164.39
REMARK 500 TYR A 261 -2.30 79.03
REMARK 500 ILE A 276 -50.02 -124.46
REMARK 500 ASP A 288 -40.94 -132.53
REMARK 500 GLU B 2 -6.48 -140.53
REMARK 500 PHE B 22 113.95 -170.91
REMARK 500 HIS B 90 -162.36 -65.71
REMARK 500 LEU B 91 145.81 72.43
REMARK 500 LEU B 114 132.45 -176.12
REMARK 500 LEU B 127 -92.32 -93.74
REMARK 500 GLU B 148 2.01 -69.76
REMARK 500 SER B 179 38.84 -94.55
REMARK 500 ALA B 180 -56.72 59.03
REMARK 500 GLU B 226 124.53 -33.49
REMARK 500 PRO B 229 150.10 -48.66
REMARK 500 PHE B 230 117.33 -166.86
REMARK 500 LYS B 238 136.90 -176.06
REMARK 500 ALA B 269 -61.00 63.19
REMARK 500 GLU B 368 2.41 -69.67
REMARK 500 ARG B 393 36.95 -92.56
REMARK 500 ASP C 23 59.45 30.88
REMARK 500 ARG C 32 -129.06 53.42
REMARK 500 GLN C 64 130.65 -38.75
REMARK 500 CYS C 71 -1.36 -159.04
REMARK 500
REMARK 500 THIS ENTRY HAS 137 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 GLN C 64 ILE C 65 149.02
REMARK 500 LEU C 308 LYS C 309 30.77
REMARK 500 GLU D 118 LEU D 119 147.49
REMARK 500 MET F 312 GLU F 313 135.84
REMARK 500 GLU F 313 ALA F 314 141.50
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 183 OD2
REMARK 620 2 ASP A 185 O 73.4
REMARK 620 3 ASP A 288 OD2 69.9 80.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 183 OD2
REMARK 620 2 ASP D 185 O 76.6
REMARK 620 3 ASP D 288 OD1 83.4 73.3
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 PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XRU RELATED DB: PDB
DBREF 4XRP A 1 312 UNP C2M8N3 C2M8N3_CAPGI 1 312
DBREF 4XRP B 1 394 UNP C2M8N4 C2M8N4_CAPGI 1 394
DBREF 4XRP C 1 436 UNP C2M7I7 C2M7I7_CAPGI 1 436
DBREF 4XRP D 1 312 UNP C2M8N3 C2M8N3_CAPGI 1 312
DBREF 4XRP E 1 394 UNP C2M8N4 C2M8N4_CAPGI 1 394
DBREF 4XRP F 1 436 UNP C2M7I7 C2M7I7_CAPGI 1 436
SEQRES 1 A 312 MET 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 MET GLN PHE GLY
SEQRES 5 A 312 ASP SER LEU MET SER PRO PHE TYR GLU GLU ARG ILE THR
SEQRES 6 A 312 LYS MET 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 MET 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 MET VAL LEU LYS MET 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 MET 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 MET 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 ALA 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 GLN 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 MET 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 MET GLN PHE GLY
SEQRES 5 D 312 ASP SER LEU MET SER PRO PHE TYR GLU GLU ARG ILE THR
SEQRES 6 D 312 LYS MET 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 MET 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 MET VAL LEU LYS MET 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 MET 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 MET 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 ALA 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 GLN 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
HET PO4 A 401 5
HET MG A 402 1
HET SO4 A 403 5
HET SO4 A 404 5
HET MG B 401 1
HET MG B 402 1
HET SO4 B 403 5
HET GOL B 404 6
HET SO4 C 501 5
HET GOL C 502 6
HET GOL C 503 6
HET GOL C 504 6
HET PO4 D 401 5
HET MG D 402 1
HET SO4 E 401 5
HET SO4 E 402 5
HET SO4 F 501 5
HET SO4 F 502 5
HET GOL F 503 6
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 PO4 2(O4 P 3-)
FORMUL 8 MG 4(MG 2+)
FORMUL 9 SO4 8(O4 S 2-)
FORMUL 14 GOL 5(C3 H8 O3)
FORMUL 26 HOH *93(H2 O)
HELIX 1 AA1 GLY A 23 GLU A 35 1 13
HELIX 2 AA2 ASN A 42 GLN A 50 1 9
HELIX 3 AA3 SER A 57 ASN A 78 1 22
HELIX 4 AA4 SER A 90 GLU A 103 1 14
HELIX 5 AA5 PRO A 115 LYS A 121 1 7
HELIX 6 AA6 SER A 137 LYS A 150 1 14
HELIX 7 AA7 ASN A 198 ASP A 205 5 8
HELIX 8 AA8 ASN A 208 LYS A 219 1 12
HELIX 9 AA9 TYR A 235 TYR A 246 1 12
HELIX 10 AB1 LYS A 263 ILE A 276 1 14
HELIX 11 AB2 ARG A 289 GLU A 299 1 11
HELIX 12 AB3 ASP B 3 ASN B 17 1 15
HELIX 13 AB4 SER B 40 ASN B 51 1 12
HELIX 14 AB5 ARG B 74 THR B 78 5 5
HELIX 15 AB6 ASP B 92 LEU B 100 1 9
HELIX 16 AB7 LEU B 100 ASP B 105 1 6
HELIX 17 AB8 ASN B 133 VAL B 151 1 19
HELIX 18 AB9 SER B 153 GLN B 163 1 11
HELIX 19 AC1 GLU B 165 ALA B 175 1 11
HELIX 20 AC2 ALA B 180 TYR B 187 1 8
HELIX 21 AC3 PRO B 188 PHE B 201 1 14
HELIX 22 AC4 ASP B 205 GLY B 224 1 20
HELIX 23 AC5 ASP B 251 LEU B 253 5 3
HELIX 24 AC6 SER B 254 ASN B 259 1 6
HELIX 25 AC7 ASP B 270 ASP B 286 1 17
HELIX 26 AC8 ASN B 316 GLY B 325 1 10
HELIX 27 AC9 PHE B 328 ASP B 330 5 3
HELIX 28 AD1 ARG B 331 ARG B 339 1 9
HELIX 29 AD2 GLY B 343 ILE B 361 1 19
HELIX 30 AD3 PRO B 362 LEU B 366 5 5
HELIX 31 AD4 ASN B 370 ASN B 388 1 19
HELIX 32 AD5 HIS C 11 LEU C 16 1 6
HELIX 33 AD6 HIS C 21 LEU C 24 5 4
HELIX 34 AD7 PHE C 67 CYS C 71 5 5
HELIX 35 AD8 SER C 72 PHE C 84 1 13
HELIX 36 AD9 LYS C 85 GLN C 89 5 5
HELIX 37 AE1 GLU C 90 SER C 96 1 7
HELIX 38 AE2 THR C 105 ASP C 110 1 6
HELIX 39 AE3 PHE C 133 PHE C 139 1 7
HELIX 40 AE4 SER C 160 ASN C 179 1 20
HELIX 41 AE5 HIS C 190 ALA C 196 1 7
HELIX 42 AE6 ARG C 197 ASN C 201 5 5
HELIX 43 AE7 PRO C 206 ILE C 218 1 13
HELIX 44 AE8 SER C 220 GLU C 237 1 18
HELIX 45 AE9 ASP C 248 GLY C 262 1 15
HELIX 46 AF1 LEU C 275 MET C 282 1 8
HELIX 47 AF2 ARG C 283 ASN C 287 5 5
HELIX 48 AF3 SER C 300 ALA C 306 1 7
HELIX 49 AF4 ASP C 322 TYR C 326 5 5
HELIX 50 AF5 THR C 344 LEU C 358 1 15
HELIX 51 AF6 SER C 370 TYR C 376 5 7
HELIX 52 AF7 THR C 394 GLY C 407 1 14
HELIX 53 AF8 GLY D 23 GLU D 35 1 13
HELIX 54 AF9 ASN D 42 GLN D 50 1 9
HELIX 55 AG1 SER D 57 ASN D 78 1 22
HELIX 56 AG2 LEU D 91 THR D 102 1 12
HELIX 57 AG3 LEU D 119 ASP D 124 1 6
HELIX 58 AG4 SER D 137 LYS D 150 1 14
HELIX 59 AG5 ASN D 198 ASP D 205 5 8
HELIX 60 AG6 ASN D 208 LYS D 219 1 12
HELIX 61 AG7 TYR D 235 TYR D 246 1 12
HELIX 62 AG8 LYS D 263 ILE D 276 1 14
HELIX 63 AG9 ARG D 289 GLU D 299 1 11
HELIX 64 AH1 ASP E 3 ASN E 17 1 15
HELIX 65 AH2 SER E 40 LEU E 50 1 11
HELIX 66 AH3 ARG E 74 THR E 78 5 5
HELIX 67 AH4 ASP E 92 ASP E 105 1 14
HELIX 68 AH5 ASN E 133 VAL E 151 1 19
HELIX 69 AH6 SER E 154 GLN E 163 1 10
HELIX 70 AH7 GLU E 165 LEU E 178 1 14
HELIX 71 AH8 SER E 179 TYR E 187 1 9
HELIX 72 AH9 PRO E 188 PHE E 201 1 14
HELIX 73 AI1 ASP E 205 GLY E 224 1 20
HELIX 74 AI2 ASP E 251 GLN E 256 5 6
HELIX 75 AI3 ASP E 270 ASP E 286 1 17
HELIX 76 AI4 ASN E 316 GLY E 325 1 10
HELIX 77 AI5 PHE E 328 ASP E 330 5 3
HELIX 78 AI6 ARG E 331 ARG E 339 1 9
HELIX 79 AI7 ILE E 341 ILE E 361 1 21
HELIX 80 AI8 PRO E 362 LEU E 366 5 5
HELIX 81 AI9 GLU E 372 ASN E 388 1 17
HELIX 82 AJ1 HIS F 11 LEU F 16 1 6
HELIX 83 AJ2 HIS F 21 LEU F 24 5 4
HELIX 84 AJ3 PHE F 67 CYS F 71 5 5
HELIX 85 AJ4 SER F 72 PHE F 84 1 13
HELIX 86 AJ5 LYS F 85 GLN F 89 5 5
HELIX 87 AJ6 GLU F 90 SER F 96 1 7
HELIX 88 AJ7 THR F 105 ASP F 110 1 6
HELIX 89 AJ8 PHE F 133 TYR F 138 5 6
HELIX 90 AJ9 SER F 160 ASN F 179 1 20
HELIX 91 AK1 HIS F 190 ALA F 196 1 7
HELIX 92 AK2 ARG F 197 ASN F 201 5 5
HELIX 93 AK3 PRO F 206 ILE F 218 1 13
HELIX 94 AK4 SER F 220 GLU F 237 1 18
HELIX 95 AK5 ASP F 248 GLY F 262 1 15
HELIX 96 AK6 LEU F 275 MET F 282 1 8
HELIX 97 AK7 ARG F 283 ASN F 287 5 5
HELIX 98 AK8 ASP F 298 LEU F 307 1 10
HELIX 99 AK9 ASP F 322 TYR F 326 5 5
HELIX 100 AL1 THR F 344 LEU F 356 1 13
HELIX 101 AL2 SER F 370 ASN F 373 5 4
HELIX 102 AL3 THR F 394 GLY F 407 1 14
SHEET 1 AA1 4 TRP A 38 VAL A 41 0
SHEET 2 AA1 4 ASN A 81 ASP A 85 1 O ASN A 81 N VAL A 39
SHEET 3 AA1 4 LYS A 12 GLY A 18 1 N LEU A 16 O ILE A 84
SHEET 4 AA1 4 ASP A 106 PHE A 112 1 O PHE A 112 N VAL A 17
SHEET 1 AA2 5 LEU A 252 ARG A 256 0
SHEET 2 AA2 5 LYS A 224 GLU A 232 1 N LEU A 227 O LEU A 254
SHEET 3 AA2 5 LYS A 178 CYS A 182 1 N VAL A 180 O ILE A 226
SHEET 4 AA2 5 PHE A 281 ASP A 287 1 O LEU A 286 N ILE A 181
SHEET 5 AA2 5 CYS A 304 GLN A 306 1 O PHE A 305 N LEU A 285
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 GLU B 293 PRO B 300 -1 N VAL B 296 O VAL B 314
SHEET 4 AA4 5 GLU B 55 TYR B 62 -1 N VAL B 57 O LYS B 299
SHEET 5 AA4 5 LEU B 264 GLN B 267 -1 O TYR B 266 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 ASP B 68 O VAL B 81
SHEET 3 AA5 5 VAL B 112 MET B 122 -1 O LEU B 121 N SER B 65
SHEET 4 AA5 5 PHE B 230 TYR B 241 -1 O VAL B 240 N LEU B 114
SHEET 5 AA5 5 GLU B 246 HIS B 247 -1 O HIS B 247 N GLU B 239
SHEET 1 AA6 7 ILE C 26 LYS C 29 0
SHEET 2 AA6 7 GLN C 35 ASN C 39 -1 O GLY C 38 N TYR C 27
SHEET 3 AA6 7 GLN C 45 GLN C 51 -1 O VAL C 49 N ILE C 37
SHEET 4 AA6 7 ILE C 2 HIS C 6 -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 THR C 145 VAL C 148 -1 N ILE C 147 O ASN C 151
SHEET 1 AA7 2 ILE C 242 ASP C 243 0
SHEET 2 AA7 2 ARG C 421 ILE C 422 -1 O ARG C 421 N ASP C 243
SHEET 1 AA8 7 LEU C 317 PHE C 320 0
SHEET 2 AA8 7 TYR C 292 THR C 295 1 N ALA C 294 O PHE C 320
SHEET 3 AA8 7 ILE C 267 ILE C 270 1 N ASP C 269 O PHE C 293
SHEET 4 AA8 7 VAL C 332 THR C 337 1 O ILE C 335 N LEU C 268
SHEET 5 AA8 7 PHE C 360 PRO C 368 1 O HIS C 361 N VAL C 332
SHEET 6 AA8 7 THR C 428 THR C 434 -1 O GLN C 429 N THR C 367
SHEET 7 AA8 7 GLU C 412 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 ASP D 85 1 O ILE D 83 N VAL D 41
SHEET 3 AA9 4 LYS D 12 GLY D 18 1 N LEU D 14 O ILE D 84
SHEET 4 AA9 4 ASP D 106 PHE D 112 1 O PHE D 112 N VAL D 17
SHEET 1 AB1 5 LEU D 252 ARG D 256 0
SHEET 2 AB1 5 LYS D 224 GLU D 232 1 N LEU D 227 O LEU D 254
SHEET 3 AB1 5 LYS D 178 CYS D 182 1 N VAL D 180 O ILE D 226
SHEET 4 AB1 5 PHE D 281 ASP D 287 1 O PHE D 281 N ALA D 179
SHEET 5 AB1 5 CYS D 304 GLN D 306 1 O PHE D 305 N LEU D 285
SHEET 1 AB2 2 SER D 189 LEU D 190 0
SHEET 2 AB2 2 LEU D 206 LEU D 207 -1 O LEU D 206 N LEU D 190
SHEET 1 AB3 5 SER E 27 PRO E 28 0
SHEET 2 AB3 5 PHE E 312 ARG E 315 1 O LYS E 313 N SER E 27
SHEET 3 AB3 5 GLU E 293 PRO E 300 -1 N VAL E 296 O VAL E 314
SHEET 4 AB3 5 GLU E 55 TYR E 62 -1 N VAL E 57 O LYS E 299
SHEET 5 AB3 5 LEU E 264 GLN E 267 -1 O TYR E 266 N ILE E 56
SHEET 1 AB4 5 TYR E 79 VAL E 81 0
SHEET 2 AB4 5 SER E 65 HIS E 72 -1 N ASP E 68 O VAL E 81
SHEET 3 AB4 5 VAL E 112 MET E 122 -1 O LEU E 121 N SER E 65
SHEET 4 AB4 5 PHE E 230 TYR E 241 -1 O VAL E 240 N LEU E 114
SHEET 5 AB4 5 GLU E 246 HIS E 247 -1 O HIS E 247 N GLU E 239
SHEET 1 AB5 7 ILE F 26 LEU F 31 0
SHEET 2 AB5 7 GLY F 34 ALA F 40 -1 O GLY F 38 N TYR F 27
SHEET 3 AB5 7 GLN F 45 GLN F 51 -1 O ASP F 47 N ASN F 39
SHEET 4 AB5 7 ILE F 2 SER F 7 -1 N ILE F 5 O TYR F 46
SHEET 5 AB5 7 CYS F 114 TYR F 122 -1 O THR F 115 N HIS F 6
SHEET 6 AB5 7 ASN F 151 GLY F 158 -1 O VAL F 156 N ILE F 116
SHEET 7 AB5 7 THR F 145 VAL F 148 -1 N THR F 145 O SER F 153
SHEET 1 AB6 2 ILE F 242 ASP F 243 0
SHEET 2 AB6 2 ARG F 421 ILE F 422 -1 O ARG F 421 N ASP F 243
SHEET 1 AB7 7 LEU F 317 PHE F 319 0
SHEET 2 AB7 7 TYR F 292 THR F 295 1 N ALA F 294 O TYR F 318
SHEET 3 AB7 7 ILE F 267 ILE F 270 1 N ASP F 269 O PHE F 293
SHEET 4 AB7 7 VAL F 332 THR F 337 1 O ASN F 333 N LEU F 268
SHEET 5 AB7 7 PHE F 360 PRO F 368 1 O ILE F 364 N ILE F 334
SHEET 6 AB7 7 THR F 428 THR F 434 -1 O GLN F 429 N THR F 367
SHEET 7 AB7 7 GLU F 412 ILE F 418 -1 N THR F 414 O VAL F 432
LINK OD2 ASP A 183 MG MG A 402 1555 1555 2.50
LINK O ASP A 185 MG MG A 402 1555 1555 2.31
LINK OD2 ASP A 288 MG MG A 402 1555 1555 1.95
LINK OE2 GLU B 43 MG MG B 401 1555 1555 2.60
LINK OD2 ASP D 183 MG MG D 402 1555 1555 2.04
LINK O ASP D 185 MG MG D 402 1555 1555 2.43
LINK OD1 ASP D 288 MG MG D 402 1555 1555 2.18
CISPEP 1 MET B 122 PRO B 123 0 -7.27
CISPEP 2 ASN C 33 GLY C 34 0 3.99
CISPEP 3 ALA C 314 ASP C 315 0 -25.12
CISPEP 4 MET E 122 PRO E 123 0 -7.85
CISPEP 5 LYS F 100 TRP F 101 0 2.05
CISPEP 6 ALA F 314 ASP F 315 0 2.44
SITE 1 AC1 7 ALA A 19 GLY A 21 SER A 22 GLY A 23
SITE 2 AC1 7 LYS A 24 SER A 25 ARG A 126
SITE 1 AC2 3 ASP A 183 ASP A 185 ASP A 288
SITE 1 AC3 4 TYR A 169 ALA A 170 GLN A 172 PHE A 281
SITE 1 AC4 2 ASP A 249 TYR A 250
SITE 1 AC5 2 GLU B 43 SO4 B 403
SITE 1 AC6 3 LYS B 60 LYS B 61 GLU B 120
SITE 1 AC7 5 SER B 32 VAL B 33 GLU B 34 GLU B 43
SITE 2 AC7 5 MG B 401
SITE 1 AC8 6 SER B 23 PRO B 24 ILE B 26 TYR B 66
SITE 2 AC8 6 ARG B 83 GLU B 120
SITE 1 AC9 2 LEU C 31 HIS C 78
SITE 1 AD1 6 SER C 125 THR C 126 TRP C 127 THR C 178
SITE 2 AD1 6 ARG C 216 PHE C 377
SITE 1 AD2 6 SER C 125 TYR C 128 SER C 129 LYS C 130
SITE 2 AD2 6 GLY C 149 ASN C 150
SITE 1 AD3 4 VAL C 205 PRO C 206 TYR C 207 GLU C 238
SITE 1 AD4 5 GLY D 21 SER D 22 GLY D 23 LYS D 24
SITE 2 AD4 5 SER D 25
SITE 1 AD5 4 ASP D 183 ASP D 185 ASP D 287 ASP D 288
SITE 1 AD6 3 PHE E 234 LYS E 299 PRO E 310
SITE 1 AD7 5 LYS E 31 SER E 32 VAL E 33 GLU E 34
SITE 2 AD7 5 GLU E 43
SITE 1 AD8 3 ASN F 17 LYS F 100 TRP F 101
SITE 1 AD9 3 HIS F 78 GLU F 82 TYR F 195
SITE 1 AE1 5 SER F 125 THR F 126 TRP F 127 THR F 178
SITE 2 AE1 5 ARG F 216
CRYST1 111.160 179.201 114.333 90.00 103.70 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 0.008996 0.000000 0.002194 0.00000
SCALE2 0.000000 0.005580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009003 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
