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HEADER HYDROLASE 04-MAR-13 3ZPX
TITLE USTILAGO MAYDIS LIPASE UM03410, SHORT FORM WITHOUT FLAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SHORT PROTEIN FORM, RESIDUES 152-582;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: USTILAGO MAYDIS;
SOURCE 3 ORGANISM_TAXID: 5270;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS HYDROLASE, ALPHA BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.PALM,W.HINRICHS
REVDAT 1 19-MAR-14 3ZPX 0
JRNL AUTH H.BRUNDIEK,G.J.PALM,U.T.BORNSCHEUER,W.HINRICHS
JRNL TITL LIPASE FROM USTILAGO
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.BRUNDIEK,S.SASS,A.EVITT,R.KOURIST,U.T.BORNSCHEUER
REMARK 1 TITL THE SHORT FORM OF THE RECOMBINANT CAL-A-TYPE LIPASE UM03410
REMARK 1 TITL 2 FROM THE SMUT FUNGUS USTILAGO MAYDIS EXHIBITS AN INHERENT
REMARK 1 TITL 3 TRANS-FATTY ACID SELECTIVITY.
REMARK 1 REF APPL.MICROBIOL.BIOTECHNOL. V. 94 141 2012
REMARK 1 REFN ISSN 0175-7598
REMARK 1 PMID 22294433
REMARK 1 DOI 10.1007/S00253-012-3903-9
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.62
REMARK 3 NUMBER OF REFLECTIONS : 45105
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.18539
REMARK 3 R VALUE (WORKING SET) : 0.18283
REMARK 3 FREE R VALUE : 0.23469
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2373
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.989
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.040
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2829
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.253
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.302
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.209
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.40
REMARK 3 B22 (A**2) : 1.06
REMARK 3 B33 (A**2) : 0.33
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.545
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6162 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5703 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8404 ; 1.241 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13131 ; 0.774 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 780 ; 5.786 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;32.728 ;24.910
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 921 ;14.196 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;13.909 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 908 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7152 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1444 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 395
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9910 19.2500 -30.4670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0411 T22: 0.0918
REMARK 3 T33: 0.0058 T12: 0.0206
REMARK 3 T13: 0.0107 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.0249 L22: 1.0202
REMARK 3 L33: 0.8502 L12: -0.1599
REMARK 3 L13: 0.2243 L23: -0.3982
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: 0.1130 S13: 0.0214
REMARK 3 S21: 0.1132 S22: -0.0359 S23: 0.0285
REMARK 3 S31: -0.0157 S32: 0.1690 S33: 0.0186
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 14 B 395
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9610 -2.2770 -1.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0597 T22: 0.0179
REMARK 3 T33: 0.0175 T12: 0.0054
REMARK 3 T13: -0.0178 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.7732 L22: 0.4597
REMARK 3 L33: 1.6097 L12: -0.0398
REMARK 3 L13: 0.3167 L23: -0.0800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: -0.0624 S13: -0.0004
REMARK 3 S21: 0.0449 S22: -0.0259 S23: 0.0034
REMARK 3 S31: -0.2001 S32: -0.0401 S33: 0.0834
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES WITH TLS ADDED. OVERALL
REMARK 3 WEIGHTING TERM 0.1. B-FACTOR WEIGHT 0.5.
REMARK 4
REMARK 4 3ZPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAR-13.
REMARK 100 THE PDBE ID CODE IS EBI-56027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.99
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.0
REMARK 200 R MERGE FOR SHELL (I) : 0.51
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3GUU
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 100 MM NAOAC PH
REMARK 280 4.5, 200 MM LI2SO4. CRYO SOLUTION: 20% PEG 8000, 20% PEG
REMARK 280 400
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 27.37650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.57900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.57900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.37650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.07500
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: 2670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.6 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 ALA A 11
REMARK 465 ALA A 12
REMARK 465 PHE A 13
REMARK 465 GLY A 397
REMARK 465 ALA A 398
REMARK 465 GLN A 399
REMARK 465 SER A 400
REMARK 465 VAL A 401
REMARK 465 MET A 402
REMARK 465 GLY A 403
REMARK 465 ALA A 404
REMARK 465 SER A 405
REMARK 465 GLY A 406
REMARK 465 PRO A 407
REMARK 465 PRO A 408
REMARK 465 ALA A 409
REMARK 465 GLN A 410
REMARK 465 ASP A 411
REMARK 465 VAL A 412
REMARK 465 LEU A 413
REMARK 465 GLY A 414
REMARK 465 ALA A 415
REMARK 465 ASP A 416
REMARK 465 LEU A 417
REMARK 465 ALA A 418
REMARK 465 SER A 419
REMARK 465 GLN A 420
REMARK 465 LEU A 421
REMARK 465 ARG A 422
REMARK 465 SER A 423
REMARK 465 LEU A 424
REMARK 465 GLN A 425
REMARK 465 GLY A 426
REMARK 465 LYS A 427
REMARK 465 PRO A 428
REMARK 465 SER A 429
REMARK 465 ALA A 430
REMARK 465 PHE A 431
REMARK 465 GLY A 432
REMARK 465 ASN A 433
REMARK 465 LYS A 434
REMARK 465 PRO A 435
REMARK 465 PHE A 436
REMARK 465 GLY A 437
REMARK 465 SER A 438
REMARK 465 ILE A 439
REMARK 465 SER A 440
REMARK 465 PRO A 441
REMARK 465 ALA A 442
REMARK 465 ALA A 443
REMARK 465 ALA A 444
REMARK 465 SER A 445
REMARK 465 PHE A 446
REMARK 465 LEU A 447
REMARK 465 GLU A 448
REMARK 465 GLN A 449
REMARK 465 LYS A 450
REMARK 465 LEU A 451
REMARK 465 ILE A 452
REMARK 465 SER A 453
REMARK 465 GLU A 454
REMARK 465 GLU A 455
REMARK 465 ASP A 456
REMARK 465 LEU A 457
REMARK 465 ASN A 458
REMARK 465 SER A 459
REMARK 465 ALA A 460
REMARK 465 VAL A 461
REMARK 465 ASP A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
REMARK 465 HIS A 465
REMARK 465 HIS A 466
REMARK 465 HIS A 467
REMARK 465 HIS A 468
REMARK 465 ALA B 11
REMARK 465 ALA B 12
REMARK 465 PHE B 13
REMARK 465 GLY B 397
REMARK 465 ALA B 398
REMARK 465 GLN B 399
REMARK 465 SER B 400
REMARK 465 VAL B 401
REMARK 465 MET B 402
REMARK 465 GLY B 403
REMARK 465 ALA B 404
REMARK 465 SER B 405
REMARK 465 GLY B 406
REMARK 465 PRO B 407
REMARK 465 PRO B 408
REMARK 465 ALA B 409
REMARK 465 GLN B 410
REMARK 465 ASP B 411
REMARK 465 VAL B 412
REMARK 465 LEU B 413
REMARK 465 GLY B 414
REMARK 465 ALA B 415
REMARK 465 ASP B 416
REMARK 465 LEU B 417
REMARK 465 ALA B 418
REMARK 465 SER B 419
REMARK 465 GLN B 420
REMARK 465 LEU B 421
REMARK 465 ARG B 422
REMARK 465 SER B 423
REMARK 465 LEU B 424
REMARK 465 GLN B 425
REMARK 465 GLY B 426
REMARK 465 LYS B 427
REMARK 465 PRO B 428
REMARK 465 SER B 429
REMARK 465 ALA B 430
REMARK 465 PHE B 431
REMARK 465 GLY B 432
REMARK 465 ASN B 433
REMARK 465 LYS B 434
REMARK 465 PRO B 435
REMARK 465 PHE B 436
REMARK 465 GLY B 437
REMARK 465 SER B 438
REMARK 465 ILE B 439
REMARK 465 SER B 440
REMARK 465 PRO B 441
REMARK 465 ALA B 442
REMARK 465 ALA B 443
REMARK 465 ALA B 444
REMARK 465 SER B 445
REMARK 465 PHE B 446
REMARK 465 LEU B 447
REMARK 465 GLU B 448
REMARK 465 GLN B 449
REMARK 465 LYS B 450
REMARK 465 LEU B 451
REMARK 465 ILE B 452
REMARK 465 SER B 453
REMARK 465 GLU B 454
REMARK 465 GLU B 455
REMARK 465 ASP B 456
REMARK 465 LEU B 457
REMARK 465 ASN B 458
REMARK 465 SER B 459
REMARK 465 ALA B 460
REMARK 465 VAL B 461
REMARK 465 ASP B 462
REMARK 465 HIS B 463
REMARK 465 HIS B 464
REMARK 465 HIS B 465
REMARK 465 HIS B 466
REMARK 465 HIS B 467
REMARK 465 HIS B 468
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 GLY A 396 CA C O
REMARK 470 GLY B 396 CA C O
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 ND2 ASN A 291 O HOH A 2127 2.16
REMARK 500 O HOH A 2052 O HOH A 2089 2.14
REMARK 500 O HOH B 2052 O HOH B 2080 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 111 -47.80 -15.20
REMARK 500 ASP A 112 41.62 -83.75
REMARK 500 LEU A 121 -83.97 -99.46
REMARK 500 SER A 184 -115.09 64.23
REMARK 500 LYS A 227 -6.10 67.34
REMARK 500 CYS A 273 -157.14 -119.95
REMARK 500 GLU A 308 41.16 -95.48
REMARK 500 LEU A 333 40.90 -101.25
REMARK 500 ILE A 336 -53.25 -121.48
REMARK 500 GLU A 365 -166.77 -108.53
REMARK 500 ASP B 112 34.46 -78.08
REMARK 500 LEU B 121 -81.19 -101.78
REMARK 500 SER B 184 -119.29 62.92
REMARK 500 LYS B 227 -2.53 74.47
REMARK 500 CYS B 273 -156.09 -114.52
REMARK 500 ASP B 292 85.59 173.96
REMARK 500 GLU B 308 43.09 -101.88
REMARK 500 GLU B 365 -166.20 -108.89
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 PEG A1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1402
DBREF 3ZPX A 11 441 UNP Q4P903 Q4P903_USTMA 152 582
DBREF 3ZPX B 11 441 UNP Q4P903 Q4P903_USTMA 152 582
SEQADV 3ZPX ALA A 442 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA A 443 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA A 444 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER A 445 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX PHE A 446 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU A 447 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU A 448 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLN A 449 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LYS A 450 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU A 451 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ILE A 452 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER A 453 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU A 454 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU A 455 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASP A 456 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU A 457 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASN A 458 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER A 459 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA A 460 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX VAL A 461 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASP A 462 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 463 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 464 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 465 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 466 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 467 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS A 468 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA B 442 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA B 443 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA B 444 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER B 445 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX PHE B 446 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU B 447 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU B 448 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLN B 449 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LYS B 450 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU B 451 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ILE B 452 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER B 453 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU B 454 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX GLU B 455 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASP B 456 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX LEU B 457 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASN B 458 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX SER B 459 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ALA B 460 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX VAL B 461 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX ASP B 462 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 463 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 464 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 465 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 466 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 467 UNP Q4P903 EXPRESSION TAG
SEQADV 3ZPX HIS B 468 UNP Q4P903 EXPRESSION TAG
SEQRES 1 A 458 ALA ALA PHE ALA ASP PRO ASN ASP ASP LEU PHE TYR THR
SEQRES 2 A 458 THR PRO ASP ASN ILE ASN THR TYR ALA ASN GLY GLN VAL
SEQRES 3 A 458 ILE GLN SER ARG LYS ALA ASP THR ASP ILE GLY ASN SER
SEQRES 4 A 458 ASN LYS VAL GLU ALA PHE GLN LEU GLN TYR ARG THR THR
SEQRES 5 A 458 ASN THR GLN LYS GLU ALA GLN ALA ASN VAL ALA THR VAL
SEQRES 6 A 458 TRP ILE PRO ASN LYS PRO ALA SER PRO PRO LYS ILE PHE
SEQRES 7 A 458 SER TYR GLN VAL TYR GLN ASP SER THR GLN LEU ASN CYS
SEQRES 8 A 458 ALA PRO SER TYR SER PHE LEU LYS GLY LEU ASP LYS PRO
SEQRES 9 A 458 ASN LYS ALA THR THR ILE LEU GLU ALA PRO ILE ILE ILE
SEQRES 10 A 458 GLY TRP ALA LEU GLN GLN GLY PHE TYR VAL VAL SER SER
SEQRES 11 A 458 ASP HIS GLU GLY PRO ARG SER SER PHE ILE ALA GLY TYR
SEQRES 12 A 458 GLU GLU GLY MET ALA ILE LEU ASP GLY ILE ARG ALA LEU
SEQRES 13 A 458 LYS ASN TYR ALA LYS LEU PRO THR ASP SER ALA ILE GLY
SEQRES 14 A 458 PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY TRP
SEQRES 15 A 458 ALA ALA ASN LEU ALA GLY SER TYR ALA PRO GLU HIS ASN
SEQRES 16 A 458 ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER ALA
SEQRES 17 A 458 ARG ASP THR PHE ASN PHE LEU ASN LYS GLY ALA PHE ALA
SEQRES 18 A 458 GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA LEU ALA
SEQRES 19 A 458 TYR PRO ASP VAL GLU THR TYR ILE GLN SER ARG LEU ASN
SEQRES 20 A 458 ALA LYS GLY GLU LYS VAL PHE LYS GLN VAL ARG SER ARG
SEQRES 21 A 458 GLY PHE CYS ILE GLY GLN VAL VAL LEU THR TYR PRO PHE
SEQRES 22 A 458 VAL ASP ALA TYR SER LEU ILE ASN ASP THR ASN LEU LEU
SEQRES 23 A 458 ASN GLU GLU PRO VAL ALA SER THR LEU LYS SER GLU THR
SEQRES 24 A 458 LEU VAL GLN ALA GLU ALA SER TYR THR VAL PRO VAL PRO
SEQRES 25 A 458 LYS PHE PRO ARG PHE ILE TRP HIS ALA LEU LEU ASP GLU
SEQRES 26 A 458 ILE VAL PRO PHE HIS SER ALA ALA THR TYR VAL LYS GLU
SEQRES 27 A 458 GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN VAL TYR
SEQRES 28 A 458 SER PHE ALA GLU HIS ILE SER ALA GLU LEU PHE GLY LEU
SEQRES 29 A 458 LEU PRO GLY LEU ASP TRP LEU ASN LYS ALA TYR LYS GLY
SEQRES 30 A 458 GLN ALA PRO LYS VAL PRO CYS GLY GLY GLY ALA GLN SER
SEQRES 31 A 458 VAL MET GLY ALA SER GLY PRO PRO ALA GLN ASP VAL LEU
SEQRES 32 A 458 GLY ALA ASP LEU ALA SER GLN LEU ARG SER LEU GLN GLY
SEQRES 33 A 458 LYS PRO SER ALA PHE GLY ASN LYS PRO PHE GLY SER ILE
SEQRES 34 A 458 SER PRO ALA ALA ALA SER PHE LEU GLU GLN LYS LEU ILE
SEQRES 35 A 458 SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS
SEQRES 36 A 458 HIS HIS HIS
SEQRES 1 B 458 ALA ALA PHE ALA ASP PRO ASN ASP ASP LEU PHE TYR THR
SEQRES 2 B 458 THR PRO ASP ASN ILE ASN THR TYR ALA ASN GLY GLN VAL
SEQRES 3 B 458 ILE GLN SER ARG LYS ALA ASP THR ASP ILE GLY ASN SER
SEQRES 4 B 458 ASN LYS VAL GLU ALA PHE GLN LEU GLN TYR ARG THR THR
SEQRES 5 B 458 ASN THR GLN LYS GLU ALA GLN ALA ASN VAL ALA THR VAL
SEQRES 6 B 458 TRP ILE PRO ASN LYS PRO ALA SER PRO PRO LYS ILE PHE
SEQRES 7 B 458 SER TYR GLN VAL TYR GLN ASP SER THR GLN LEU ASN CYS
SEQRES 8 B 458 ALA PRO SER TYR SER PHE LEU LYS GLY LEU ASP LYS PRO
SEQRES 9 B 458 ASN LYS ALA THR THR ILE LEU GLU ALA PRO ILE ILE ILE
SEQRES 10 B 458 GLY TRP ALA LEU GLN GLN GLY PHE TYR VAL VAL SER SER
SEQRES 11 B 458 ASP HIS GLU GLY PRO ARG SER SER PHE ILE ALA GLY TYR
SEQRES 12 B 458 GLU GLU GLY MET ALA ILE LEU ASP GLY ILE ARG ALA LEU
SEQRES 13 B 458 LYS ASN TYR ALA LYS LEU PRO THR ASP SER ALA ILE GLY
SEQRES 14 B 458 PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY TRP
SEQRES 15 B 458 ALA ALA ASN LEU ALA GLY SER TYR ALA PRO GLU HIS ASN
SEQRES 16 B 458 ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER ALA
SEQRES 17 B 458 ARG ASP THR PHE ASN PHE LEU ASN LYS GLY ALA PHE ALA
SEQRES 18 B 458 GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA LEU ALA
SEQRES 19 B 458 TYR PRO ASP VAL GLU THR TYR ILE GLN SER ARG LEU ASN
SEQRES 20 B 458 ALA LYS GLY GLU LYS VAL PHE LYS GLN VAL ARG SER ARG
SEQRES 21 B 458 GLY PHE CYS ILE GLY GLN VAL VAL LEU THR TYR PRO PHE
SEQRES 22 B 458 VAL ASP ALA TYR SER LEU ILE ASN ASP THR ASN LEU LEU
SEQRES 23 B 458 ASN GLU GLU PRO VAL ALA SER THR LEU LYS SER GLU THR
SEQRES 24 B 458 LEU VAL GLN ALA GLU ALA SER TYR THR VAL PRO VAL PRO
SEQRES 25 B 458 LYS PHE PRO ARG PHE ILE TRP HIS ALA LEU LEU ASP GLU
SEQRES 26 B 458 ILE VAL PRO PHE HIS SER ALA ALA THR TYR VAL LYS GLU
SEQRES 27 B 458 GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN VAL TYR
SEQRES 28 B 458 SER PHE ALA GLU HIS ILE SER ALA GLU LEU PHE GLY LEU
SEQRES 29 B 458 LEU PRO GLY LEU ASP TRP LEU ASN LYS ALA TYR LYS GLY
SEQRES 30 B 458 GLN ALA PRO LYS VAL PRO CYS GLY GLY GLY ALA GLN SER
SEQRES 31 B 458 VAL MET GLY ALA SER GLY PRO PRO ALA GLN ASP VAL LEU
SEQRES 32 B 458 GLY ALA ASP LEU ALA SER GLN LEU ARG SER LEU GLN GLY
SEQRES 33 B 458 LYS PRO SER ALA PHE GLY ASN LYS PRO PHE GLY SER ILE
SEQRES 34 B 458 SER PRO ALA ALA ALA SER PHE LEU GLU GLN LYS LEU ILE
SEQRES 35 B 458 SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS
SEQRES 36 B 458 HIS HIS HIS
HET PEG A1401 7
HET EDO A1402 4
HET EDO B1401 4
HET PG4 B1402 13
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 HOH *319(H2 O)
HELIX 1 1 ASP A 15 ASP A 19 5 5
HELIX 2 2 ASP A 19 THR A 23 5 5
HELIX 3 3 ASN A 27 TYR A 31 5 5
HELIX 4 4 THR A 44 LYS A 51 1 8
HELIX 5 5 GLN A 98 CYS A 101 5 4
HELIX 6 6 ALA A 102 PHE A 107 1 6
HELIX 7 7 ASN A 115 ILE A 120 5 6
HELIX 8 8 LEU A 121 GLN A 133 1 13
HELIX 9 9 ALA A 151 ALA A 170 1 20
HELIX 10 10 SER A 184 ALA A 201 1 18
HELIX 11 11 SER A 217 ASN A 226 1 10
HELIX 12 12 PHE A 230 TYR A 245 1 16
HELIX 13 13 TYR A 245 LEU A 256 1 12
HELIX 14 14 ASN A 257 ARG A 268 1 12
HELIX 15 15 CYS A 273 TYR A 281 1 9
HELIX 16 16 ASP A 285 LEU A 289 5 5
HELIX 17 17 ASN A 294 GLU A 298 5 5
HELIX 18 18 PRO A 300 GLU A 308 1 9
HELIX 19 19 PRO A 338 LYS A 352 1 15
HELIX 20 20 GLU A 365 LYS A 386 1 22
HELIX 21 21 ASP B 15 ASP B 19 5 5
HELIX 22 22 ASP B 19 THR B 23 5 5
HELIX 23 23 ASN B 27 TYR B 31 5 5
HELIX 24 24 THR B 44 LYS B 51 1 8
HELIX 25 25 GLN B 98 CYS B 101 5 4
HELIX 26 26 ALA B 102 LEU B 108 1 7
HELIX 27 27 ASN B 115 THR B 119 5 5
HELIX 28 28 GLU B 122 GLN B 133 1 12
HELIX 29 29 ALA B 151 ALA B 170 1 20
HELIX 30 30 SER B 184 ALA B 201 1 18
HELIX 31 31 SER B 217 ASN B 226 1 10
HELIX 32 32 PHE B 230 TYR B 245 1 16
HELIX 33 33 TYR B 245 LEU B 256 1 12
HELIX 34 34 ASN B 257 ARG B 268 1 12
HELIX 35 35 CYS B 273 TYR B 281 1 9
HELIX 36 36 ASP B 285 LEU B 289 5 5
HELIX 37 37 ASN B 294 GLU B 298 5 5
HELIX 38 38 PRO B 300 GLU B 308 1 9
HELIX 39 39 VAL B 311 ALA B 315 5 5
HELIX 40 40 PRO B 338 LYS B 352 1 15
HELIX 41 41 GLU B 365 LYS B 386 1 22
SHEET 1 AA 9 VAL A 36 LYS A 41 0
SHEET 2 AA 9 GLU A 53 THR A 62 -1 O GLN A 56 N ARG A 40
SHEET 3 AA 9 ALA A 68 ILE A 77 -1 O GLN A 69 N THR A 61
SHEET 4 AA 9 TYR A 136 SER A 140 -1 O VAL A 137 N TRP A 76
SHEET 5 AA 9 LYS A 86 GLN A 91 1 O LYS A 86 N TYR A 136
SHEET 6 AA 9 ALA A 177 TYR A 183 1 O ALA A 177 N ILE A 87
SHEET 7 AA 9 ASN A 205 GLY A 212 1 O ASN A 205 N ILE A 178
SHEET 8 AA 9 ARG A 326 ALA A 331 1 O PHE A 327 N TYR A 211
SHEET 9 AA 9 ILE A 356 TYR A 361 1 O ASN A 357 N ILE A 328
SHEET 1 BA 9 VAL B 36 LYS B 41 0
SHEET 2 BA 9 GLU B 53 THR B 62 -1 O GLN B 56 N ARG B 40
SHEET 3 BA 9 ALA B 68 ILE B 77 -1 O GLN B 69 N THR B 61
SHEET 4 BA 9 TYR B 136 SER B 140 -1 O VAL B 137 N TRP B 76
SHEET 5 BA 9 LYS B 86 GLN B 91 1 O LYS B 86 N TYR B 136
SHEET 6 BA 9 ALA B 177 TYR B 183 1 O ALA B 177 N ILE B 87
SHEET 7 BA 9 ASN B 205 GLY B 212 1 O ASN B 205 N ILE B 178
SHEET 8 BA 9 PRO B 325 ALA B 331 1 O PRO B 325 N ALA B 209
SHEET 9 BA 9 ASP B 355 TYR B 361 1 O ASP B 355 N ARG B 326
SSBOND 1 CYS A 101 CYS A 273 1555 1555 2.04
SSBOND 2 CYS A 350 CYS A 394 1555 1555 2.04
SSBOND 3 CYS B 101 CYS B 273 1555 1555 2.04
SSBOND 4 CYS B 350 CYS B 394 1555 1555 2.03
CISPEP 1 SER A 83 PRO A 84 0 -1.85
CISPEP 2 GLU A 299 PRO A 300 0 1.09
CISPEP 3 SER B 83 PRO B 84 0 -5.96
CISPEP 4 GLU B 299 PRO B 300 0 6.16
SITE 1 AC1 5 ASN A 257 ALA A 258 ASN A 291 ASP A 379
SITE 2 AC1 5 HOH A2161
SITE 1 AC2 4 PRO A 320 PRO A 322 HOH A2092 HIS B 340
SITE 1 AC3 2 TRP B 358 VAL B 360
SITE 1 AC4 6 GLU B 299 LYS B 306 ALA B 313 ALA B 315
SITE 2 AC4 6 SER B 316 GLY B 353
CRYST1 54.753 100.150 129.158 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 0.018264 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007742 0.00000
MTRIX1 1 -0.999930 0.002710 0.011420 -3.02917 1
MTRIX2 1 0.011710 0.294740 0.955510 21.74548 1
MTRIX3 1 -0.000770 0.955570 -0.294750 -28.94955 1
TER 2957 GLY A 396
TER 5969 GLY B 396
MASTER 511 0 4 41 18 0 6 9 6314 2 36 72
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