HEADER OXIDOREDUCTASE 30-JUN-13 4LGZ
TITLE STRUCTURE OF MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE (ALDH4A1)
TITLE 2 COMPLEXED WITH ACETATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 21-563;
COMPND 6 SYNONYM: P5C DEHYDROGENASE, ALDEHYDE DEHYDROGENASE FAMILY 4 MEMBER
COMPND 7 A1;
COMPND 8 EC: 1.5.1.12;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ALDH4A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PROLINE CATABOLISM, SUBSTRATE RECOGNITION, ROSSMANN FOLD,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.PEMBERTON,J.J.TANNER
REVDAT 4 28-FEB-24 4LGZ 1 REMARK SEQADV
REVDAT 3 12-NOV-14 4LGZ 1 KEYWDS
REVDAT 2 09-OCT-13 4LGZ 1 JRNL
REVDAT 1 28-AUG-13 4LGZ 0
JRNL AUTH T.A.PEMBERTON,J.J.TANNER
JRNL TITL STRUCTURAL BASIS OF SUBSTRATE SELECTIVITY OF DELTA
JRNL TITL 2 (1)-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE (ALDH4A1):
JRNL TITL 3 SEMIALDEHYDE CHAIN LENGTH.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 538 34 2013
JRNL REFN ISSN 0003-9861
JRNL PMID 23928095
JRNL DOI 10.1016/J.ABB.2013.07.024
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 119722
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5992
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.6171 - 5.1737 1.00 4121 216 0.1757 0.1695
REMARK 3 2 5.1737 - 4.1190 1.00 3949 211 0.1379 0.1661
REMARK 3 3 4.1190 - 3.6020 1.00 3910 213 0.1580 0.1701
REMARK 3 4 3.6020 - 3.2743 1.00 3892 219 0.1736 0.1754
REMARK 3 5 3.2743 - 3.0405 1.00 3872 220 0.1911 0.2196
REMARK 3 6 3.0405 - 2.8618 1.00 3861 219 0.1755 0.1929
REMARK 3 7 2.8618 - 2.7189 1.00 3904 187 0.1790 0.2045
REMARK 3 8 2.7189 - 2.6008 1.00 3816 229 0.1674 0.1944
REMARK 3 9 2.6008 - 2.5009 1.00 3832 207 0.1621 0.1765
REMARK 3 10 2.5009 - 2.4148 1.00 3844 204 0.1635 0.2051
REMARK 3 11 2.4148 - 2.3394 1.00 3871 189 0.1588 0.2094
REMARK 3 12 2.3394 - 2.2726 1.00 3826 226 0.1591 0.1758
REMARK 3 13 2.2726 - 2.2129 1.00 3859 187 0.1561 0.1899
REMARK 3 14 2.2129 - 2.1590 1.00 3834 197 0.1584 0.2116
REMARK 3 15 2.1590 - 2.1099 1.00 3815 199 0.1605 0.2210
REMARK 3 16 2.1099 - 2.0651 1.00 3867 188 0.1610 0.2048
REMARK 3 17 2.0651 - 2.0238 1.00 3792 215 0.1583 0.1794
REMARK 3 18 2.0238 - 1.9857 1.00 3829 199 0.1553 0.1879
REMARK 3 19 1.9857 - 1.9502 1.00 3816 202 0.1572 0.1965
REMARK 3 20 1.9502 - 1.9172 1.00 3814 188 0.1592 0.1918
REMARK 3 21 1.9172 - 1.8863 1.00 3783 200 0.1592 0.1977
REMARK 3 22 1.8863 - 1.8573 0.99 3803 227 0.1739 0.2136
REMARK 3 23 1.8573 - 1.8300 0.99 3808 172 0.1790 0.2208
REMARK 3 24 1.8300 - 1.8042 0.99 3785 186 0.1920 0.2345
REMARK 3 25 1.8042 - 1.7799 0.99 3787 192 0.1935 0.2468
REMARK 3 26 1.7799 - 1.7568 0.99 3819 190 0.1940 0.2287
REMARK 3 27 1.7568 - 1.7348 0.99 3750 192 0.1928 0.2253
REMARK 3 28 1.7348 - 1.7139 0.99 3759 200 0.1963 0.2278
REMARK 3 29 1.7139 - 1.6940 0.90 3433 167 0.2115 0.2516
REMARK 3 30 1.6940 - 1.6750 0.71 2679 151 0.2420 0.2925
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 42.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.34500
REMARK 3 B22 (A**2) : 1.76140
REMARK 3 B33 (A**2) : -0.41630
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 8451
REMARK 3 ANGLE : 1.041 11510
REMARK 3 CHIRALITY : 0.071 1272
REMARK 3 PLANARITY : 0.005 1505
REMARK 3 DIHEDRAL : 11.636 3012
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5280 0.6564 3.2373
REMARK 3 T TENSOR
REMARK 3 T11: 0.0454 T22: 0.0450
REMARK 3 T33: 0.0534 T12: -0.0012
REMARK 3 T13: 0.0015 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3352 L22: 0.1301
REMARK 3 L33: 0.2321 L12: -0.0438
REMARK 3 L13: -0.0319 L23: 0.0496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.0116 S13: 0.0456
REMARK 3 S21: -0.0166 S22: 0.0122 S23: -0.0164
REMARK 3 S31: -0.0200 S32: 0.0254 S33: -0.0189
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4351 7.1193 18.2824
REMARK 3 T TENSOR
REMARK 3 T11: 0.0435 T22: 0.0435
REMARK 3 T33: 0.0414 T12: 0.0084
REMARK 3 T13: 0.0019 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.3950 L22: 0.1437
REMARK 3 L33: 0.0894 L12: -0.0882
REMARK 3 L13: 0.0142 L23: 0.0705
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0778 S13: 0.0394
REMARK 3 S21: 0.0068 S22: -0.0104 S23: -0.0050
REMARK 3 S31: -0.0234 S32: -0.0318 S33: 0.0131
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 4LGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 148
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC BLUE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119816
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.674
REMARK 200 RESOLUTION RANGE LOW (A) : 19.644
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.26300
REMARK 200 R SYM FOR SHELL (I) : 0.26300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 (%): 42.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-25% PEG 3350, 0.2 M LITHIUM
REMARK 280 SULFATE, 0.1 M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 42.46900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.07500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.07500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.46900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.94000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
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 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 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 LEU A 22
REMARK 465 ARG A 23
REMARK 465 TRP A 24
REMARK 465 LYS A 25
REMARK 465 HIS A 26
REMARK 465 THR A 27
REMARK 465 SER A 28
REMARK 465 SER A 29
REMARK 465 LEU A 30
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 GLN A 42 CG CD OE1 NE2
REMARK 470 LYS A 52 CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 58 CD CE NZ
REMARK 470 LYS A 99 CD CE NZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 130 CE NZ
REMARK 470 LYS A 175 CE NZ
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 GLU A 277 CD OE1 OE2
REMARK 470 GLN A 300 CG CD OE1 NE2
REMARK 470 ARG A 304 CD NE CZ NH1 NH2
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 ARG A 367 NE CZ NH1 NH2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 ARG A 374 CD NE CZ NH1 NH2
REMARK 470 GLU A 382 CG CD OE1 OE2
REMARK 470 LYS A 395 CD CE NZ
REMARK 470 LYS A 402 CE NZ
REMARK 470 LYS A 445 NZ
REMARK 470 LYS A 462 CD CE NZ
REMARK 470 ARG A 464 CD NE CZ NH1 NH2
REMARK 470 GLU A 465 CD OE1 OE2
REMARK 470 LYS A 468 CE NZ
REMARK 470 LYS A 487 CE NZ
REMARK 470 LYS A 552 CD CE NZ
REMARK 470 GLN A 563 CG CD OE1 NE2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 HIS B 26 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 28 OG
REMARK 470 GLN B 42 CD OE1 NE2
REMARK 470 LYS B 52 CD CE NZ
REMARK 470 LYS B 55 CD CE NZ
REMARK 470 LYS B 58 CD CE NZ
REMARK 470 LYS B 114 CE NZ
REMARK 470 LYS B 130 CD CE NZ
REMARK 470 GLU B 183 CD OE1 OE2
REMARK 470 ARG B 247 NE CZ NH1 NH2
REMARK 470 GLU B 277 CD OE1 OE2
REMARK 470 GLN B 300 CG CD OE1 NE2
REMARK 470 ARG B 304 CD NE CZ NH1 NH2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 LYS B 358 CE NZ
REMARK 470 ARG B 367 CD NE CZ NH1 NH2
REMARK 470 GLU B 370 CD OE1 OE2
REMARK 470 ARG B 374 CD NE CZ NH1 NH2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 GLU B 382 CG CD OE1 OE2
REMARK 470 LYS B 395 CG CD CE NZ
REMARK 470 LYS B 402 CE NZ
REMARK 470 ARG B 408 NE CZ NH1 NH2
REMARK 470 GLN B 440 CG CD OE1 NE2
REMARK 470 LYS B 445 CE NZ
REMARK 470 ARG B 464 NE CZ NH1 NH2
REMARK 470 GLN B 485 CD OE1 NE2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 GLN B 491 CD OE1 NE2
REMARK 470 ARG B 495 NE CZ NH1 NH2
REMARK 470 LYS B 552 CE NZ
REMARK 470 GLN B 563 CG CD OE1 NE2
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 86 80.58 -155.32
REMARK 500 ASP A 161 -78.90 -99.79
REMARK 500 ALA A 163 -80.31 -96.23
REMARK 500 PRO A 190 45.01 -99.85
REMARK 500 CYS A 315 -160.92 -118.59
REMARK 500 SER A 389 -163.56 -116.20
REMARK 500 LEU A 478 -80.51 -89.77
REMARK 500 ALA A 523 -137.92 -103.79
REMARK 500 ARG A 524 -134.24 46.78
REMARK 500 ASN B 86 76.55 -155.23
REMARK 500 ASP B 161 -76.83 -102.12
REMARK 500 ALA B 163 -78.96 -96.12
REMARK 500 PRO B 190 36.30 -98.42
REMARK 500 CYS B 315 -160.67 -121.23
REMARK 500 SER B 389 -163.80 -118.07
REMARK 500 LEU B 478 -78.75 -89.12
REMARK 500 ALA B 523 -139.14 -104.33
REMARK 500 ARG B 524 -135.40 48.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V9L RELATED DB: PDB
REMARK 900 RELATED ID: 3V9G RELATED DB: PDB
REMARK 900 RELATED ID: 3V9H RELATED DB: PDB
REMARK 900 RELATED ID: 3V9I RELATED DB: PDB
REMARK 900 RELATED ID: 3V9J RELATED DB: PDB
REMARK 900 RELATED ID: 3V9K RELATED DB: PDB
REMARK 900 RELATED ID: 4HL0 RELATED DB: PDB
REMARK 900 RELATED ID: 4LH1 RELATED DB: PDB
REMARK 900 RELATED ID: 4LH3 RELATED DB: PDB
REMARK 900 RELATED ID: 4LH2 RELATED DB: PDB
DBREF 4LGZ A 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
DBREF 4LGZ B 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
SEQADV 4LGZ MET A 1 UNP Q8CHT0 INITIATING METHIONINE
SEQADV 4LGZ GLY A 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER A 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER A 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER A 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER A 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ GLY A 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ LEU A 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ VAL A 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ PRO A 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ ARG A 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ GLY A 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER A 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS A 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ MET A 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ ALA A 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 4LGZ THR A 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 4LGZ LYS A 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQADV 4LGZ MET B 1 UNP Q8CHT0 INITIATING METHIONINE
SEQADV 4LGZ GLY B 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER B 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER B 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER B 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER B 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ GLY B 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ LEU B 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ VAL B 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ PRO B 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ ARG B 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ GLY B 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ SER B 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ HIS B 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ MET B 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4LGZ ALA B 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 4LGZ THR B 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 4LGZ LYS B 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQRES 1 A 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 A 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 A 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 A 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 A 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 A 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 A 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 A 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 A 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 A 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 A 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 A 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 A 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 A 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 A 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 A 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 A 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 A 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 A 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 A 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 A 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 A 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 A 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 A 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 A 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 A 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 A 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 A 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 A 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 A 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 A 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 A 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 A 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 A 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 A 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 A 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 A 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 A 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 A 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 A 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 A 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 A 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 A 563 SER TYR MET GLN
SEQRES 1 B 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 B 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 B 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 B 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 B 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 B 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 B 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 B 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 B 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 B 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 B 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 B 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 B 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 B 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 B 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 B 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 B 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 B 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 B 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 B 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 B 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 B 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 B 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 B 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 B 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 B 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 B 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 B 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 B 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 B 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 B 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 B 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 B 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 B 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 B 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 B 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 B 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 B 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 B 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 B 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 B 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 B 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 B 563 SER TYR MET GLN
HET ACY A 601 4
HET 1PE A 602 16
HET ACY A 603 4
HET ACY B 601 4
HET 1PE B 602 16
HET ACY B 603 4
HETNAM ACY ACETIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 ACY 4(C2 H4 O2)
FORMUL 4 1PE 2(C10 H22 O6)
FORMUL 9 HOH *660(H2 O)
HELIX 1 1 SER A 44 LYS A 58 1 15
HELIX 2 2 ASP A 98 LYS A 119 1 22
HELIX 3 3 PRO A 120 GLY A 137 1 18
HELIX 4 4 ARG A 139 GLY A 152 1 14
HELIX 5 5 THR A 154 ALA A 163 1 10
HELIX 6 6 ALA A 163 GLU A 181 1 19
HELIX 7 7 PHE A 212 MET A 226 1 15
HELIX 8 8 SER A 235 THR A 237 5 3
HELIX 9 9 ALA A 238 ALA A 252 1 15
HELIX 10 10 ASP A 265 SER A 275 1 11
HELIX 11 11 SER A 287 ASN A 301 1 15
HELIX 12 12 ASP A 328 GLU A 342 1 15
HELIX 13 13 TYR A 343 GLN A 346 5 4
HELIX 14 14 LEU A 360 ILE A 375 1 16
HELIX 15 15 ASP A 393 SER A 410 1 18
HELIX 16 16 GLU A 441 LYS A 445 5 5
HELIX 17 17 PRO A 459 ASP A 461 5 3
HELIX 18 18 LYS A 462 THR A 473 1 12
HELIX 19 19 ASP A 486 LEU A 497 1 12
HELIX 20 20 HIS A 536 ARG A 540 5 5
HELIX 21 21 TYR A 559 GLN A 563 5 5
HELIX 22 22 SER B 44 ASP B 56 1 13
HELIX 23 23 ASP B 98 LYS B 119 1 22
HELIX 24 24 PRO B 120 GLY B 137 1 18
HELIX 25 25 ARG B 139 GLY B 152 1 14
HELIX 26 26 THR B 154 ALA B 162 1 9
HELIX 27 27 ALA B 163 GLU B 181 1 19
HELIX 28 28 PHE B 212 MET B 226 1 15
HELIX 29 29 SER B 235 THR B 237 5 3
HELIX 30 30 ALA B 238 ALA B 252 1 15
HELIX 31 31 ASP B 265 SER B 275 1 11
HELIX 32 32 SER B 287 ASN B 301 1 15
HELIX 33 33 LEU B 302 PHE B 305 5 4
HELIX 34 34 ASP B 328 GLU B 342 1 15
HELIX 35 35 TYR B 343 GLN B 346 5 4
HELIX 36 36 LEU B 360 SER B 373 1 14
HELIX 37 37 ASP B 393 SER B 410 1 18
HELIX 38 38 GLU B 441 LYS B 445 5 5
HELIX 39 39 PRO B 459 ASP B 461 5 3
HELIX 40 40 LYS B 462 THR B 473 1 12
HELIX 41 41 ASP B 486 LEU B 497 1 12
HELIX 42 42 HIS B 536 ARG B 540 5 5
HELIX 43 43 TYR B 559 GLN B 563 5 5
SHEET 1 A 3 GLU A 62 ALA A 63 0
SHEET 2 A 3 ASN A 86 CYS A 95 1 O LYS A 93 N GLU A 62
SHEET 3 A 3 ILE A 78 SER A 83 -1 N GLN A 79 O PHE A 94
SHEET 1 B 2 CYS A 66 VAL A 68 0
SHEET 2 B 2 GLU A 71 VAL A 73 -1 O VAL A 73 N CYS A 66
SHEET 1 C 9 SER A 191 GLY A 199 0
SHEET 2 C 9 THR A 542 THR A 550 -1 O GLN A 545 N VAL A 196
SHEET 3 C 9 ASN B 503 ILE B 506 1 O ILE B 506 N LYS A 548
SHEET 4 C 9 THR B 479 PHE B 483 1 N VAL B 482 O TYR B 505
SHEET 5 C 9 ASN B 319 VAL B 323 1 N PHE B 322 O ALA B 481
SHEET 6 C 9 CYS B 351 PRO B 357 1 O TYR B 355 N VAL B 323
SHEET 7 C 9 VAL B 452 TYR B 458 1 O TYR B 456 N LEU B 354
SHEET 8 C 9 CYS B 432 SER B 436 1 N ILE B 434 O VAL B 455
SHEET 9 C 9 LEU B 413 ALA B 417 -1 N SER B 414 O GLU B 435
SHEET 1 D 5 ILE A 259 PHE A 261 0
SHEET 2 D 5 VAL A 229 LYS A 233 1 N VAL A 230 O GLN A 260
SHEET 3 D 5 PHE A 203 ILE A 207 1 N ALA A 206 O LEU A 231
SHEET 4 D 5 LEU A 279 THR A 285 1 O CYS A 280 N PHE A 203
SHEET 5 D 5 ARG A 310 GLU A 314 1 O ALA A 312 N PHE A 284
SHEET 1 E 9 LEU A 413 ALA A 417 0
SHEET 2 E 9 CYS A 432 SER A 436 -1 O ILE A 433 N LEU A 416
SHEET 3 E 9 VAL A 452 TYR A 458 1 O LEU A 453 N ILE A 434
SHEET 4 E 9 CYS A 351 PRO A 357 1 N LEU A 354 O TYR A 456
SHEET 5 E 9 ASN A 319 VAL A 323 1 N VAL A 323 O TYR A 355
SHEET 6 E 9 THR A 479 PHE A 483 1 O ALA A 481 N PHE A 322
SHEET 7 E 9 ASN A 503 ILE A 506 1 O TYR A 505 N VAL A 482
SHEET 8 E 9 THR B 542 THR B 550 1 O LYS B 548 N ILE A 506
SHEET 9 E 9 SER B 191 GLY B 199 -1 N VAL B 196 O GLN B 545
SHEET 1 F 2 CYS A 421 ASN A 422 0
SHEET 2 F 2 TYR A 428 VAL A 429 -1 O TYR A 428 N ASN A 422
SHEET 1 G 2 TYR A 476 GLY A 477 0
SHEET 2 G 2 ALA A 523 ARG A 524 -1 N ALA A 523 O GLY A 477
SHEET 1 H 3 GLU B 62 ILE B 64 0
SHEET 2 H 3 ASN B 86 CYS B 95 1 O LYS B 93 N ILE B 64
SHEET 3 H 3 ILE B 78 SER B 83 -1 N GLN B 79 O PHE B 94
SHEET 1 I 2 CYS B 66 VAL B 68 0
SHEET 2 I 2 GLU B 71 VAL B 73 -1 O VAL B 73 N CYS B 66
SHEET 1 J 5 ILE B 259 PHE B 261 0
SHEET 2 J 5 VAL B 229 LYS B 233 1 N VAL B 230 O GLN B 260
SHEET 3 J 5 PHE B 203 ILE B 207 1 N ALA B 206 O LYS B 233
SHEET 4 J 5 LEU B 279 THR B 285 1 O ASN B 283 N ALA B 205
SHEET 5 J 5 ARG B 310 GLU B 314 1 O ALA B 312 N PHE B 284
SHEET 1 K 2 CYS B 421 ASN B 422 0
SHEET 2 K 2 TYR B 428 VAL B 429 -1 O TYR B 428 N ASN B 422
SHEET 1 L 2 TYR B 476 GLY B 477 0
SHEET 2 L 2 ALA B 523 ARG B 524 -1 O ALA B 523 N GLY B 477
CISPEP 1 PRO A 189 PRO A 190 0 2.06
CISPEP 2 PRO B 189 PRO B 190 0 5.77
SITE 1 AC1 6 SER A 349 GLY A 512 SER A 513 PHE A 520
SITE 2 AC1 6 HOH A 982 HOH A 984
SITE 1 AC2 7 ALA A 63 TRP A 74 TYR A 80 LYS A 93
SITE 2 AC2 7 THR B 61 HOH B 708 HOH B1000
SITE 1 AC3 6 PRO A 519 HIS A 536 HOH A 841 HOH A 855
SITE 2 AC3 6 HOH A1013 TYR B 197
SITE 1 AC4 6 SER B 349 GLY B 512 SER B 513 PHE B 520
SITE 2 AC4 6 HOH B 976 HOH B 977
SITE 1 AC5 7 THR A 61 HOH A 878 THR B 61 ALA B 63
SITE 2 AC5 7 TRP B 74 TYR B 80 LYS B 93
SITE 1 AC6 6 TYR A 197 HOH A 921 PRO B 519 HIS B 536
SITE 2 AC6 6 HOH B 849 HOH B 851
CRYST1 84.938 93.880 132.150 90.00 90.00 90.00 P 21 21 21 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 0.011773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007567 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
